PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 33992625-15 2021 Immunfluorescent staining and Western blot analysis showed increased MMP-2, -9 and caspase-3 in the UVB only group compared with the UVB/citicoline group. Cytidine Diphosphate Choline 137-147 matrix metallopeptidase 2 Rattus norvegicus 69-78 3656358-1 1987 C1- and C3-methyl-substituted derivatives of the potent dopamine (DA) receptor agonist 7-hydroxy-2-(di-n-propylamino)tetralin (7-OH-DPAT) have been synthesized, and their conformational preferences have been studied by use of NMR spectroscopy, X-ray crystallography, and molecular mechanics (MMP2) calculations. 7-hydroxy-2-N,N-dipropylaminotetralin 87-125 matrix metallopeptidase 2 Rattus norvegicus 292-296 3599021-1 1987 C3-Methyl-substituted derivatives of the potent dopamine (DA) receptor agonist 5-hydroxy-2-(di-n-propylamino)tetralin (5-OH-DPAT) have been synthesized and their conformational preferences have been studied by use of NMR spectroscopy, X-ray crystallography, and molecular mechanics calculations (MMP2). 5-hydroxy-2-N,N-dipropylaminotetralin 79-117 matrix metallopeptidase 2 Rattus norvegicus 296-300 33746002-10 2021 Besides, SN induced the expression of apoptotic proteins including Bax and Cleaved Caspase-3, downregulated anti-apoptotic protein Bcl-2, and decreased the level of migratory proteins MMP-2 and MMP-9. Tin 9-11 matrix metallopeptidase 2 Rattus norvegicus 184-189 32638240-17 2021 Increases in MMP-2 were found in the H and H + PBM groups compared to the control group at both 7 and 14 days. pbm 47-50 matrix metallopeptidase 2 Rattus norvegicus 13-18 33216283-9 2021 Proinflammatory cytokines (IL-1beta and TNF-alpha) and metalloproteinase-2 and 9 (MMP-2/9) were increased by cisplatin treatment. Cisplatin 109-118 matrix metallopeptidase 2 Rattus norvegicus 82-89 33216283-13 2021 Mesna partially alleviated redox imbalance, reduced the proinflammatory cytokines, and MMP-2/9 levels. Mesna 0-5 matrix metallopeptidase 2 Rattus norvegicus 87-94 34058185-2 2021 We examined whether the PPI omeprazole promotes vascular oxidative stress mediated by xanthine oxidoreductase (XOR) leading to activation of matrix metalloproteinases (MMPs) and vascular remodeling. Omeprazole 28-38 matrix metallopeptidase 2 Rattus norvegicus 168-172 34058185-7 2021 Omeprazole increased vascular active MMP-2 expression and activity assessed by gel zymography and in situ zymography, respectively (P<0.05). Omeprazole 0-10 matrix metallopeptidase 2 Rattus norvegicus 37-42 34058185-11 2021 Our results suggest that the long-term use of omeprazole induces vascular dysfunction and remodeling by promoting XOR-derived reactive oxygen species formation and MMP activation. Omeprazole 46-56 matrix metallopeptidase 2 Rattus norvegicus 164-167 33443645-11 2021 Thirdly, febuxostat alleviated MPP+-induced inflammatory responses in astrocytes by reducing the expressions of IL-8, IL-1beta, TNF-alpha, GFAP, MMP-2, and MMP-9. Febuxostat 9-19 matrix metallopeptidase 2 Rattus norvegicus 145-150 33443645-11 2021 Thirdly, febuxostat alleviated MPP+-induced inflammatory responses in astrocytes by reducing the expressions of IL-8, IL-1beta, TNF-alpha, GFAP, MMP-2, and MMP-9. mangion-purified polysaccharide (Candida albicans) 31-35 matrix metallopeptidase 2 Rattus norvegicus 145-150 34024143-11 2021 Renal damage, TIMP-1, IL-33, and MMP-2 increased after CKF induction, while COX 1, MMP-9, and MMP-13 levels were significantly reduced. ckf 55-58 matrix metallopeptidase 2 Rattus norvegicus 33-38 33579535-10 2021 Moreover, heroin-paired cues increased tissue inhibitor of metalloproteinases TIMP-1,2, which caused transient inhibition of MMP-2 activity around D2-MSNs during cue-induced heroin seeking. Heroin 10-16 matrix metallopeptidase 2 Rattus norvegicus 125-130 33579535-10 2021 Moreover, heroin-paired cues increased tissue inhibitor of metalloproteinases TIMP-1,2, which caused transient inhibition of MMP-2 activity around D2-MSNs during cue-induced heroin seeking. Heroin 174-180 matrix metallopeptidase 2 Rattus norvegicus 125-130 33579535-11 2021 CONCLUSIONS: The differential regulation of heroin seeking and extinguished seeking by different MMP subtypes on distinct cell populations poses MMP-2,9 activity as an important mediator and contributor in heroin-induced cell-specific synaptic plasticity. Heroin 44-50 matrix metallopeptidase 2 Rattus norvegicus 145-150 33579535-11 2021 CONCLUSIONS: The differential regulation of heroin seeking and extinguished seeking by different MMP subtypes on distinct cell populations poses MMP-2,9 activity as an important mediator and contributor in heroin-induced cell-specific synaptic plasticity. Heroin 206-212 matrix metallopeptidase 2 Rattus norvegicus 145-150 33870805-9 2021 Losartan 2.5, 5 and 10mg/kg combined with physical exercise lowered respectively 25.4%, 24.8%, and 31.8% of MMP-2 activity. Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 108-113 33341427-11 2021 R. vomitoria extract significantly reduced the testosterone-induced proliferation markers, including proliferating cell nuclear antigen and cyclin D1, in the prostate glands of BPH rats; it also reduced levels of androgen receptor, its associated protein steroid 5alpha-reductase 1 and its downstream target genes (FK506-binding protein 5 and matrix metalloproteinase 2). Testosterone 47-59 matrix metallopeptidase 2 Rattus norvegicus 343-369 33550530-0 2021 DNMT3b SUMOylation Mediated MMP-2 Upregulation Contribute to Paclitaxel Induced Neuropathic Pain. Paclitaxel 61-71 matrix metallopeptidase 2 Rattus norvegicus 28-33 33550530-3 2021 Our present study revealed that MMP-2 is also upregulated in paclitaxel induced neuropathic pain (NP), and knockdown it by siRNA can ameliorate mechanical allodynia. Paclitaxel 61-71 matrix metallopeptidase 2 Rattus norvegicus 32-37 33550530-7 2021 Intrathecal administration of SUMOylation inhibitor, ginkgolic acid (GA), could reverse enhanced SUMO1 modification of DNMT3b and upregulation of MMP-2 in the model rats. ginkgolic acid 53-67 matrix metallopeptidase 2 Rattus norvegicus 146-151 33550530-7 2021 Intrathecal administration of SUMOylation inhibitor, ginkgolic acid (GA), could reverse enhanced SUMO1 modification of DNMT3b and upregulation of MMP-2 in the model rats. ginkgolic acid 69-71 matrix metallopeptidase 2 Rattus norvegicus 146-151 33550530-8 2021 Further investigation suggested that DNMT3b binding activity to the promoter region of the MMP-2 gene is significantly decreased in paclitaxel treated rats, and the administration of GA can reverse these effects, which is also accompanied by changes in the promoter methylation status of the MMP-2 gene. Paclitaxel 132-142 matrix metallopeptidase 2 Rattus norvegicus 91-96 33550530-8 2021 Further investigation suggested that DNMT3b binding activity to the promoter region of the MMP-2 gene is significantly decreased in paclitaxel treated rats, and the administration of GA can reverse these effects, which is also accompanied by changes in the promoter methylation status of the MMP-2 gene. Paclitaxel 132-142 matrix metallopeptidase 2 Rattus norvegicus 292-297 33550530-8 2021 Further investigation suggested that DNMT3b binding activity to the promoter region of the MMP-2 gene is significantly decreased in paclitaxel treated rats, and the administration of GA can reverse these effects, which is also accompanied by changes in the promoter methylation status of the MMP-2 gene. ginkgolic acid 183-185 matrix metallopeptidase 2 Rattus norvegicus 91-96 33550530-8 2021 Further investigation suggested that DNMT3b binding activity to the promoter region of the MMP-2 gene is significantly decreased in paclitaxel treated rats, and the administration of GA can reverse these effects, which is also accompanied by changes in the promoter methylation status of the MMP-2 gene. ginkgolic acid 183-185 matrix metallopeptidase 2 Rattus norvegicus 292-297 33550530-9 2021 Our study demonstrates that MMP-2 up-regulation mediated by DNMT3b SUMOylation is essential for paclitaxel induced NP development, which brings us new therapeutic options for CIPN. Paclitaxel 96-106 matrix metallopeptidase 2 Rattus norvegicus 28-33 33929391-7 2021 The result showed that DOX promoted apoptosis and increased the expression of TNF-alpha (by 3.65 fold changes), IL-1beta (by 4.98 fold changes), IL-6 (by 3.44 fold changes), MMP-2 (by 1.98 fold changes), MMP-9 (by 1.98 fold changes) levels in H9c2 cells. Doxorubicin 23-26 matrix metallopeptidase 2 Rattus norvegicus 174-179 33879850-7 2021 Moreover, these Delta9-THC-exposed offsprings exhibited increased expression of collagen I and III, decreased matrix metallopeptidase-2 expression, and increased inactivation of glycogen synthase kinase-3beta, all associated with cardiac remodelling. Dronabinol 16-26 matrix metallopeptidase 2 Rattus norvegicus 110-135 33462684-5 2021 In BAPN-treated animals, PTU reduced apoptosis, p-SMAD2 staining, MMP-2, and -9 expression, and markedly decreased the damage to the aortic wall. Aminopropionitrile 3-7 matrix metallopeptidase 2 Rattus norvegicus 66-79 33462684-5 2021 In BAPN-treated animals, PTU reduced apoptosis, p-SMAD2 staining, MMP-2, and -9 expression, and markedly decreased the damage to the aortic wall. Propylthiouracil 25-28 matrix metallopeptidase 2 Rattus norvegicus 66-79 33881685-12 2021 Additionally, SN diminished lipid peroxidation and downregulated NF-kB in animals exposed to a low dose of LPS, with increased TIMP1 expression, while in animals treated with a high dose of LPS, SN increased NF-kB, MMP2, and MMP9 levels. Tin 14-16 matrix metallopeptidase 2 Rattus norvegicus 215-219 33881685-12 2021 Additionally, SN diminished lipid peroxidation and downregulated NF-kB in animals exposed to a low dose of LPS, with increased TIMP1 expression, while in animals treated with a high dose of LPS, SN increased NF-kB, MMP2, and MMP9 levels. Tin 195-197 matrix metallopeptidase 2 Rattus norvegicus 215-219 33881685-13 2021 In conclusion, SN extract diminished the inflammatory response, reduced generation of reactive oxygen species (ROS) and, influenced MMPs expressions, suggesting the benficial effect of SN extract on tissue remodeling in subacute rhinosinusitis and on systemic inflammatory response. Tin 15-17 matrix metallopeptidase 2 Rattus norvegicus 132-136 33719799-5 2021 BCA suppressed the expressions of proinflammatory cytokines and MMPs in ISO-induced MI in rats when compared to normal untreated MI rats. Isoproterenol 72-75 matrix metallopeptidase 2 Rattus norvegicus 64-68 33508402-7 2021 The data obtained from this study showed that the use of miR mimic and Q10 increased the level of miR-149, decreased the extent of neurological defects and tissue damage, increased BBB integrity, decreased brain water percentage and also decreased the level of inflammatory cytokines and MMPs. Water 212-217 matrix metallopeptidase 2 Rattus norvegicus 288-292 33508402-8 2021 It seems that the use of miRNA-149-5p mimic and Q10 can have a protective effect on the brain by reducing MMPs and inflammatory factors following cerebral ischemia and this could lead to a new treatment strategy to reduce the complications of cerebral ischemia. mirna-149-5p 25-37 matrix metallopeptidase 2 Rattus norvegicus 106-110 33400052-11 2021 Indeed, the nonselective MMP inhibitors TAPI-0 or TIMP2 and the MMP-2-selective ARP-100 enhanced hypertrophic growth. N-hydroxy-2-((4-phenylphenyl)sulfonylpropan-2-yloxyamino)acetamide 80-87 matrix metallopeptidase 2 Rattus norvegicus 64-69 33418305-10 2021 The extract significantly ameliorated the AAC-induced altered expression of heart failure markers such as ANP, NT-proBNP, and beta-MHC, as well as fibrosis, hypertrophy markers MMP-2 and MMP-9, and other heart failure-related factors including plasma levels of TNF-alpha and IL-6. aac 42-45 matrix metallopeptidase 2 Rattus norvegicus 177-182 32594359-0 2021 Co-administration of Aluminum Sulfate and Propolis Regulates Matrix Metalloproteinases-2/9 Expression and Improves the Uterine Leiomyoma in Adult Rat Model. aluminum sulfate 21-37 matrix metallopeptidase 2 Rattus norvegicus 61-90 32594359-6 2021 PR administration (100 and 200 mg/kg) alone or with alum (35 and 75 mg/kg) significantly decreased myometrium collagen contents and the gene expression and protein concentration of MMP-2 and 9 compared with UL and UL + Coi subgroups (P 0.05). Propolis 0-2 matrix metallopeptidase 2 Rattus norvegicus 181-192 32594359-6 2021 PR administration (100 and 200 mg/kg) alone or with alum (35 and 75 mg/kg) significantly decreased myometrium collagen contents and the gene expression and protein concentration of MMP-2 and 9 compared with UL and UL + Coi subgroups (P 0.05). aluminum sulfate 52-56 matrix metallopeptidase 2 Rattus norvegicus 181-192 33480300-9 2021 HDAC9 inhibition or miR-92a elevation improved pathological changes and repressed apoptosis and expression of MMP-2, MMP-9, VEGF and inflammatory factors in vascular tissues from IA rats. mir-92a 20-27 matrix metallopeptidase 2 Rattus norvegicus 110-115 32594359-7 2021 Alum (75 mg/kg) with PR (200 mg/kg) could improve UL features and reduce MMP-2 and 9 gene expression. aluminum sulfate 0-4 matrix metallopeptidase 2 Rattus norvegicus 73-84 32594359-7 2021 Alum (75 mg/kg) with PR (200 mg/kg) could improve UL features and reduce MMP-2 and 9 gene expression. Propolis 21-23 matrix metallopeptidase 2 Rattus norvegicus 73-84 33179312-6 2021 The results from both the rats with STZ and the HSCs treated with HG showed increased expression of DRD2, NOX-5, inflammation-related proteins (IL-6 and TNFalpha) and fibrosis-related proteins (TGF-beta1, CO-I/III/ IV, MMP-2/9 and Fibronectin). Streptozocin 36-39 matrix metallopeptidase 2 Rattus norvegicus 219-226 33179312-6 2021 The results from both the rats with STZ and the HSCs treated with HG showed increased expression of DRD2, NOX-5, inflammation-related proteins (IL-6 and TNFalpha) and fibrosis-related proteins (TGF-beta1, CO-I/III/ IV, MMP-2/9 and Fibronectin). Mercury 66-68 matrix metallopeptidase 2 Rattus norvegicus 219-226 33611790-8 2021 The results evidenced both short- and long-term alterations on MMP-2 and -9 expression in the limbic structures following CFA-induced temporomandibular inflammation. 3-chloro-4-fluoroaniline 122-125 matrix metallopeptidase 2 Rattus norvegicus 63-75 33609350-4 2021 RESULTS The levels of heat-shock protein (HSP)-70 increased and matrix metalloproteinase (MMP)-2, MMP-9, and tumor necrosis factor (TNF)-alpha decreased in the group that received NIPPV treatment compared with the control group. nippv 180-185 matrix metallopeptidase 2 Rattus norvegicus 64-96 33335249-7 2020 MMP-2 in the perfusate was significantly reduced in both treatment groups [Control 43.7 +- 7.2 arbitrary units, versus Preemptive Doxy group 23.2 +- 5.5 (p = 0.03), and "Preemptive and Perfusion" group 18.0 +- 5.6 (p = 0.02)]. Doxycycline 130-134 matrix metallopeptidase 2 Rattus norvegicus 0-5 33508970-3 2021 Gene expression study revealed that EZ significantly down-regulated the renal AGEs-receptor (RAGE), nuclear factor-kappaB (NFkappaB-2), transforming growth factor-beta (TGF-beta1), and matrix metalloproteinase-2 (MMP-2) mRNA expression, however, the neuropilin-1 (NRP-1) mRNA expression was up-regulated. Ezetimibe 36-38 matrix metallopeptidase 2 Rattus norvegicus 185-211 33508970-3 2021 Gene expression study revealed that EZ significantly down-regulated the renal AGEs-receptor (RAGE), nuclear factor-kappaB (NFkappaB-2), transforming growth factor-beta (TGF-beta1), and matrix metalloproteinase-2 (MMP-2) mRNA expression, however, the neuropilin-1 (NRP-1) mRNA expression was up-regulated. Ezetimibe 36-38 matrix metallopeptidase 2 Rattus norvegicus 213-218 33396569-7 2020 We found that exposure to F during pre- and postnatal period causes a change in the mRNA and protein level of MMP2, MMP9, TIMP2 and TIMP3 in the prefrontal cortex, striatum, hippocampus and cerebellum. Fluorides 26-27 matrix metallopeptidase 2 Rattus norvegicus 110-114 33380311-7 2021 The effects of MEL on the activity of MMP-2 and MMP-9 were assessed using gelatin zymography method every week till day 28 post-SCI. Melatonin 15-18 matrix metallopeptidase 2 Rattus norvegicus 38-43 33380311-10 2021 Moreover, MEL suppressed MMP-9 activity while increasing that of MMP-2 post-SCI indicating its anti-neuroinflammatory effects. Melatonin 10-13 matrix metallopeptidase 2 Rattus norvegicus 65-70 33490282-16 2021 Inhibition of miR-124-3p or upregulation of MMP2 reversed inhibitory effects of SNHG14 silence on inflammation and oxidative stress as well as the promoting effect of SNHG14 silence on cell viability in H/R-induced HK-2 cells. snhg14 80-86 matrix metallopeptidase 2 Rattus norvegicus 44-48 33490282-16 2021 Inhibition of miR-124-3p or upregulation of MMP2 reversed inhibitory effects of SNHG14 silence on inflammation and oxidative stress as well as the promoting effect of SNHG14 silence on cell viability in H/R-induced HK-2 cells. snhg14 167-173 matrix metallopeptidase 2 Rattus norvegicus 44-48 33490282-17 2021 Conclusion: Knockdown of SNHG14 alleviated I/R-induced AKI by miR-124-3p-mediated downregulation of MMP2. snhg14 25-31 matrix metallopeptidase 2 Rattus norvegicus 100-104 33381584-11 2020 Both mRNA expression and activity of MMP-2 increased, with the largest increase in the DMAPA-Glyp+siRNA group. dimethylarsinopenicillamine 87-92 matrix metallopeptidase 2 Rattus norvegicus 37-42 33381584-11 2020 Both mRNA expression and activity of MMP-2 increased, with the largest increase in the DMAPA-Glyp+siRNA group. glyp 93-97 matrix metallopeptidase 2 Rattus norvegicus 37-42 33219891-6 2021 In a rat model of chemically induced RCC, squalene displayed chemopreventive capabilities by substantial reversal of lipid peroxidation, mitochondrial redox regulation, maintaining psim, inflammation [Akt, nuclear factor kappaB (NF-kappaB)], angiogenesis (VEGFalpha), metastasis [matrix metalloproteinase 2 (MMP-2)], and survival (Bax/Bcl2, cytochrome-c, Casp3). Squalene 42-50 matrix metallopeptidase 2 Rattus norvegicus 281-307 32772200-9 2020 Then, BHB treatments were found to up-regulate renal MMP-2 generation of the diabetic rats significantly, while not affecting the increased TGF-beta/Smad3 contents. 3-Hydroxybutyric Acid 6-9 matrix metallopeptidase 2 Rattus norvegicus 53-58 32772200-10 2020 Furthermore, the contents of H3K9bhb in the Mmp-2 promoter were elevated significantly for the middle and high concentrations of BHB treatments, up-regulating MMP-2 generation. 3-Hydroxybutyric Acid 129-132 matrix metallopeptidase 2 Rattus norvegicus 44-49 32772200-10 2020 Furthermore, the contents of H3K9bhb in the Mmp-2 promoter were elevated significantly for the middle and high concentrations of BHB treatments, up-regulating MMP-2 generation. 3-Hydroxybutyric Acid 129-132 matrix metallopeptidase 2 Rattus norvegicus 159-164 32772200-11 2020 CONCLUSION: BHB treatments could up-regulate MMP-2 generation via causing elevated H3K9bhb in its promoter to antagonize glomerulosclerosis in the diabetic rats. 3-Hydroxybutyric Acid 12-15 matrix metallopeptidase 2 Rattus norvegicus 45-50 31201434-10 2020 CONCLUSION: Typhaneoside regulates IL-6 and TNF-alpha as well as MMP-2 and MMP-9 in rats with heart failure after myocardial infarction. typhaneoside 12-24 matrix metallopeptidase 2 Rattus norvegicus 65-70 33292360-0 2020 Water treadmill training attenuates blood-spinal cord barrier disruption in rats by promoting angiogenesis and inhibiting matrix metalloproteinase-2/9 expression following spinal cord injury. Water 0-5 matrix metallopeptidase 2 Rattus norvegicus 122-150 33292360-12 2020 CONCLUSIONS: The results of this study indicate that TT promotes functional recovery for the following reasons: TT (1) protects residual BSCB structure from further damage, (2) promotes vascular regeneration, and (3) inhibits MMP-2/9 expression to mitigate BSCB damage. 6-thiotheophylline 53-55 matrix metallopeptidase 2 Rattus norvegicus 226-233 33292360-12 2020 CONCLUSIONS: The results of this study indicate that TT promotes functional recovery for the following reasons: TT (1) protects residual BSCB structure from further damage, (2) promotes vascular regeneration, and (3) inhibits MMP-2/9 expression to mitigate BSCB damage. 6-thiotheophylline 112-114 matrix metallopeptidase 2 Rattus norvegicus 226-233 33219891-6 2021 In a rat model of chemically induced RCC, squalene displayed chemopreventive capabilities by substantial reversal of lipid peroxidation, mitochondrial redox regulation, maintaining psim, inflammation [Akt, nuclear factor kappaB (NF-kappaB)], angiogenesis (VEGFalpha), metastasis [matrix metalloproteinase 2 (MMP-2)], and survival (Bax/Bcl2, cytochrome-c, Casp3). Squalene 42-50 matrix metallopeptidase 2 Rattus norvegicus 309-314 32592722-20 2020 The findings of the present study suggest that PTX and ETN treatment exerts immunomodulatory effects, blunted excessive ROS formation, and decreased renovascular hypertension-induced MMP-2 up-regulation, leading to improvement ofvascular remodeling typically found in 2K1C hypertension. Pentoxifylline 47-50 matrix metallopeptidase 2 Rattus norvegicus 183-188 32976827-8 2020 Seven days post-MI, morphine led to significant reduction in MMP - 2 activity, apoptotic cell death and fibroblast density. Morphine 20-28 matrix metallopeptidase 2 Rattus norvegicus 61-68 32955605-10 2020 Nanoformulation enhances the bioavailability of Naringenin and liver specific delivery of the same, which up-regulates MMP-2 hepatic proteins resulting in reduced liver fibrosis. naringenin 48-58 matrix metallopeptidase 2 Rattus norvegicus 119-124 32564302-11 2020 The downregulation of BAPN-induced MMP2 expression by SIRT1 was mediated by deacetylation of histone H3 lysine 9 (H3K9) on the Mmp2 promoter in the A7r5 cells. Lysine 104-110 matrix metallopeptidase 2 Rattus norvegicus 35-39 32564302-11 2020 The downregulation of BAPN-induced MMP2 expression by SIRT1 was mediated by deacetylation of histone H3 lysine 9 (H3K9) on the Mmp2 promoter in the A7r5 cells. Lysine 104-110 matrix metallopeptidase 2 Rattus norvegicus 127-131 32440769-12 2020 PDTC treatment reduced MMP-2 activity and iNOS and p65 NFkappaB nuclear expression found increased in diabetic kidneys. prolinedithiocarbamate 0-4 matrix metallopeptidase 2 Rattus norvegicus 23-28 32440769-13 2020 Our results show that the NFkappaB inhibitor PDTC reduces renal damage through reduction of Nox4, iNOS, macrophages, and MMP-2 in the alloxan-induced diabetic model. prolinedithiocarbamate 45-49 matrix metallopeptidase 2 Rattus norvegicus 121-126 32081684-12 2020 alpha-Tocopherol also inhibited maternal endotoxemia-induced changes in TGF-beta1/NOX2/MMP-2 signaling. alpha-Tocopherol 0-16 matrix metallopeptidase 2 Rattus norvegicus 87-92 32911524-1 2020 BACKGROUND: We have previously shown that obeticholic acid (OCA) upregulates the biliary excretion of asymmetric dimethylarginine (ADMA), an inhibitor of iNOS regulating the activity of matrix metalloproteinases (MMPs). obeticholic acid 42-58 matrix metallopeptidase 2 Rattus norvegicus 213-217 32911524-1 2020 BACKGROUND: We have previously shown that obeticholic acid (OCA) upregulates the biliary excretion of asymmetric dimethylarginine (ADMA), an inhibitor of iNOS regulating the activity of matrix metalloproteinases (MMPs). obeticholic acid 60-63 matrix metallopeptidase 2 Rattus norvegicus 213-217 32911524-1 2020 BACKGROUND: We have previously shown that obeticholic acid (OCA) upregulates the biliary excretion of asymmetric dimethylarginine (ADMA), an inhibitor of iNOS regulating the activity of matrix metalloproteinases (MMPs). dimethylarginine 113-129 matrix metallopeptidase 2 Rattus norvegicus 213-217 32911524-1 2020 BACKGROUND: We have previously shown that obeticholic acid (OCA) upregulates the biliary excretion of asymmetric dimethylarginine (ADMA), an inhibitor of iNOS regulating the activity of matrix metalloproteinases (MMPs). N,N-dimethylarginine 131-135 matrix metallopeptidase 2 Rattus norvegicus 213-217 32619673-9 2020 Mechanistically, 14.0 mg/kg of (-)-kusunokinin decreased cell proliferation (c-Src, PI3K, Akt, p-Erk1/2 and c-Myc), cell cycle (E2f-1, cyclin B1 and CDK1), and metastasis (E-cadherin, MMP-2 and MMP-9) proteins in tumor tissues, which supports its anticancer effect. kusunokinin 35-46 matrix metallopeptidase 2 Rattus norvegicus 184-189 32704495-8 2020 Similarly, significantly lower mRNA expression of collagen alpha-1(I), matrix metalloproteinase-2, platelet-derived growth factor (PDGF)-B chain, and connective tissue growth factor (CTGF) were evident in the BDL+TZD group compared to those in the BDL group (p=0.0002, p<0.035, p<0.0001, and p=0.0123 respectively). 2,4-thiazolidinedione 213-216 matrix metallopeptidase 2 Rattus norvegicus 71-97 32111755-6 2020 RESULTS: An improvement in oxidative stress, antioxidant status, and TNF-alpha, MMP-2 and MMP-9 levels was obtained in groups pretreated with LCC compared to silymarin treatment, in a dose-dependent manner. [(1R,3R,4R,7S)-7-HYDROXY-3-(5-METHYLCYTOSIN-1-YL)-2,5-DIOXABICYCLO[2.2.1]HEPT-1-YL]METHYL DIHYDROGEN PHOSPHATE 142-145 matrix metallopeptidase 2 Rattus norvegicus 80-85 32322413-3 2020 Increased production of toxic peroxynitrite (ONOO-) during oxidative stress is a source of increased nitration/nitrosylation of contractile proteins, which enhance their degradation through MMP-2. Peroxynitrous Acid 30-43 matrix metallopeptidase 2 Rattus norvegicus 190-195 32322413-3 2020 Increased production of toxic peroxynitrite (ONOO-) during oxidative stress is a source of increased nitration/nitrosylation of contractile proteins, which enhance their degradation through MMP-2. oxido nitrite 45-50 matrix metallopeptidase 2 Rattus norvegicus 190-195 32214801-12 2020 There was a significant increase in the expression of VEGF, MMP-2 and MMP-9 secreted by MSCs treated with 1,25(OH)2D3, as well as in the activity of MMP-2 and MMP-9. Calcitriol 106-117 matrix metallopeptidase 2 Rattus norvegicus 60-65 32091104-5 2020 Overexpressing KLF2 in LPS-AMs inhibited the phosphorylation of STAT3 and reduced the levels of STAT3 target genes, including matrix metalloproteinase-2/9 (MMP-2/9). lps-ams 23-30 matrix metallopeptidase 2 Rattus norvegicus 126-154 32091104-5 2020 Overexpressing KLF2 in LPS-AMs inhibited the phosphorylation of STAT3 and reduced the levels of STAT3 target genes, including matrix metalloproteinase-2/9 (MMP-2/9). lps-ams 23-30 matrix metallopeptidase 2 Rattus norvegicus 156-163 32214801-8 2020 Western blotting and gelatin zymography were used to detect the expression and activities of VEGF, MMP-2 and MMP-9 secreted by MSCs under the influence of 1,25(OH)2D3. Calcitriol 155-166 matrix metallopeptidase 2 Rattus norvegicus 99-104 30648329-3 2020 Previously, we showed that escalation of alcohol self-administration is a learned plasticity-dependent process that requires an intact MMP system. Alcohols 41-48 matrix metallopeptidase 2 Rattus norvegicus 135-138 30648329-4 2020 To identify the MMP subtypes within specific brain regions that are associated with plasticity underlying the negative reinforcing effects of alcohol (as measured by escalated alcohol self-administration) during acute withdrawal in alcohol dependence, male Wistar rats were trained to self-administer alcohol in an operant paradigm, subjected to one month of intermittent alcohol vapor exposure to induce alcohol dependence and then allowed to self-administer alcohol during repeated acute withdrawal self-administration sessions. Alcohols 142-149 matrix metallopeptidase 2 Rattus norvegicus 16-19 31830479-11 2020 VRP decreased hypertension-induced enhances in calpain-1 and MMP-2 activities, oxidative stress and mature TGF-beta levels. Verapamil 0-3 matrix metallopeptidase 2 Rattus norvegicus 61-66 31738197-0 2020 Sulodexide Improves Contraction and Decreases Matrix Metalloproteinase-2 and -9 in Veins under Prolonged Stretch. glucuronyl glucosamine glycan sulfate 0-10 matrix metallopeptidase 2 Rattus norvegicus 46-79 31738197-12 2020 The SDX-induced improvement of contraction and restoration of vein function appear to involve decreases in MMP-2 and MMP-9 and may contribute to the benefits of SDX in CVI and VVs. glucuronyl glucosamine glycan sulfate 4-7 matrix metallopeptidase 2 Rattus norvegicus 107-112 31830479-13 2020 SIGNIFICANCE: Treatment with VRP decreases calpain-1 and MMP-2 activities and also reduces TGF-beta and MMP-14/TIMP-2 levels in the LV of hypertensive rats, thus contributing to ameliorate cardiac hypertrophy. Verapamil 29-32 matrix metallopeptidase 2 Rattus norvegicus 57-62 32016456-10 2020 Urantide treatment resulted in markedly decreased expression levels of matrix metalloproteinase 2 (MMP-2), collagen type I/III, and genes and proteins in the JAK2/STAT3 pathway. urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)- 0-8 matrix metallopeptidase 2 Rattus norvegicus 71-97 32016456-10 2020 Urantide treatment resulted in markedly decreased expression levels of matrix metalloproteinase 2 (MMP-2), collagen type I/III, and genes and proteins in the JAK2/STAT3 pathway. urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)- 0-8 matrix metallopeptidase 2 Rattus norvegicus 99-104 32016456-12 2020 In addition, the MMP-2/TIMP-2 protein ratio was significantly decreased in rats treated with urantide compared with AS rats with no urantide treatment. urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)- 93-101 matrix metallopeptidase 2 Rattus norvegicus 17-22 31922224-9 2020 The results demonstrated that FMN significantly alleviated the changes of hemodynamics and pulmonary vascular morphology, and decreased the MCT-induced upregulations of TGFbeta1, MMP2 and MMP9 expression levels. formononetin 30-33 matrix metallopeptidase 2 Rattus norvegicus 179-183 32016456-12 2020 In addition, the MMP-2/TIMP-2 protein ratio was significantly decreased in rats treated with urantide compared with AS rats with no urantide treatment. urotensin II (4-11), Pen(5)-Trp(7)-Orn(8)- 132-140 matrix metallopeptidase 2 Rattus norvegicus 17-22 31820448-7 2020 ICS II (8 and 16 mg/kg) downregulated the expression of MMP-2 and MMP9 and upregulated the expression of TIMP1. baohuoside I 0-6 matrix metallopeptidase 2 Rattus norvegicus 56-61 31922224-9 2020 The results demonstrated that FMN significantly alleviated the changes of hemodynamics and pulmonary vascular morphology, and decreased the MCT-induced upregulations of TGFbeta1, MMP2 and MMP9 expression levels. Monocrotaline 140-143 matrix metallopeptidase 2 Rattus norvegicus 179-183 32093214-13 2020 MMP-2 and -9 were also significantly reduced in the L-EGCG-treated group compared with the EGCG group (p < 0.001). epigallocatechin gallate 52-58 matrix metallopeptidase 2 Rattus norvegicus 0-12 32093214-13 2020 MMP-2 and -9 were also significantly reduced in the L-EGCG-treated group compared with the EGCG group (p < 0.001). epigallocatechin gallate 54-58 matrix metallopeptidase 2 Rattus norvegicus 0-12 32093214-14 2020 CONCLUSIONS: the liposomal nanoformulation of EGCG may serve as an adjuvant therapy in DM due to its unique modulatory effect on oxidative stress/antioxidant biomarkers and MMP-2 and -9. epigallocatechin gallate 46-50 matrix metallopeptidase 2 Rattus norvegicus 173-185 31894295-8 2020 The inhibition of VEGF attenuated the effects of the overexpression of miR-15a-5p on the inhibition of cell proliferation, apoptotic rate, caspase-3/9 activity and protein expression of Bax, and it attenuated the increased inflammation, as indicated by the protein expression of p38 and MMP-2 in the PASMCs. mir-15a-5p 71-81 matrix metallopeptidase 2 Rattus norvegicus 287-292 31894295-9 2020 In conclusion, the data of the present study demonstrated that miR-15a-5p induced the apoptosis of PASMCs in an animal model of PAH via the VEGF/p38/MMP-2 signaling pathway. mir-15a-5p 63-73 matrix metallopeptidase 2 Rattus norvegicus 149-154 31698141-12 2020 (2) LXA4 inhibited LPS-induced Hyp production, meanwhile down-regulated LPS-induced Collagen I, Collagen III, MMP-2, and MMP-9 in HSC-T6 cells. lipoxin A4 4-8 matrix metallopeptidase 2 Rattus norvegicus 110-115 32673649-10 2020 RESULTS AND CONCLUSIONS: Curcumin reduced liver damage, oxidative stress, fibrosis, and restored normal activity of MMP-9 and MMP-2. Curcumin 25-33 matrix metallopeptidase 2 Rattus norvegicus 126-131 31947691-2 2020 We aimed to test our hypothesis that omega-3 (eicosapentaenoic acid-EPA, docosahexaenoic acid-DHA) may inhibit matrix metalloproteinase (MMP-2) activity to prevent cleavage of beta1-AR and formation of beta1-AA resulting in attenuation of pro-arrhythmic connexin-43 (Cx43) and protein kinase C (PKC) signaling in the diseased heart. Eicosapentaenoic Acid 46-67 matrix metallopeptidase 2 Rattus norvegicus 137-142 31947691-2 2020 We aimed to test our hypothesis that omega-3 (eicosapentaenoic acid-EPA, docosahexaenoic acid-DHA) may inhibit matrix metalloproteinase (MMP-2) activity to prevent cleavage of beta1-AR and formation of beta1-AA resulting in attenuation of pro-arrhythmic connexin-43 (Cx43) and protein kinase C (PKC) signaling in the diseased heart. 2,3-epoxypropyl acrylate 68-71 matrix metallopeptidase 2 Rattus norvegicus 137-142 31947691-2 2020 We aimed to test our hypothesis that omega-3 (eicosapentaenoic acid-EPA, docosahexaenoic acid-DHA) may inhibit matrix metalloproteinase (MMP-2) activity to prevent cleavage of beta1-AR and formation of beta1-AA resulting in attenuation of pro-arrhythmic connexin-43 (Cx43) and protein kinase C (PKC) signaling in the diseased heart. Docosahexaenoic Acids 73-97 matrix metallopeptidase 2 Rattus norvegicus 137-142 31947691-7 2020 The implication of MMP-2 in the action of omega-3 was also demonstrated in cultured cardiomyocytes in which desensitization of beta1-AR due to permanent activation of beta1-AR with isoproterenol was prevented by MMP-2 inhibitor or EPA. Isoproterenol 181-194 matrix metallopeptidase 2 Rattus norvegicus 19-24 31947691-7 2020 The implication of MMP-2 in the action of omega-3 was also demonstrated in cultured cardiomyocytes in which desensitization of beta1-AR due to permanent activation of beta1-AR with isoproterenol was prevented by MMP-2 inhibitor or EPA. Isoproterenol 181-194 matrix metallopeptidase 2 Rattus norvegicus 212-217 31947691-7 2020 The implication of MMP-2 in the action of omega-3 was also demonstrated in cultured cardiomyocytes in which desensitization of beta1-AR due to permanent activation of beta1-AR with isoproterenol was prevented by MMP-2 inhibitor or EPA. 2,3-epoxypropyl acrylate 231-234 matrix metallopeptidase 2 Rattus norvegicus 19-24 31947691-7 2020 The implication of MMP-2 in the action of omega-3 was also demonstrated in cultured cardiomyocytes in which desensitization of beta1-AR due to permanent activation of beta1-AR with isoproterenol was prevented by MMP-2 inhibitor or EPA. 2,3-epoxypropyl acrylate 231-234 matrix metallopeptidase 2 Rattus norvegicus 212-217 31629700-6 2020 We also show that saxagliptin can reduce the expression of matrix metallopeptidase-2 (MMP-2) and matrix metallopeptidase-9 (MMP-9), two important degradative enzymes. saxagliptin 18-29 matrix metallopeptidase 2 Rattus norvegicus 59-84 31629700-6 2020 We also show that saxagliptin can reduce the expression of matrix metallopeptidase-2 (MMP-2) and matrix metallopeptidase-9 (MMP-9), two important degradative enzymes. saxagliptin 18-29 matrix metallopeptidase 2 Rattus norvegicus 86-91 31834839-13 2020 Decreased uterine vascularization and uterine arterial expansive remodeling by MMPs could be contributing mechanisms to uteroplacental ischemia in HTN-Preg and preeclampsia.NEW & NOTEWORTHY Preeclampsia is a pregnancy-related disorder in which initial inadequate placentation and RUPP cause the release of cytoactive factors and trigger a ceaseless cycle of suppressed trophoblast invasion of spiral arteries, further RUPP, and progressive placental ischemia leading to HTN-Preg and IUGR; however, the extent/depth of uterine vascularization and the driving proteolytic enzymes and ECM proteins are unclear. rupp 280-284 matrix metallopeptidase 2 Rattus norvegicus 79-83 31746394-7 2020 Moreover, KXS significantly attenuated ISO + depression-induced MMP-2 and MMP-9 expression at the mRNA and protein level and decreased TIMP in the heart compared to the complex model group. iso 39-42 matrix metallopeptidase 2 Rattus norvegicus 64-69 31638216-5 2019 Ang II significantly upregulated NF-kappaB, activator protein-1, transforming growth factor-beta1 (TGF-beta1), collagen I and matrix metalloproteinase 2, leading to atrial fibrosis, and downregulated expression of Cx40 and Cx43. Angiotensins 0-3 matrix metallopeptidase 2 Rattus norvegicus 111-152 31618621-12 2019 Naringenin reversed liver damage, biochemical and oxidative stress marker elevation, and fibrosis and restored normal MMP-9 and MMP-2 activity. naringenin 0-10 matrix metallopeptidase 2 Rattus norvegicus 128-133 31027431-6 2019 RESULTS: Our study showed that the chrysin-curcumin-loaded nanofibres have anti-inflammatory properties in several stages of the wound-healing process by affecting the IL-6, MMP-2, TIMP-1, TIMP-2 and iNOS gene expression. Curcumin 43-51 matrix metallopeptidase 2 Rattus norvegicus 174-179 31762036-0 2019 Ligustilide Inhibited Rat Vascular Smooth Muscle Cells Migration via c-Myc/MMP2 and ROCK/JNK Signaling Pathway. ligustilide 0-11 matrix metallopeptidase 2 Rattus norvegicus 75-79 31762036-9 2019 In vitro, LIG suppressed AngII-induced VSMCs migration and downregulated the expression of migration related protein c-Myc, MMP2, ROCK1, ROCK2, p-JNK, and JNK. ligustilide 10-13 matrix metallopeptidase 2 Rattus norvegicus 124-128 31762036-10 2019 These findings suggested the protective effect of LIG on VSMCs migration was associated with the decrement of c-Myc/MMP2 signaling pathway and ROCK-JNK signaling pathway. ligustilide 50-53 matrix metallopeptidase 2 Rattus norvegicus 116-120 31454490-6 2019 Furthermore, pretreatment with daidzein, a specific inhibitor of Cav-1, reversed the inhibitory effects of recombinant FABP7 on matrix metalloproteinase (MMP)-2/9 expression and abolished its BBB protection after TBI. daidzein 31-39 matrix metallopeptidase 2 Rattus norvegicus 128-162 31638340-13 2019 Thymoquinone blocked VSMC migration by inhibiting MMP2. thymoquinone 0-12 matrix metallopeptidase 2 Rattus norvegicus 50-54 31801223-7 2019 Our results showed that EGCG integration attenuated MMP-2 (70.6%) and -9 expression (69.1%) in the 1 week group, increased residual gelatin (118.7%), and augmented bone formation (101.8%) in the 4 weeks group in critical-sized bone defects of rat calvaria compared with vacuum-heated gelatin sponges without EGCG. epigallocatechin gallate 24-28 matrix metallopeptidase 2 Rattus norvegicus 52-57 31600634-7 2019 CONCLUSION: Ticagrelor, empagliflozin and tamoxifen may correct vascular reactivity defects, where modulation of vascular AMPK, eNOS, Ang-II, ET-1, P-selectin, VCAM-1 and MMP-2 underline their protective effects. Ticagrelor 12-22 matrix metallopeptidase 2 Rattus norvegicus 171-176 31600634-7 2019 CONCLUSION: Ticagrelor, empagliflozin and tamoxifen may correct vascular reactivity defects, where modulation of vascular AMPK, eNOS, Ang-II, ET-1, P-selectin, VCAM-1 and MMP-2 underline their protective effects. Tamoxifen 42-51 matrix metallopeptidase 2 Rattus norvegicus 171-176 31801223-9 2019 The results indicated that integration of EGCG in gelatin-based materials modulated the production and activity of MMP-2 and -9 in vivo, thereby enhancing bone-forming capacity. epigallocatechin gallate 42-46 matrix metallopeptidase 2 Rattus norvegicus 115-127 31578682-12 2019 According to our findings, it can be suggested that nicotine has negative effects on microvascular circulation by increasing VEGF and MMP2 levels. Nicotine 52-60 matrix metallopeptidase 2 Rattus norvegicus 134-138 31757048-3 2019 The suppressive activities of ginkgetin and resveratrol in VEGF-mediated angiogenesis were supported by several lines of evidence including (i) inhibiting the formation of sub-intestinal vessel in zebrafish embryos and microvascular sprouting in rat aortic ring; and (ii) suppressing the phosphorylations of VEGFR2, Akt, eNOS, and Erk as well as expressions of matrix metalloproteinases (MMPs), MMP-2, and MMP-9 in human umbilical vein endothelial cells (HUVECs). ginkgetin 30-39 matrix metallopeptidase 2 Rattus norvegicus 388-392 31757048-3 2019 The suppressive activities of ginkgetin and resveratrol in VEGF-mediated angiogenesis were supported by several lines of evidence including (i) inhibiting the formation of sub-intestinal vessel in zebrafish embryos and microvascular sprouting in rat aortic ring; and (ii) suppressing the phosphorylations of VEGFR2, Akt, eNOS, and Erk as well as expressions of matrix metalloproteinases (MMPs), MMP-2, and MMP-9 in human umbilical vein endothelial cells (HUVECs). ginkgetin 30-39 matrix metallopeptidase 2 Rattus norvegicus 395-400 31757048-3 2019 The suppressive activities of ginkgetin and resveratrol in VEGF-mediated angiogenesis were supported by several lines of evidence including (i) inhibiting the formation of sub-intestinal vessel in zebrafish embryos and microvascular sprouting in rat aortic ring; and (ii) suppressing the phosphorylations of VEGFR2, Akt, eNOS, and Erk as well as expressions of matrix metalloproteinases (MMPs), MMP-2, and MMP-9 in human umbilical vein endothelial cells (HUVECs). resveratrol 44-55 matrix metallopeptidase 2 Rattus norvegicus 388-392 31757048-3 2019 The suppressive activities of ginkgetin and resveratrol in VEGF-mediated angiogenesis were supported by several lines of evidence including (i) inhibiting the formation of sub-intestinal vessel in zebrafish embryos and microvascular sprouting in rat aortic ring; and (ii) suppressing the phosphorylations of VEGFR2, Akt, eNOS, and Erk as well as expressions of matrix metalloproteinases (MMPs), MMP-2, and MMP-9 in human umbilical vein endothelial cells (HUVECs). resveratrol 44-55 matrix metallopeptidase 2 Rattus norvegicus 395-400 31578682-0 2019 Nicotine increased VEGF and MMP2 levels in the rat eye and kidney. Nicotine 0-8 matrix metallopeptidase 2 Rattus norvegicus 28-32 31578682-4 2019 The aim of this study was to investigate the effect of nicotine on VEGF and MMP2 levels in kidney and eyes, where microcirculation is very important for their function. Nicotine 55-63 matrix metallopeptidase 2 Rattus norvegicus 76-80 31578682-7 2019 The VEGF and MMP2 levels were increased in kidney tissue of both genders as a result of given nicotine. Nicotine 94-102 matrix metallopeptidase 2 Rattus norvegicus 13-17 31271212-10 2019 Thus, ascorbic acid insufficiency affected the immunolocalization of cathepsin H and MMP2; however, ligamentous fibroblasts appear to possess the potential to synthesize collagen fibers when supplied with ascorbic acid. Ascorbic Acid 6-19 matrix metallopeptidase 2 Rattus norvegicus 85-89 31578682-10 2019 The use of nicotine made VEGF and MMP2 levels increase in kidney tissue in both genders of rats. Nicotine 11-19 matrix metallopeptidase 2 Rattus norvegicus 34-38 30989649-0 2019 Metformin treatment alleviates polycystic ovary syndrome by decreasing the expression of MMP-2 and MMP-9 via H19/miR-29b-3p and AKT/mTOR/autophagy signaling pathways. Metformin 0-9 matrix metallopeptidase 2 Rattus norvegicus 89-94 30989649-1 2019 In this study, we aimed to investigate the molecular pathway(s) underlying the effect of metformin (MET) on the expression of matrix metalloproteinase (MMP)-2 and MMP-9. Metformin 89-98 matrix metallopeptidase 2 Rattus norvegicus 126-158 31106412-10 2019 In addition, omega-3 combined with ASA also inhibited the RANKL-induced gene expressions of MMPs in dose-dependent manners. Fatty Acids, Omega-3 13-20 matrix metallopeptidase 2 Rattus norvegicus 92-96 31106412-10 2019 In addition, omega-3 combined with ASA also inhibited the RANKL-induced gene expressions of MMPs in dose-dependent manners. Aspirin 35-38 matrix metallopeptidase 2 Rattus norvegicus 92-96 31625370-9 2019 Introduction of SB203580 inhibited the expression of RE, which then abolished the up-regulation role of RE on the expression of MMP-2, MMP-9, and PAI-1. SB 203580 16-24 matrix metallopeptidase 2 Rattus norvegicus 128-133 31408234-3 2019 A glutathione (GSH)-modified collagen hydrogel (collagen-GSH) is prepared by conjugating collagen amine groups with GSH sulfhydryl groups and the recombinant protein GST-TIMP-bFGF (bFGF: basic fibroblast growth factor) by fusing bFGF with glutathione-S-transferase (GST) and MMP-2/9 cleavable peptide PLGLAG (TIMP). Glutathione 57-60 matrix metallopeptidase 2 Rattus norvegicus 275-282 31229551-5 2019 DM-celecoxib also suppressed the proliferation and the production of matrix metalloproteinase-2 and fibronectin of rat cardiac fibroblasts. dm-celecoxib 0-12 matrix metallopeptidase 2 Rattus norvegicus 69-95 31353051-7 2019 Further, alpha-smooth-muscle actin (alpha-SMA), collagen I, profibrotic factor-connective tissue growth factor (CTGF), matrix metalloproteinase-2 (MMP2) and MMP9 levels were down-regulated in hyperoside-treated ACF rats. hyperoside 192-202 matrix metallopeptidase 2 Rattus norvegicus 119-145 31408234-3 2019 A glutathione (GSH)-modified collagen hydrogel (collagen-GSH) is prepared by conjugating collagen amine groups with GSH sulfhydryl groups and the recombinant protein GST-TIMP-bFGF (bFGF: basic fibroblast growth factor) by fusing bFGF with glutathione-S-transferase (GST) and MMP-2/9 cleavable peptide PLGLAG (TIMP). Glutathione 2-13 matrix metallopeptidase 2 Rattus norvegicus 275-282 31408234-3 2019 A glutathione (GSH)-modified collagen hydrogel (collagen-GSH) is prepared by conjugating collagen amine groups with GSH sulfhydryl groups and the recombinant protein GST-TIMP-bFGF (bFGF: basic fibroblast growth factor) by fusing bFGF with glutathione-S-transferase (GST) and MMP-2/9 cleavable peptide PLGLAG (TIMP). Glutathione 15-18 matrix metallopeptidase 2 Rattus norvegicus 275-282 31408234-3 2019 A glutathione (GSH)-modified collagen hydrogel (collagen-GSH) is prepared by conjugating collagen amine groups with GSH sulfhydryl groups and the recombinant protein GST-TIMP-bFGF (bFGF: basic fibroblast growth factor) by fusing bFGF with glutathione-S-transferase (GST) and MMP-2/9 cleavable peptide PLGLAG (TIMP). Glutathione 57-60 matrix metallopeptidase 2 Rattus norvegicus 275-282 31310955-9 2019 Meanwhile, the activation of MMP-2 and MMP-9 induced by HI was partially blocked by Van. hi 56-58 matrix metallopeptidase 2 Rattus norvegicus 29-34 31310955-9 2019 Meanwhile, the activation of MMP-2 and MMP-9 induced by HI was partially blocked by Van. vanillin 84-87 matrix metallopeptidase 2 Rattus norvegicus 29-34 31177586-8 2019 Obeticholic acid inhibited hepatic TLR4 expression and increased hepatic matrix metalloproteinase-2 expression. obeticholic acid 0-16 matrix metallopeptidase 2 Rattus norvegicus 73-99 31220437-0 2019 Angiogenic and MMPs modulatory effects of icariin improved cutaneous wound healing in rats. icariin 42-49 matrix metallopeptidase 2 Rattus norvegicus 15-19 31386877-7 2019 The SA-treated diabetic wounds after 14 days of treatment demonstrated inhibition of pro-inflammatory response (NF-kappaB p65, TNF-alpha, IL-1beta, IL-8 and IL-2) with improvement in anti-inflammatory response (IL-10), inhibited the elevated oxidative stress and decreased the concentrations of matrix metalloproteinases (MMP-2, -8 and -9) and increased the concentrations of TIMP-1 & TIMP- 2. syringic acid 4-6 matrix metallopeptidase 2 Rattus norvegicus 322-338 31506724-4 2019 Matrix metalloproteinase-2 (MMP-2) is a zinc and calcium-dependent protease that is activated by oxidative stress in myocardial IR injury and cleaves both intracellular and extracellular substrates. Calcium 49-56 matrix metallopeptidase 2 Rattus norvegicus 0-26 31506724-4 2019 Matrix metalloproteinase-2 (MMP-2) is a zinc and calcium-dependent protease that is activated by oxidative stress in myocardial IR injury and cleaves both intracellular and extracellular substrates. Calcium 49-56 matrix metallopeptidase 2 Rattus norvegicus 28-33 31220437-9 2019 The MMP-2 and MMP-9 activities were reduced in icariin treated groups. icariin 47-54 matrix metallopeptidase 2 Rattus norvegicus 4-9 30908945-0 2019 Alterations in myocardial connexin-43 and matrix metalloproteinase-2 signaling in response to pregnancy and oxygen deprivation of Wistar rats: a pilot study 1. Oxygen 108-114 matrix metallopeptidase 2 Rattus norvegicus 42-68 31461499-4 2019 METHODS: Rat cardiomyoblasts (H9C2 cells) were examined to determine whether high glucose can induce the expression of the two isoforms of MMP-2. Glucose 82-89 matrix metallopeptidase 2 Rattus norvegicus 139-144 31295411-6 2019 The folic acid treatment of diabetic rats did not change aminotransferase activity; it alleviated the increase in alkaline phosphatase and the decrease in albumin and fibrinogen concentration, and reduced MMP-2 activity; however, it increased urea and creatinine concentration. Folic Acid 4-14 matrix metallopeptidase 2 Rattus norvegicus 205-210 30900747-10 2019 RESULTS: TNF-alpha, IL-1beta, MMP-1, MMP-2 levels were significantly lower in AP + ALA group compared with AP group (P < 0.05). ap + ala 78-86 matrix metallopeptidase 2 Rattus norvegicus 37-42 31461499-9 2019 RESULTS: Quantitative RT-PCR and immunofluorescence staining showed that the two MMP-2 isoforms were strongly induced by high glucose stimulation in H9C2 cells. Glucose 126-133 matrix metallopeptidase 2 Rattus norvegicus 81-86 31167987-6 2019 In vitro experiments, we found that high glucose (HG) could increase the expression of CaSR, alpha-smooth muscle actin (alpha-SMA), transforming growth factor-beta1 (TGF-beta1) collagen I/III, matrix metalloproteinase-2 (MMP-2), MMP9, along with cardiac fibroblast migration and proliferation. Glucose 41-48 matrix metallopeptidase 2 Rattus norvegicus 193-219 31167987-6 2019 In vitro experiments, we found that high glucose (HG) could increase the expression of CaSR, alpha-smooth muscle actin (alpha-SMA), transforming growth factor-beta1 (TGF-beta1) collagen I/III, matrix metalloproteinase-2 (MMP-2), MMP9, along with cardiac fibroblast migration and proliferation. Glucose 41-48 matrix metallopeptidase 2 Rattus norvegicus 221-226 31085245-8 2019 Apart from their known PDE inhibition, up-regulation of vascular AMPK and eNOS coupled with down-regulation of Ang-II, ET-1, P-selectin, VCAM-1 and MMP-2 may explain vardenafil and cilostazol protective effect against RA/DM-co-morbidity-induced endothelial dysfunction and vascular reactivity defects. Vardenafil Dihydrochloride 166-176 matrix metallopeptidase 2 Rattus norvegicus 148-153 31364649-6 2019 Furthermore, we found that trans-THSG significantly down-regulated CCl4-induced excessive collagen secretion and increased the levels of desmin, MMP2 and MMP9 in rat liver tissues, suggesting that trans-THSG prevents liver fibrosis by attenuating the activation of hepatic stellate cells (HSCs) through the inhibition of Smad and ERK signaling pathways. trans-thsg 27-37 matrix metallopeptidase 2 Rattus norvegicus 145-149 31364649-6 2019 Furthermore, we found that trans-THSG significantly down-regulated CCl4-induced excessive collagen secretion and increased the levels of desmin, MMP2 and MMP9 in rat liver tissues, suggesting that trans-THSG prevents liver fibrosis by attenuating the activation of hepatic stellate cells (HSCs) through the inhibition of Smad and ERK signaling pathways. trans-thsg 197-207 matrix metallopeptidase 2 Rattus norvegicus 145-149 31067604-8 2019 On the other hand, expression of matrix metalloproteinase 2 of mesenteric arteries is reduced in HS group while expression of tissue inhibitors of metalloproteinase is increased, indicating that extra cellular matrix (ECM) is remodeled. hassio 97-99 matrix metallopeptidase 2 Rattus norvegicus 33-59 30977399-6 2019 Furthermore, expression of MMP-2, MMP-9, collagen type I, alpha-SMA, and TGF-beta downregulated in UA-administered rats. ursolic acid 99-101 matrix metallopeptidase 2 Rattus norvegicus 27-32 30977399-0 2019 Ursolic acid modulates MMPs, collagen-I, alpha-SMA, and TGF-beta expression in isoproterenol-induced myocardial infarction in rats. ursolic acid 0-12 matrix metallopeptidase 2 Rattus norvegicus 23-27 30444646-2 2019 Although the increased intracellular Zn2+ level ([Zn2+]i), oxidative stress, and altered cardiac matrix metalloproteinases (MMPs) in diabetic cardiomyopathy can intersect with different signaling pathways, the exact mechanisms are not known yet. Zinc 37-41 matrix metallopeptidase 2 Rattus norvegicus 124-128 30444646-10 2019 Overall, we showed that DAP has important antioxidant-like cardio-protective effects in MetS-rats, similar to INS-effect, affecting Zn2+-regulation via Zn2+-transporters, MMPs, and oxidative stress. dapagliflozin 24-27 matrix metallopeptidase 2 Rattus norvegicus 171-175 31205590-11 2019 MMP-2 and MMP-9 levels decreased more after pretreatment with CCNP than with CC. ccnp 62-66 matrix metallopeptidase 2 Rattus norvegicus 0-5 30474386-11 2019 The sirolimus mesh markedly suppressed MMP-2 and MMP-9 expression, decreased PCNA-positive cell numbers, inhibited RAAFC migration, and reduced phospho-mTOR levels. Sirolimus 4-13 matrix metallopeptidase 2 Rattus norvegicus 39-44 31082337-1 2019 Objective: To investigate the effect of anluohuaxianwan (ALHXW) using rat model of carbon tetrachloride (CCl(4)) induced liver fibrosis on the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Carbon Tetrachloride 83-103 matrix metallopeptidase 2 Rattus norvegicus 184-188 30339939-2 2019 Peroxynitrite may directly activate latent matrix metalloproteinase (MMP)-2 in vascular smooth muscle cells (VSMC) by its S-glutathiolation. Peroxynitrous Acid 0-13 matrix metallopeptidase 2 Rattus norvegicus 43-75 31082337-1 2019 Objective: To investigate the effect of anluohuaxianwan (ALHXW) using rat model of carbon tetrachloride (CCl(4)) induced liver fibrosis on the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Cefaclor 105-108 matrix metallopeptidase 2 Rattus norvegicus 184-188 31975775-4 2019 In a recent study, we demonstrated that folic acid (FA) treatment to cSCI rats reduced NP and improved functional recovery by repressing MMP-2 expression. Folic Acid 40-50 matrix metallopeptidase 2 Rattus norvegicus 137-142 31975775-8 2019 Purpose: Furthering our previous findings on inhibiting MMP-2 expression by FA in mid- and late- phase following cSCI in rats, we hypothesized that FA will methylate and suppress MMP-9 expression during the early- phase, day 1, 3, 7 post cSCI and mid- phase (day 18 post cSCI), in comparison with MMP-2 expression during mid- and the late-phase of cSCI. potassium methylate 156-165 matrix metallopeptidase 2 Rattus norvegicus 56-61 31975775-8 2019 Purpose: Furthering our previous findings on inhibiting MMP-2 expression by FA in mid- and late- phase following cSCI in rats, we hypothesized that FA will methylate and suppress MMP-9 expression during the early- phase, day 1, 3, 7 post cSCI and mid- phase (day 18 post cSCI), in comparison with MMP-2 expression during mid- and the late-phase of cSCI. potassium methylate 156-165 matrix metallopeptidase 2 Rattus norvegicus 297-302 30810635-9 2019 Treatment with 1 mg/kg gliclazide reduced myeloperoxidase activity, malondialdehyde, IL-1beta, and TNF-alpha levels (p<=0.05), and resulted in weak staining for COX-2, cathepsin k, MMP-2, RANK, RANKL, SOD-1, GPx-1,MIF and PI3k. Gliclazide 23-33 matrix metallopeptidase 2 Rattus norvegicus 184-189 30684466-9 2019 Morphine also altered the mRNA expression of fibrosis-related genes, TNF-alpha, MMP-2 and MMP-9. Morphine 0-8 matrix metallopeptidase 2 Rattus norvegicus 80-85 30169834-11 2019 MMP-2 and MMP-9 levels were significantly increased in BAPN-treated rats compared to the controls, but no statistical significance was found between rats with and without DA. Aminopropionitrile 55-59 matrix metallopeptidase 2 Rattus norvegicus 0-5 30549180-7 2019 Western blotting demonstrated that treatment with FKA down-regulated MMP-9 and MMP-2 and up-regulated TIMP-1 expression. flavokawain A 50-53 matrix metallopeptidase 2 Rattus norvegicus 79-84 30569164-9 2019 Myocardial cells under high glucose conditions treated with DDAH2 showed reductions in collagen I, MMP2 and TIMP2, indicating that DDAH2 reduced cell migration. Glucose 28-35 matrix metallopeptidase 2 Rattus norvegicus 99-103 30769782-2 2019 The current study examined the effects of AQU-118, an orally active inhibitor of metalloproteinase-2 (MMP-2) and MMP-9, in the spinal nerve ligation (SNL) rat model of neuropathic pain. AQU-118 42-49 matrix metallopeptidase 2 Rattus norvegicus 102-107 30769782-8 2019 Results demonstrate that oral dosing with the dual active, MMP-2/-9 inhibitor, AQU-118, attenuated mechanical allodynia while at the same time significantly reduced the levels of caspase-3 in the DRG. AQU-118 79-86 matrix metallopeptidase 2 Rattus norvegicus 59-67 30543783-9 2019 We found that the administration of MFA markedly decreased the levels of hyaluronic acid (HA), procollagen type III (PC-III), type IV collagen (CIV) and laminin (LN) in the serum, inhibited the expression of alpha-smooth muscle actin (alpha-SMA) as well as type I and type III collagen, and up-regulated the ratio of MMP-2/TIMP-1 in rats. mfa 36-39 matrix metallopeptidase 2 Rattus norvegicus 317-322 30367734-7 2019 Results showed collagen deposition and up-regulation of matrix metalloproteinases-MMP-2 and -9 in D-galactose-induced aging rats. Galactose 98-109 matrix metallopeptidase 2 Rattus norvegicus 82-94 30638989-8 2019 The TGF-beta1 and MMP-2 protein levels were attenuated by linagliptin in DPP-4-deficient cardiac fibroblasts. Linagliptin 58-69 matrix metallopeptidase 2 Rattus norvegicus 18-23 30528028-5 2019 In line with this cellular effect, the mRNA expression of two pro-migratory genes, including cell division cycle 42 (CDC42) and matrix metalloproteinase 2 (MMP2) was induced by TCDD treatment. Polychlorinated Dibenzodioxins 177-181 matrix metallopeptidase 2 Rattus norvegicus 128-154 30528028-5 2019 In line with this cellular effect, the mRNA expression of two pro-migratory genes, including cell division cycle 42 (CDC42) and matrix metalloproteinase 2 (MMP2) was induced by TCDD treatment. Polychlorinated Dibenzodioxins 177-181 matrix metallopeptidase 2 Rattus norvegicus 156-160 30536359-2 2019 The negative effects of formaldehyde were described using vascular endothelial growth factor (VEGF), matrix metallopeptidase 2 (MMP-2) and osteonectin antibodies involved in the extracellular matrix and angiogenetic development. Formaldehyde 24-36 matrix metallopeptidase 2 Rattus norvegicus 101-126 30686819-3 2019 Afterwards, intraperitoneal injection of these rats with 40 mg/kg GM6001 (a MMPs inhibitor). N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 66-72 matrix metallopeptidase 2 Rattus norvegicus 76-80 30686819-8 2019 Furthermore, we found that recombinant MMP2 and MMP9 triggered the cleavage of beta-dystroglycan in vitro, and this action could be inhibited by GM6001 administration. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 145-151 matrix metallopeptidase 2 Rattus norvegicus 39-43 31113607-0 2019 Celastrol Attenuates Intrahepatic Cholestasis of Pregnancy by Inhibiting Matrix Metalloproteinases-2 and 9. celastrol 0-9 matrix metallopeptidase 2 Rattus norvegicus 73-106 31113607-6 2019 RESULTS: In rats with ICP, both MMP-2 and -9 exhibited significantly elevated activities, which were inhibited by the administration of celastrol. celastrol 136-145 matrix metallopeptidase 2 Rattus norvegicus 32-44 31113607-9 2019 CONCLUSION: Our findings described for the first time the effects of celastrol to attenuate ICP symptoms through an inhibition of both MMP-2 and -9, providing evidence for a potential role of celastrol as a new drug for the treatment of ICP. celastrol 69-78 matrix metallopeptidase 2 Rattus norvegicus 135-147 31113607-9 2019 CONCLUSION: Our findings described for the first time the effects of celastrol to attenuate ICP symptoms through an inhibition of both MMP-2 and -9, providing evidence for a potential role of celastrol as a new drug for the treatment of ICP. celastrol 192-201 matrix metallopeptidase 2 Rattus norvegicus 135-147 31403269-15 2019 Doxorubicin injection increased caspase-3 protein expression, myocardium lipid hydroperoxide concentration, MMP-2 activity, phosphofructokinase and lactate dehydrogenase activity, and decreased beta-hydroxyacyl-CoA dehydrogenase, pyruvate dehydrogenase, citrate synthase, complex I, complex II and ATP synthase activity in myocardium. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 108-113 30399409-0 2019 Nitrite treatment downregulates vascular MMP-2 activity and inhibits vascular remodeling in hypertension independently of its antihypertensive effects. Nitrites 0-7 matrix metallopeptidase 2 Rattus norvegicus 41-46 30399409-2 2019 Given that impaired redox state activates matrix metalloproteinase (MMP)- 2 and promotes vascular remodeling, we hypothesized that nitrite treatment at a non-antihypertensive dose exerts antioxidant effects and attenuates both MMP-2 activation and vascular remodeling of hypertension. Nitrites 131-138 matrix metallopeptidase 2 Rattus norvegicus 42-75 30399409-2 2019 Given that impaired redox state activates matrix metalloproteinase (MMP)- 2 and promotes vascular remodeling, we hypothesized that nitrite treatment at a non-antihypertensive dose exerts antioxidant effects and attenuates both MMP-2 activation and vascular remodeling of hypertension. Nitrites 131-138 matrix metallopeptidase 2 Rattus norvegicus 227-232 30399409-14 2019 This response is mediated, at least in part, by XOR and is attributable to antioxidant effects of nitrite blunting vascular MMP-2 activation. Nitrites 98-105 matrix metallopeptidase 2 Rattus norvegicus 124-129 30662833-8 2019 VEGF, ICAM-1 and MMP2 induced by HG were also suppressed by 5-aza-dC treatment. Azacitidine 60-65 matrix metallopeptidase 2 Rattus norvegicus 17-21 31403269-18 2019 CONCLUSION: Doxorubicin induced left ventricular dysfunction, increases in oxidative stress, changes in myocardium metabolism and MMP-2 activation. Doxorubicin 12-23 matrix metallopeptidase 2 Rattus norvegicus 130-135 30393115-9 2019 Interestingly, both L and EU from HCB-treated rats exhibited higher estrogen receptor alpha (ERalpha) (immunohistochemistry) and metalloproteases (MMP)-2 and -9 levels (Western Blot), as well as lower progesterone receptor (PR) expression (immunohistochemistry) than in control rats. Hexachlorobenzene 34-37 matrix metallopeptidase 2 Rattus norvegicus 68-160 30536359-11 2019 When compared inflammation, MMP-2 and osteonectin expressions were significant (p < 0.01) in the formaldehyde group. Formaldehyde 97-109 matrix metallopeptidase 2 Rattus norvegicus 28-33 30536359-12 2019 CONCLUSIONS: It was suggested that formaldehyde toxicity decreased the expression of MMP-2 and in osteoblasts as well as affecting the retention of MMP levels in tooth cavity, which is very low in collagen fibres. Formaldehyde 35-47 matrix metallopeptidase 2 Rattus norvegicus 85-90 30536359-12 2019 CONCLUSIONS: It was suggested that formaldehyde toxicity decreased the expression of MMP-2 and in osteoblasts as well as affecting the retention of MMP levels in tooth cavity, which is very low in collagen fibres. Formaldehyde 35-47 matrix metallopeptidase 2 Rattus norvegicus 85-88 31168029-7 2019 Our results showed that ellagic acid significantly reduced protein expression of HDAC1, mRNA expression of collagen I, collagen III, MMP-2 and MMP-9 and the area of cardiac fibrosis in MI rats. Ellagic Acid 24-36 matrix metallopeptidase 2 Rattus norvegicus 133-138 30309728-2 2019 Matrix metalloproteinases-2/9 (MMP-2/9) have been shown to participate in the disruption of the BBB and hemorrhagic transformation after cerebral ischemia. 1-((2-HYDROXYETHOXY)METHYL)-5-(3-(BENZYLOXY)BENZYL)-6-HYDROXYPYRIMIDINE-2,4(1H,3H)-DIONE 96-99 matrix metallopeptidase 2 Rattus norvegicus 0-29 30309728-2 2019 Matrix metalloproteinases-2/9 (MMP-2/9) have been shown to participate in the disruption of the BBB and hemorrhagic transformation after cerebral ischemia. 1-((2-HYDROXYETHOXY)METHYL)-5-(3-(BENZYLOXY)BENZYL)-6-HYDROXYPYRIMIDINE-2,4(1H,3H)-DIONE 96-99 matrix metallopeptidase 2 Rattus norvegicus 31-38 31168029-8 2019 In Ang II-stimulated CFs, ellagic acid (60 mumol/L) decreased the protein expression of HDAC1, collagen I, collagen III, MMP-2 and MMP-9, and inhibited cell proliferation and migration. Ellagic Acid 26-38 matrix metallopeptidase 2 Rattus norvegicus 121-126 31168029-9 2019 Further, HDAC1 over-expression reversed the inhibitor effects of ellagic acid on proteins expression (collagen I, collagen III, MMP-2 and MMP-9) and proliferation and migration of CFs. Ellagic Acid 65-77 matrix metallopeptidase 2 Rattus norvegicus 128-133 30336141-0 2018 Hypertension, augmented activity of matrix metalloproteinases-2 and -9 and angiogenic imbalance in hypertensive pregnancy are attenuated by doxycycline. Doxycycline 140-151 matrix metallopeptidase 2 Rattus norvegicus 36-70 30336141-2 2018 Matrix metalloproteinases (MMPs) are involved in hypertension and doxycycline reduces blood pressure by inhibition of MMPs. Doxycycline 66-77 matrix metallopeptidase 2 Rattus norvegicus 27-31 30336141-2 2018 Matrix metalloproteinases (MMPs) are involved in hypertension and doxycycline reduces blood pressure by inhibition of MMPs. Doxycycline 66-77 matrix metallopeptidase 2 Rattus norvegicus 118-122 30336141-9 2018 Increased activity of placental MMP-2 and MMP-9 and uterine MMP-2 were attenuated by doxycycline. Doxycycline 85-96 matrix metallopeptidase 2 Rattus norvegicus 32-37 30336141-9 2018 Increased activity of placental MMP-2 and MMP-9 and uterine MMP-2 were attenuated by doxycycline. Doxycycline 85-96 matrix metallopeptidase 2 Rattus norvegicus 60-65 30336141-14 2018 Therefore, we suggest that L-NAME reduced NO and this triggered the increases in MMP-2 and -9 activities during hypertensive pregnancy. NG-Nitroarginine Methyl Ester 27-33 matrix metallopeptidase 2 Rattus norvegicus 81-93 30336141-15 2018 Importantly, increases in MMPs activation and angiogenic imbalance were attenuated by doxycycline and these effects were associated with decreases in systolic blood pressure. Doxycycline 86-97 matrix metallopeptidase 2 Rattus norvegicus 26-30 30308129-0 2018 Doxorubicin induces de novo expression of N-terminal-truncated matrix metalloproteinase-2 in cardiac myocytes. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 63-89 30308129-7 2018 MMP inhibitors ARP-100 or ONO-4817 (1 muM) prevented doxorubicin-induced MMP-2 activation. N-hydroxy-2-((4-phenylphenyl)sulfonylpropan-2-yloxyamino)acetamide 15-22 matrix metallopeptidase 2 Rattus norvegicus 73-78 30308129-7 2018 MMP inhibitors ARP-100 or ONO-4817 (1 muM) prevented doxorubicin-induced MMP-2 activation. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 26-34 matrix metallopeptidase 2 Rattus norvegicus 73-78 30308129-7 2018 MMP inhibitors ARP-100 or ONO-4817 (1 muM) prevented doxorubicin-induced MMP-2 activation. Doxorubicin 53-64 matrix metallopeptidase 2 Rattus norvegicus 73-78 30308129-8 2018 Doxorubicin also increased the levels and activity of MMP-2 secreted into the conditioned media. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 54-59 30308129-9 2018 Doxorubicin upregulated the mRNA expression of both full-length MMP-2 and NTT-MMP-2. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 64-69 30308129-9 2018 Doxorubicin upregulated the mRNA expression of both full-length MMP-2 and NTT-MMP-2. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 78-83 30308129-11 2018 Doxorubicin induces oxidative stress and stimulates a robust increase in MMP-2 expression and activity in NRVM, including NTT-MMP-2. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 73-78 30308129-11 2018 Doxorubicin induces oxidative stress and stimulates a robust increase in MMP-2 expression and activity in NRVM, including NTT-MMP-2. Doxorubicin 0-11 matrix metallopeptidase 2 Rattus norvegicus 126-131 30031694-10 2018 Further analysis revealed that fluoxetine alleviated both the increase of p53, MMP13, MMP2 and MMP9 and the decrease of pp53Ser15 and MDM2 in lungs and RV tissues of MCT-induced PAH rats. Fluoxetine 31-41 matrix metallopeptidase 2 Rattus norvegicus 86-90 30556894-8 2018 At 3 h, 24 h, 48 h, and 96 h after cerebral ischemia-reperfusion, the expressions of the MMP-2 protein and MMP-9 protein in the ischemic brain tissue were evidently increased, which were inhibited by retigabine. ezogabine 200-210 matrix metallopeptidase 2 Rattus norvegicus 89-94 30556894-10 2018 CONCLUSIONS: The regulatory roles of retigabine in the distribution and expressions of claudin-5, occludin, and ZO-1 may be associated with the inhibition of the expressions of the MMP-2, MMP-9, and PKCdelta proteins. ezogabine 37-47 matrix metallopeptidase 2 Rattus norvegicus 181-186 30408628-7 2018 Compared with untreated CIA rats, Lipo-DiMC treatments relieved paw-swellings, suppressed the increments of immunocytes numbers and inhibited DPPI and MMP-2/9 over-activity in blood. lipo-dimc 34-43 matrix metallopeptidase 2 Rattus norvegicus 151-158 30408628-10 2018 Lipo-DiMC exhibited its therapeutic functions by attenuating CIA development in rats, associated with down-regulating CIA-induced lymphocytes numbers, inhibiting over-expressed of DPPI and MMP-2/9, and adjusting cell cycles. lipo-dimc 0-9 matrix metallopeptidase 2 Rattus norvegicus 189-196 30193865-10 2018 In the PPE-induced model, Sal-B reduced induction of lung"s matrix metalloproteinase (MMP)-9 and MMP-2 activities by 59 and 94%, respectively, and restored pSTAT3 and VEGF expressions to the healthy lung levels, while leaving neutrophil accumulation unchecked [myeloperoxidase (MPO) activity]. salvianolic acid B 26-31 matrix metallopeptidase 2 Rattus norvegicus 97-102 29439623-8 2018 Additionally, aspirin also reversed T0070907-induced changes in the levels of thromboxane B2, vascular endothelial growth factor, soluble fms-like tyrosine kinase, and matrix metalloproteinase 2 in both maternal blood and placental tissue. Aspirin 14-21 matrix metallopeptidase 2 Rattus norvegicus 168-194 30257319-6 2018 Moreover, the expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 in rat heart were also inhibited by cycloastragenol. cycloastragenol 110-125 matrix metallopeptidase 2 Rattus norvegicus 29-55 29439623-8 2018 Additionally, aspirin also reversed T0070907-induced changes in the levels of thromboxane B2, vascular endothelial growth factor, soluble fms-like tyrosine kinase, and matrix metalloproteinase 2 in both maternal blood and placental tissue. T 0070907 36-44 matrix metallopeptidase 2 Rattus norvegicus 168-194 30517321-0 2018 Oxymatrine alleviates periodontitis in rats by inhibiting inflammatory factor secretion and regulating MMPs/TIMP protein expression1. oxymatrine 0-10 matrix metallopeptidase 2 Rattus norvegicus 103-107 30171854-10 2018 Trans-resveratrol increased A1AR and A2AAR expression, cellular PLC, pERK1/2 levels and MMP-2, tPA and uPA secretion by HTMC. Resveratrol 0-17 matrix metallopeptidase 2 Rattus norvegicus 88-93 30171854-12 2018 In conclusion, IOP lowering effect of trans-resveratrol involves upregulation of A1AR expression, PLC and ERK1/2 activation and increased MMP-2 secretion. Resveratrol 38-55 matrix metallopeptidase 2 Rattus norvegicus 138-143 30257319-6 2018 Moreover, the expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 in rat heart were also inhibited by cycloastragenol. cycloastragenol 110-125 matrix metallopeptidase 2 Rattus norvegicus 57-62 30066023-0 2018 Glibenclamide protects against thioacetamide-induced hepatic damage in Wistar rat: investigation on NLRP3, MMP-2, and stellate cell activation. Glyburide 0-13 matrix metallopeptidase 2 Rattus norvegicus 107-112 29377254-7 2018 Retinoic acid, an agonist of GnT-V, further increased glycosylated CD147, and activated matrix metalloproteinase-2/-9 (MMP-2 and MMP-9) in the hypertrophied left ventricle of 2K1C rat. Tretinoin 0-13 matrix metallopeptidase 2 Rattus norvegicus 88-117 29377254-7 2018 Retinoic acid, an agonist of GnT-V, further increased glycosylated CD147, and activated matrix metalloproteinase-2/-9 (MMP-2 and MMP-9) in the hypertrophied left ventricle of 2K1C rat. Tretinoin 0-13 matrix metallopeptidase 2 Rattus norvegicus 119-124 30066023-12 2018 GLB treatment significantly downregulated the expressions of TGF-beta1, alpha-SMA, NLRP3, ASC, caspase-1, and IL-1beta, and upregulated MMP-2 and catalase against TAA-induced liver damage. Glyburide 0-3 matrix metallopeptidase 2 Rattus norvegicus 136-154 30239560-0 2018 LncRNA-HOTAIR inhibition aggravates oxidative stress-induced H9c2 cells injury through suppression of MMP2 by miR-125. mir-125 110-117 matrix metallopeptidase 2 Rattus norvegicus 102-106 30459606-8 2018 Astilbin treatment also attenuated HG-induced decrease in expression of matrix metalloproteinase (MMP)-2 and MMP-9. astilbin 0-8 matrix metallopeptidase 2 Rattus norvegicus 72-104 30347737-0 2018 Hesperidin Prevents Nitric Oxide Deficiency-Induced Cardiovascular Remodeling in Rats via Suppressing TGF-beta1 and MMPs Protein Expression. Hesperidin 0-10 matrix metallopeptidase 2 Rattus norvegicus 116-120 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. NG-Nitroarginine Methyl Ester 229-235 matrix metallopeptidase 2 Rattus norvegicus 137-163 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. NG-Nitroarginine Methyl Ester 229-235 matrix metallopeptidase 2 Rattus norvegicus 165-170 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. Hesperidin 254-264 matrix metallopeptidase 2 Rattus norvegicus 137-163 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. Hesperidin 254-264 matrix metallopeptidase 2 Rattus norvegicus 165-170 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. Captopril 268-277 matrix metallopeptidase 2 Rattus norvegicus 137-163 30347737-7 2018 Furthermore, up-regulation of tumor necrosis factor receptor type 1 (TNF-R1) and TGF- beta1 protein expression and the overexpression of matrix metalloproteinase-2 (MMP-2) and matrix metalloproteinase-9 (MMP-9) was suppressed in l-NAME rats treated with hesperidin or captopril. Captopril 268-277 matrix metallopeptidase 2 Rattus norvegicus 165-170 29774825-3 2018 Because dietary zinc (Zn) improved recovery in nonblast mTBI models, and the MMPs are Zn-requiring enzymes, we evaluated the effects of low- (LoZn) and adequate-Zn (AdZn) diets on MMP expression and behavioral responses, subsequent to exposure to a single blast. Zinc 86-88 matrix metallopeptidase 2 Rattus norvegicus 77-81 29774825-9 2018 Taken together, our results support a relationship between marginally Zn-deficient status and a compromised regenerative response post-injury in muscle, likely through the MMP pathway. Zinc 70-72 matrix metallopeptidase 2 Rattus norvegicus 172-175 29774825-10 2018 However, in neuronal tissue, changes in MMP/TIMP levels after blast indicate a variable response to marginally Zn-deficient diets that may help explain compromised repair mechanism(s) previously associated with the systemic hypozincemia that develops in patients with TBI. Zinc 111-113 matrix metallopeptidase 2 Rattus norvegicus 40-43 30239560-9 2018 Meanwhile, MMP2 was identified as a target of miR-125. mir-125 46-53 matrix metallopeptidase 2 Rattus norvegicus 11-15 30239560-10 2018 MMP2 knockdown blocked miR-125 inhibitors" protect effect on H9c2 cells in oxidative stress. mir-125 23-30 matrix metallopeptidase 2 Rattus norvegicus 0-4 30443948-1 2018 The present study investigated the therapeutic potential of omega-6 fatty acids, according to their effects on antioxidant markers and matrix metalloproteinases (MMPs), in coronary heart disease-induced rats. Fatty Acids, Omega-6 60-79 matrix metallopeptidase 2 Rattus norvegicus 162-166 29957017-6 2018 High glucose treatment or IGF-1R overexpression increased matrix metalloproteinase (MMP)-2/MMP-9 expression, alpha-smooth muscle actin (alpha-SMA), and collagen type I expression in cardiac fibroblasts. Glucose 5-12 matrix metallopeptidase 2 Rattus norvegicus 58-90 29957017-7 2018 In contrast, berberine treatment significantly inhibited IGF-1R expression and exerted an antifibrotic effect in high glucose-cultured cardiac fibroblasts, as manifested by decreased MMP-2/MMP-9, alpha-SMA, and collagen type I expression, whereas IGF-1R siRNA plus berberine treatment did not further enhance this antifibrotic effect compared with berberine treatment alone. Berberine 13-22 matrix metallopeptidase 2 Rattus norvegicus 183-188 29957017-8 2018 Taken together, long-term berberine treatment ameliorates cardiac fibrosis and dysfunction by downregulating IGF-1R expression in cardiac fibroblasts and subsequently reducing MMP-2/MMP-9, alpha-SMA, and collagen type I expression in diabetic hearts. Berberine 26-35 matrix metallopeptidase 2 Rattus norvegicus 176-181 30019466-11 2018 To investigate the mechanism of the effect of TMZ on CR, we pretreated H9c2 cells with H2 O2 and found that TMZ treatment markedly decreased H2 O2 -induced MMP-2 and MMP-9 expression. Trimetazidine 108-111 matrix metallopeptidase 2 Rattus norvegicus 156-161 30019466-11 2018 To investigate the mechanism of the effect of TMZ on CR, we pretreated H9c2 cells with H2 O2 and found that TMZ treatment markedly decreased H2 O2 -induced MMP-2 and MMP-9 expression. Hydrogen Peroxide 141-146 matrix metallopeptidase 2 Rattus norvegicus 156-161 29957017-0 2018 Antifibrotic cardioprotection of berberine via downregulating myocardial IGF-1 receptor-regulated MMP-2/MMP-9 expression in diabetic rats. Berberine 33-42 matrix metallopeptidase 2 Rattus norvegicus 98-103 30443948-14 2018 Furthermore, omega-6 fatty acids significantly downregulated MMP-2 and MMP-9 expression in our coronary heart disease-induced rat model. Fatty Acids, Omega-6 13-32 matrix metallopeptidase 2 Rattus norvegicus 61-66 30140998-3 2018 Our present study revealed that an industrial chemical, bisphenol S (BPS), can promote the migration and invasion of PCC PC12 cells, which was evidenced by the upregulation of fibronectin (FN) and matrix metalloproteinases (MMP-2 and MMP-9). bis(4-hydroxyphenyl)sulfone 56-67 matrix metallopeptidase 2 Rattus norvegicus 224-229 30140998-3 2018 Our present study revealed that an industrial chemical, bisphenol S (BPS), can promote the migration and invasion of PCC PC12 cells, which was evidenced by the upregulation of fibronectin (FN) and matrix metalloproteinases (MMP-2 and MMP-9). bis(4-hydroxyphenyl)sulfone 69-72 matrix metallopeptidase 2 Rattus norvegicus 224-229 29453608-7 2018 The study revealed that the expression of VEGF, MMP-2, MMP-9, and the chemokine MCP-1 to be very high in DMBA and DMBA + LPS groups, while Bcl-2 also shows an elevated expression. 9,10-Dimethyl-1,2-benzanthracene 105-109 matrix metallopeptidase 2 Rattus norvegicus 48-53 29453608-7 2018 The study revealed that the expression of VEGF, MMP-2, MMP-9, and the chemokine MCP-1 to be very high in DMBA and DMBA + LPS groups, while Bcl-2 also shows an elevated expression. 9,10-Dimethyl-1,2-benzanthracene 114-118 matrix metallopeptidase 2 Rattus norvegicus 48-53 30233326-6 2018 Our results showed that ischemia produced BBB damage and MMP-2/9 upregulation was colocalized with Rhodamine-dextran leakage. Rhodamines 99-108 matrix metallopeptidase 2 Rattus norvegicus 57-62 29932881-6 2018 In this study, abovine serum albumin (BSA)-overload rat model was first established and collagen deposition and deficient autophagic response were observed in vivo, and stimulation with albumin nanoparticles resulted in MMP-2 overactivation and obstructed autophagic flux induced by lysosomal dysfunction in vitro. abovine 15-22 matrix metallopeptidase 2 Rattus norvegicus 220-225 30102955-10 2018 CEPO-Fc treatment prevented the elevation of hippocampal of P38, ERK, MMP-2 activity and also Akt/GSK-3beta signaling impairment induced by Abeta25-35 but it had no effect on JNK. cepo-fc 0-7 matrix metallopeptidase 2 Rattus norvegicus 70-75 30233326-6 2018 Our results showed that ischemia produced BBB damage and MMP-2/9 upregulation was colocalized with Rhodamine-dextran leakage. Dextrans 109-116 matrix metallopeptidase 2 Rattus norvegicus 57-62 30186462-0 2018 Morroniside protects against cerebral ischemia/reperfusion injury by inhibiting neuron apoptosis and MMP2/9 expression. morroniside 0-11 matrix metallopeptidase 2 Rattus norvegicus 101-107 30229846-11 2018 After mifepristone intervention, the protein levels of TNF-alpha, IL-1beta, IL-6, MMP-2, and MMP-9 in the infarcted brain tissues of rats were markedly decreased, while the expression of the TIMP-1 protein was increased. Mifepristone 6-18 matrix metallopeptidase 2 Rattus norvegicus 82-87 30186462-1 2018 The aim of the present study was to investigate the effect of morroniside against matrix metalloproteinase (MMP)2/9 and focal cerebral ischemia/reperfusion (I/R) injury in rats. morroniside 62-73 matrix metallopeptidase 2 Rattus norvegicus 82-115 30186462-8 2018 The inhibitory effect of morroniside on MMP2/9 expression and neuron apoptosis was dose dependent. morroniside 25-36 matrix metallopeptidase 2 Rattus norvegicus 40-46 30186462-6 2018 However, treatment with morroniside significantly inhibited I/R-induced MMP2/9 expression and neuron apoptosis compared with the untreated I/R injury group. morroniside 24-35 matrix metallopeptidase 2 Rattus norvegicus 72-76 29353381-11 2018 Kaempferol at highest dose showed reduction in pro-MMP-2 expression and MMP-9 level. kaempferol 0-10 matrix metallopeptidase 2 Rattus norvegicus 51-56 30713757-5 2018 Conclusion: These findings indicate that ethanol-induced kidney abnormalities may be in part associated with alteration in expressions of VEGFRs, nephrin, and podocin and in increasing activities of MMP2 and MMP9 as key molecular mediators in the kidney function. Ethanol 41-48 matrix metallopeptidase 2 Rattus norvegicus 199-203 30174499-0 2018 Plumbagin inhibits neuronal apoptosis, intimal hyperplasia and also suppresses TNF-alpha/NF-kappaB pathway induced inflammation and matrix metalloproteinase-2/9 expression in rat cerebral ischemia. plumbagin 0-9 matrix metallopeptidase 2 Rattus norvegicus 132-160 30174499-11 2018 Overall, the results reveal the potent neuroprotective efficacy of plumbagin against I/R-induced brain injury via effectively modulating apoptotic pathways, MMPs and neuro-inflammatory cascades. plumbagin 67-76 matrix metallopeptidase 2 Rattus norvegicus 157-161 29926827-8 2018 Our results demonstrated that following implantation of CGM after surgical brain trauma, significant increases in MMP2+/SOX2+ cells and MMP9+/SOX2+ cells were seen within the lesion boundary zone in the L + CGM group. cgm 56-59 matrix metallopeptidase 2 Rattus norvegicus 114-118 29704151-12 2018 Treatment of sulforaphane, likewise, decreased sciatic nerve malondialdehyde, nitric oxide, interleukin-6, and matrix metalloproteinase-2 and -9 contents. sulforaphane 13-25 matrix metallopeptidase 2 Rattus norvegicus 111-144 29704151-19 2018 Treatment of sulforaphane, likewise, decreased sciatic nerve malondialdehyde, nitric oxide, interleukin-6, matrix metalloproteinase-2 and -9 contents. sulforaphane 13-25 matrix metallopeptidase 2 Rattus norvegicus 107-140 29926706-7 2018 In addition, the ID-CBT5101 treatments inhibited the mRNA expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases (i.e., MMP-2, MMP-3, MMP-9, MMP-13, TIMP-1, and TIMP-2). cbt5101 20-27 matrix metallopeptidase 2 Rattus norvegicus 149-154 29562216-8 2018 A significant increase was detected in MMP-2, MMP-9 levels and MMP-2/TIMP-2 ratio in DMH group as compared with controls and treatment groups. 1,2-Dimethylhydrazine 85-88 matrix metallopeptidase 2 Rattus norvegicus 39-44 29562216-8 2018 A significant increase was detected in MMP-2, MMP-9 levels and MMP-2/TIMP-2 ratio in DMH group as compared with controls and treatment groups. 1,2-Dimethylhydrazine 85-88 matrix metallopeptidase 2 Rattus norvegicus 63-68 29562216-9 2018 In immunohistochemical evaluations, there was an increase in intensity and extent of staining of MMP-2 and MMP-9 in DMH group as compared to controls and treatment groups. 1,2-Dimethylhydrazine 116-119 matrix metallopeptidase 2 Rattus norvegicus 97-102 29380561-8 2018 RESULTS: Compared to the control group, the CIH group showed higher interstitial collagen fraction, increased MMP-9, miR-21, and p-ERK1/2 levels, and decreased MMP-2 and Spry1 levels. cih 44-47 matrix metallopeptidase 2 Rattus norvegicus 160-165 29380561-9 2018 Doxycycline treatment attenuated CIH-induced atrial fibrosis, reduced MMP-2, MMP-9, miR-21, and p-ERK1/2, and increased Spry1. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 70-75 29417224-10 2018 Gelatin zymography showed dietary iron restriction decreased both renal MMP-2 and MMP-9 activities in SHR-SP at 15 weeks old. Iron 34-38 matrix metallopeptidase 2 Rattus norvegicus 72-77 29417224-12 2018 Furthermore, dietary iron restriction decreased renal fibrosis, renal MMP-2 and MMP-9 activities, renal TGFbeta-RI expression, and Smad2 phosphorylation in rats with unilateral ureteral obstruction. Iron 21-25 matrix metallopeptidase 2 Rattus norvegicus 70-75 29749525-0 2018 Quercetin protects against inflammation, MMP-2 activation and apoptosis induction in rat model of cardiopulmonary resuscitation through modulating Bmi-1 expression. Quercetin 0-9 matrix metallopeptidase 2 Rattus norvegicus 41-46 29749525-6 2018 Treatment with quercetin significantly inhibited ROS generation, inflammation and MMP-2 protein expression in the rat model CPR. Quercetin 15-24 matrix metallopeptidase 2 Rattus norvegicus 82-87 29749525-8 2018 The results demonstrated that quercetin protects against inflammation, MMP-2 activation and apoptosis induction in a rat model of CPR, and that this may be mediated by modulating Bmi-1 expression. Quercetin 30-39 matrix metallopeptidase 2 Rattus norvegicus 71-76 29547743-4 2018 Our data demonstrated that the proliferation, migration and MMP-2 expressions of ASMCs were inhibited by CDAE or CDE; the protein expressions of p38, Bcl-2 and FAK in ASMCs were substantially reduced by CDAE and CDE detected by western blotting or immunocytochemistry; also the increased calcium influx has been observed instantaneously after ASMCs were stimulated by CDAE or CDE. asmcs 81-86 matrix metallopeptidase 2 Rattus norvegicus 60-65 29547743-4 2018 Our data demonstrated that the proliferation, migration and MMP-2 expressions of ASMCs were inhibited by CDAE or CDE; the protein expressions of p38, Bcl-2 and FAK in ASMCs were substantially reduced by CDAE and CDE detected by western blotting or immunocytochemistry; also the increased calcium influx has been observed instantaneously after ASMCs were stimulated by CDAE or CDE. cdae 105-109 matrix metallopeptidase 2 Rattus norvegicus 60-65 29547743-4 2018 Our data demonstrated that the proliferation, migration and MMP-2 expressions of ASMCs were inhibited by CDAE or CDE; the protein expressions of p38, Bcl-2 and FAK in ASMCs were substantially reduced by CDAE and CDE detected by western blotting or immunocytochemistry; also the increased calcium influx has been observed instantaneously after ASMCs were stimulated by CDAE or CDE. cdae 203-207 matrix metallopeptidase 2 Rattus norvegicus 60-65 29547743-4 2018 Our data demonstrated that the proliferation, migration and MMP-2 expressions of ASMCs were inhibited by CDAE or CDE; the protein expressions of p38, Bcl-2 and FAK in ASMCs were substantially reduced by CDAE and CDE detected by western blotting or immunocytochemistry; also the increased calcium influx has been observed instantaneously after ASMCs were stimulated by CDAE or CDE. cdae 203-207 matrix metallopeptidase 2 Rattus norvegicus 60-65 29086909-6 2018 Finally, extracellular acidification increased the expression of c-jun and MMP-2/9, and these effects were blocked by the Ca2+ chelator BAPTA-AM, P38 MAPK inhibitor SB203580, and ASIC1a-specific blocker PcTx-1, but not the ERK1/2 inhibitor PD98059. 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester 136-144 matrix metallopeptidase 2 Rattus norvegicus 75-82 29086909-6 2018 Finally, extracellular acidification increased the expression of c-jun and MMP-2/9, and these effects were blocked by the Ca2+ chelator BAPTA-AM, P38 MAPK inhibitor SB203580, and ASIC1a-specific blocker PcTx-1, but not the ERK1/2 inhibitor PD98059. SB 203580 165-173 matrix metallopeptidase 2 Rattus norvegicus 75-82 29632167-6 2018 We found that exposing isolated rat brain capillaries to glutamate increased MMP-2 and MMP-9 protein and activity levels, and decreased tight junction protein levels, which resulted in barrier leakage. Glutamic Acid 57-66 matrix metallopeptidase 2 Rattus norvegicus 77-82 29853950-5 2018 In vitro, astragalosides inhibited the activation of HSC and regulated the expression of MMP-2 and TIMP-2 and reduced the formation of collagen fibers. astragalosides 10-24 matrix metallopeptidase 2 Rattus norvegicus 89-94 28820947-1 2018 We evaluated the effects of ethanol consumption on the mitogen-activated protein kinases (MAPK) and metalloproteinases (MMP) pathways in the rat cavernosal smooth muscle (CSM). Ethanol 28-35 matrix metallopeptidase 2 Rattus norvegicus 120-123 29850586-6 2018 Mechanistically, PCB pretreatment inhibited the activation of MMP-2 and MMP-9 and degradation of tight junction proteins (TJPs) occludin and claudin-5 in the ischemic hemisphere. pinocembrin 17-20 matrix metallopeptidase 2 Rattus norvegicus 62-67 29425960-0 2018 Quercetin decreases the activity of matrix metalloproteinase-2 and ameliorates vascular remodeling in renovascular hypertension. Quercetin 0-9 matrix metallopeptidase 2 Rattus norvegicus 36-62 29425960-2 2018 As quercetin is an important flavonoid with significant antioxidant effects, the hypothesis here is that quercetin will reduce increased MMP-2 activity by decreasing oxidative stress in aortas of hypertensive rats and then ameliorate hypertension-induced vascular remodeling. Quercetin 3-12 matrix metallopeptidase 2 Rattus norvegicus 137-142 29425960-2 2018 As quercetin is an important flavonoid with significant antioxidant effects, the hypothesis here is that quercetin will reduce increased MMP-2 activity by decreasing oxidative stress in aortas of hypertensive rats and then ameliorate hypertension-induced vascular remodeling. Quercetin 105-114 matrix metallopeptidase 2 Rattus norvegicus 137-142 29425960-13 2018 CONCLUSIONS: Quercetin reduces hypertension-induced vascular remodeling, oxidative stress and MMP-2 activity in aortas. Quercetin 13-22 matrix metallopeptidase 2 Rattus norvegicus 94-99 29674965-4 2018 Based on these results, a 568-membered focused library of imidazole and thiazole compounds was generated in silico and then the library members were docked to the 3D model of MMP-2 followed by an in vitro medium throughput screening (MTS) based on a fluorescent assay employing MMP-2 catalytic domain. imidazole 58-67 matrix metallopeptidase 2 Rattus norvegicus 175-180 29674965-4 2018 Based on these results, a 568-membered focused library of imidazole and thiazole compounds was generated in silico and then the library members were docked to the 3D model of MMP-2 followed by an in vitro medium throughput screening (MTS) based on a fluorescent assay employing MMP-2 catalytic domain. Thiazoles 72-80 matrix metallopeptidase 2 Rattus norvegicus 175-180 29674965-8 2018 This is the first demonstration that imidazole and thiazole carboxylic acid-based compounds are more efficacious MMP-2 inhibitor than their hydroxamic acid derivatives. imidazole 37-46 matrix metallopeptidase 2 Rattus norvegicus 113-118 29674965-8 2018 This is the first demonstration that imidazole and thiazole carboxylic acid-based compounds are more efficacious MMP-2 inhibitor than their hydroxamic acid derivatives. Thiazole-2-carboxylic acid 51-75 matrix metallopeptidase 2 Rattus norvegicus 113-118 29674965-8 2018 This is the first demonstration that imidazole and thiazole carboxylic acid-based compounds are more efficacious MMP-2 inhibitor than their hydroxamic acid derivatives. Hydroxamic Acids 140-155 matrix metallopeptidase 2 Rattus norvegicus 113-118 29674965-9 2018 MMPI-1154 is a promising novel cardio-cytoprotective imidazole-carboxylic acid MMP-2 inhibitor lead candidate for the treatment of acute myocardial infarction. MMPI-1154 0-9 matrix metallopeptidase 2 Rattus norvegicus 79-84 29674965-9 2018 MMPI-1154 is a promising novel cardio-cytoprotective imidazole-carboxylic acid MMP-2 inhibitor lead candidate for the treatment of acute myocardial infarction. imidazole-carboxylic acid 53-78 matrix metallopeptidase 2 Rattus norvegicus 79-84 29411262-4 2018 reduced MA-induced mechanical allodynia and multiple methane treatments blocked activation of glial cells, decreased IL-1beta and TNF-alpha production and MMP-2 activity, and upregulated IL-10 expression in the spinal cord on day 10 post-MA. Methane 53-60 matrix metallopeptidase 2 Rattus norvegicus 155-160 29212295-3 2018 In aged rats, the oral administration of BPE (200 mg kg-1 day-1) for 8 weeks significantly reduced the mRNA and protein expression of interleukin-1beta, nuclear factor-kappa B, matrix metalloproteinase (MMP)-2, and MMP-8 in gingival tissues (p < 0.01). 1,2-bis(4-pyridyl)ethene 41-44 matrix metallopeptidase 2 Rattus norvegicus 177-209 29504102-0 2018 Role of Matrix Metalloproteinase-2 in the Development of Cyclophosphamide-Induced Cardiomyopathy. Cyclophosphamide 57-73 matrix metallopeptidase 2 Rattus norvegicus 8-34 29504102-1 2018 Immunohistochemical assay was employed to determine localization of MMP-2 in cardiomyocytes of WAG rats and changes in MMP-2 expression during modeled cardiomyopathy induced by single intraperitoneal injection of cyclophosphamide (125 mg/kg) alone or in combination with preventive intraperitoneal administration of an equal dose of asparcam-L (potassium-magnesium asparaginate) 30 min prior to the cytostatic. Cyclophosphamide 213-229 matrix metallopeptidase 2 Rattus norvegicus 119-124 28820947-5 2018 Additionally, ethanol consumption decreased the expression of MMP-2. Ethanol 14-21 matrix metallopeptidase 2 Rattus norvegicus 62-67 29504102-3 2018 During the development of cyclophosphamide-induced cardiomyopathy (in 3 days after injection), the index of MMP-2-positive cardiomyocyte nuclei increased by 76%. Cyclophosphamide 26-42 matrix metallopeptidase 2 Rattus norvegicus 108-113 29504102-5 2018 Preventive injection of asparcam-L moderated the cardiotoxic effect of cyclophosphamide, which manifested in less pronounced increase in the volume density of cardiomyocytes with lytic changes (by 42%) and index of MMP-2+ cardiomyocyte nuclei (by 23%) in comparison with the rats exposed to cyclophosphamide alone. asparcam-l 24-34 matrix metallopeptidase 2 Rattus norvegicus 215-220 29504102-5 2018 Preventive injection of asparcam-L moderated the cardiotoxic effect of cyclophosphamide, which manifested in less pronounced increase in the volume density of cardiomyocytes with lytic changes (by 42%) and index of MMP-2+ cardiomyocyte nuclei (by 23%) in comparison with the rats exposed to cyclophosphamide alone. Cyclophosphamide 71-87 matrix metallopeptidase 2 Rattus norvegicus 215-220 28820947-7 2018 Treatment with ethanol decreased MMP-2 activity, but did not change net MMP activity in the rat CSM. Ethanol 15-22 matrix metallopeptidase 2 Rattus norvegicus 33-38 28820947-7 2018 Treatment with ethanol decreased MMP-2 activity, but did not change net MMP activity in the rat CSM. Ethanol 15-22 matrix metallopeptidase 2 Rattus norvegicus 33-36 28820947-8 2018 Ethanol consumption increased the circulating levels of MMP-2, MMP-9, and TIMP-2 as well as the MMP-9/TIMP-1 ratio. Ethanol 0-7 matrix metallopeptidase 2 Rattus norvegicus 56-61 28820947-9 2018 The major finding of our study is that ethanol consumption down-regulates both MAPK and MMP pathways in the rat CSM, whereas it increases the circulating levels of MMP-9. Ethanol 39-46 matrix metallopeptidase 2 Rattus norvegicus 88-91 29321035-11 2018 SB431542 significantly reduced the expression of pro-fibrotic molecules (TGF-beta, Smad3, Smad2, a-SMA) and increased anti-fibrotic factor MMP2. 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide 0-8 matrix metallopeptidase 2 Rattus norvegicus 139-143 29489916-3 2018 Zymographic tests showed a decrease of MMP-2 activity in BALF in rats pretreated only with high concentration of tiotropium. Tiotropium Bromide 113-123 matrix metallopeptidase 2 Rattus norvegicus 39-44 29636780-5 2018 Moreover, we found that HACE treatment could on one hand inhibit oxidative stress in DN rats through regulating enzymatic activity for scavenging reactive oxygen species and on the other hand increase the ECM degradation through regulating the activity of metalloproteinase-2 (MMP-2) and the expression of tissue transglutaminase (tTG), which explained why HACE treatment inhibited ECM accumulation. hace 24-28 matrix metallopeptidase 2 Rattus norvegicus 277-282 29287196-11 2018 MEMC treatment significantly decreased Cox-2, VEGF, HDAC and MMP-2,-9 and increased Casp-3,-8 as compared to DENAgroup,which demonstrated that the anticancer effect of MEMC may be through the inhibition of angiogenesis, proliferation and metastasis and the activation of apoptosis. Mercury, chloro(2-methoxyethyl)- 0-4 matrix metallopeptidase 2 Rattus norvegicus 61-69 29287196-11 2018 MEMC treatment significantly decreased Cox-2, VEGF, HDAC and MMP-2,-9 and increased Casp-3,-8 as compared to DENAgroup,which demonstrated that the anticancer effect of MEMC may be through the inhibition of angiogenesis, proliferation and metastasis and the activation of apoptosis. Mercury, chloro(2-methoxyethyl)- 168-172 matrix metallopeptidase 2 Rattus norvegicus 61-69 29489916-10 2018 The combination of tiotropium with budesonide inhibits cadmium-induced inflammatory injuries with a synergistic interaction on MMP-2 and MMP-9 activity and airway hyper-responsiveness. Tiotropium Bromide 19-29 matrix metallopeptidase 2 Rattus norvegicus 127-132 29489916-10 2018 The combination of tiotropium with budesonide inhibits cadmium-induced inflammatory injuries with a synergistic interaction on MMP-2 and MMP-9 activity and airway hyper-responsiveness. Budesonide 35-45 matrix metallopeptidase 2 Rattus norvegicus 127-132 28887194-6 2018 Increases in HIF-1alpha and VEGF proteins and activation of MMP-2 in the hippocampus were also observed in the hippocamp of isoflurane-exposed rats compared with control rats. Isoflurane 124-134 matrix metallopeptidase 2 Rattus norvegicus 60-65 28887194-7 2018 Pharmacological inhibition of HIF-1alpha activation by 3-(5"-hydroxymethyl-2"-furyl)-1-benzylindazole (YC-1) markedly suppressed the expression of HIF-1alpha, VEGF and MMP-2, and mitigated the severity of BBB disruption.YC-1 pretreatment also significantly attenuated isoflurane-induced cognitive deficits in the Morris water maze task. 3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole 55-101 matrix metallopeptidase 2 Rattus norvegicus 168-173 29434760-5 2018 Furthermore, gambogic acid reduced inducible nitric oxide synthase (iNOS), matrix metalloproteinase (MMP)-2, MMP-9, intercellular adhesion molecule-1 (ICAM-1), nuclear factor (NF)-kappaB/p65 and phosphorylated p38 protein in ischemic myocardial tissue of MI rats. gambogic acid 13-26 matrix metallopeptidase 2 Rattus norvegicus 75-107 29434760-6 2018 In conclusion, gambogic acid exerted anti-inflammatory effects in MI rats by targeting the iNOS, MMPs, ICAM-1, NF-kappaB and p38 pathways. gambogic acid 15-28 matrix metallopeptidase 2 Rattus norvegicus 97-101 29321035-12 2018 CONCLUSION: TGF-betaRI inhibitor (SB431542) inhibits the downstream signaling molecules of TGF-beta and upregulates MMP2, which in turn prevent collagen deposition. 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide 34-42 matrix metallopeptidase 2 Rattus norvegicus 116-120 29976082-6 2018 Furthermore, glycyrrhizin arginine salt significantly reduced the expression of transforming growth factor [Formula: see text]1 (TGF-[Formula: see text]1), [Formula: see text]-smooth muscle actin, tumor necrosis factor-[Formula: see text] and matrix metalloproteinases 2 and 9. glycyrrhizin arginine salt 13-39 matrix metallopeptidase 2 Rattus norvegicus 243-276 29378386-0 2018 Stachydrine ameliorates carbon tetrachloride-induced hepatic fibrosis by inhibiting inflammation, oxidative stress and regulating MMPs/TIMPs system in rats. stachydrine 0-11 matrix metallopeptidase 2 Rattus norvegicus 130-134 28987762-2 2018 Doxycycline (Dc) belongs to the tetracycline-class of antibiotics with demonstrated beneficial molecular effects in the brain and heart, mainly through matrix metalloproteinases inhibition (MMP). Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 190-193 28987762-2 2018 Doxycycline (Dc) belongs to the tetracycline-class of antibiotics with demonstrated beneficial molecular effects in the brain and heart, mainly through matrix metalloproteinases inhibition (MMP). Doxycycline 13-15 matrix metallopeptidase 2 Rattus norvegicus 190-193 28987762-2 2018 Doxycycline (Dc) belongs to the tetracycline-class of antibiotics with demonstrated beneficial molecular effects in the brain and heart, mainly through matrix metalloproteinases inhibition (MMP). Tetracycline 32-44 matrix metallopeptidase 2 Rattus norvegicus 190-193 28987762-11 2018 In vitro, total MMP activity was augmented in I/R and inhibited by 25 and 50muM Dc. Doxycycline 80-82 matrix metallopeptidase 2 Rattus norvegicus 16-19 28987762-13 2018 Doxycycline treatment downregulated total MMP activity and MMP-2 and -9 protein content. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 42-45 28987762-13 2018 Doxycycline treatment downregulated total MMP activity and MMP-2 and -9 protein content. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 59-71 29378386-12 2018 STA also significantly increased the protein expressions of tissue inhibitor of metallopeptidase-1 (TIMP-1) and TIMP-2 but decreased those of matrix metalloproteinase-2 (MMP-2) and MMP-9, indicating excessive basement membrane in the fibrotic liver. stachydrine 0-3 matrix metallopeptidase 2 Rattus norvegicus 142-168 29378386-12 2018 STA also significantly increased the protein expressions of tissue inhibitor of metallopeptidase-1 (TIMP-1) and TIMP-2 but decreased those of matrix metalloproteinase-2 (MMP-2) and MMP-9, indicating excessive basement membrane in the fibrotic liver. stachydrine 0-3 matrix metallopeptidase 2 Rattus norvegicus 170-175 29345720-0 2018 Effects of nicotine administration in rats on MMP2 and VEGF levels in periodontal membrane. Nicotine 11-19 matrix metallopeptidase 2 Rattus norvegicus 46-50 29186367-8 2018 In PASMCs, hypoxia-induced changes, including effects on the expression of cell cycle regulators (cyclin B1 and cyclin D1), apoptosis-related proteins (bax, bcl-2, and cleaved caspase-3), migration promoters (matrix metalloproteinases 2 and 9), and NF-kappaB expression, as well as the production of HOCl, were all inhibited by silencing VPO1 with small interfering RNAs. pasmcs 3-9 matrix metallopeptidase 2 Rattus norvegicus 209-242 28165813-7 2018 Administration of piperine improved the morphological structure of tendon, increased glycosaminoglycans and hydroxyproline levels, and inhibited the expression and activities of MMP-2 and MMP-9. piperine 18-26 matrix metallopeptidase 2 Rattus norvegicus 178-183 28358226-8 2018 RESULTS: Excess maternal and postnatal thyroxine reduced the intensity of Alcian blue staining, altered the number of chondrocytes in proliferative and hypertrophic zones in growth cartilage, and reduced the gene expression of Sox9, Mmp2, Mmp9, Col II, and Bmp2 in the growth cartilage of all offspring. Thyroxine 39-48 matrix metallopeptidase 2 Rattus norvegicus 233-237 28851074-4 2018 Moreover, MIF facilitated the migration of ASMCs by upregulating the expression of matrix metalloproteinase (MMP)-2. asmcs 43-48 matrix metallopeptidase 2 Rattus norvegicus 83-115 29345720-8 2018 CONCLUSIONS: Nicotine reduces MMP production, disrupts collagen synthesis and causes periodontitis. Nicotine 13-21 matrix metallopeptidase 2 Rattus norvegicus 30-33 29441762-5 2017 The protein expressions of MMP-2 and MMP-9 in contused liver tissue of the rats in each group were observed by immunohistochemical staining (SP method) and Western blotting. TFF2 protein, human 141-143 matrix metallopeptidase 2 Rattus norvegicus 27-32 30234068-0 2018 Downregulation of Matrix Metalloproteinases 2 and 9 is Involved in the Protective Effect of Trehalose on Spinal Cord Injury. Trehalose 92-101 matrix metallopeptidase 2 Rattus norvegicus 18-51 30234068-3 2018 Therefore, we investigated the effect of trehalose on MMP-2 and MMP-9 expression in SCI. Trehalose 41-50 matrix metallopeptidase 2 Rattus norvegicus 54-59 30234068-10 2018 Treatment with 10 mM trehalose significantly reduced MMP-2 expression in 3 and 7 days (P< 0.01) and MMP-9 expression in 1, 3, and 7 days (P< 0.05) post-damage compared with vehicle. Trehalose 21-30 matrix metallopeptidase 2 Rattus norvegicus 53-58 30234068-13 2018 We propose that the neuroprotective effect of low dose trehalose is mediated by attenuation of MMP-2 and MMP-9 expression. Trehalose 55-64 matrix metallopeptidase 2 Rattus norvegicus 95-100 29285138-7 2017 Moreover, the results of immunohistochemical analysis indicated that the expression levels of histone deacetylase 1 (HDAC1), matrix metalloproteinase-2 (MMP-2) and transforming growth factor beta (TGFbeta) decreased in the curcumin treatment group, compared with the non-treated group or the negative control group. Curcumin 223-231 matrix metallopeptidase 2 Rattus norvegicus 125-151 29285138-7 2017 Moreover, the results of immunohistochemical analysis indicated that the expression levels of histone deacetylase 1 (HDAC1), matrix metalloproteinase-2 (MMP-2) and transforming growth factor beta (TGFbeta) decreased in the curcumin treatment group, compared with the non-treated group or the negative control group. Curcumin 223-231 matrix metallopeptidase 2 Rattus norvegicus 153-158 28854816-0 2018 Carvedilol Inhibits Matrix Metalloproteinase-2 Activation in Experimental Autoimmune Myocarditis: Possibilities of Cardioprotective Application. Carvedilol 0-10 matrix metallopeptidase 2 Rattus norvegicus 20-46 28854816-4 2018 However, effects of carvedilol administration in acute myocarditis with its impact on matrix metalloproteinases" (MMPs) activation have not been elucidated. Carvedilol 20-30 matrix metallopeptidase 2 Rattus norvegicus 114-118 28854816-12 2018 CONCLUSIONS: The protective effects of carvedilol on heart function observed in the acute phase of experimental autoimmune myocarditis seem to be associated with its ability to decrease MMP-2 activity and subsequently prevent degradation of myofilaments and release of troponin I while not related to suppression of inflammation. Carvedilol 39-49 matrix metallopeptidase 2 Rattus norvegicus 186-191 28118507-7 2017 The effects of nebivolol on level and expression of MMP-2 and MMP-9 levels were investigated by enzyme-linked immunosorbent assay and immunohistochemistry, respectively. Nebivolol 15-24 matrix metallopeptidase 2 Rattus norvegicus 52-57 28118507-10 2017 Rats in the nebivolol-pretreated group showed significant decrease in expression and quantity of MMP-2 and MMP-9 during IRI. Nebivolol 12-21 matrix metallopeptidase 2 Rattus norvegicus 97-102 28645608-0 2017 The role of losartan in preventing vascular remodeling in spontaneously hypertensive rats by inhibition of the H2O2/VPO1/HOCl/MMPs pathway. Losartan 12-20 matrix metallopeptidase 2 Rattus norvegicus 126-130 27782741-8 2017 Treatment with apocynin significantly inhibited deposition of collagen and reduced the level of MMP-2. acetovanillone 15-23 matrix metallopeptidase 2 Rattus norvegicus 96-101 28901438-7 2017 Notably, beta-aminopropionitrile inhibited paw swelling and the decreased the arthritis index, the MVD in the synovial membranes and the expression levels of MMP-2 and MMP-9. Aminopropionitrile 9-32 matrix metallopeptidase 2 Rattus norvegicus 158-163 28811128-6 2017 However, TMP-C4a effectively reversed this phenotypic switch, which was accompanied by a decreased expression of Matrix metalloproteinase 2 and 9 (MMP2 and MMP9) and cell cycle related proteins, including cyclin D1 and CDK4. tmp-c4a 9-16 matrix metallopeptidase 2 Rattus norvegicus 113-145 28811128-6 2017 However, TMP-C4a effectively reversed this phenotypic switch, which was accompanied by a decreased expression of Matrix metalloproteinase 2 and 9 (MMP2 and MMP9) and cell cycle related proteins, including cyclin D1 and CDK4. tmp-c4a 9-16 matrix metallopeptidase 2 Rattus norvegicus 147-151 28737133-8 2017 The effects of paricalcitol on the quantity and expression of MMP-2 and MMP-9 in renal tubular epithelial cells were investigated by enzyme-linked immunosorbent assay and immunohistochemistry, respectively. paricalcitol 15-27 matrix metallopeptidase 2 Rattus norvegicus 62-67 28776262-12 2017 In addition, vaspin significantly inhibited IL-1beta-induced ROS generation and MMP-2 activation in PASMCs. pasmcs 100-106 matrix metallopeptidase 2 Rattus norvegicus 80-85 28460073-9 2017 Conclusions: VDRAs, particularly paricalcitol, attenuated cardiac fibrosis acting on COL1A1, MMP-2 and CTGF expression, partly through regulation of miR-29b and miR-30c. paricalcitol 33-45 matrix metallopeptidase 2 Rattus norvegicus 93-98 28731157-0 2017 Curcumin prevents lipopolysaccharide-induced matrix metalloproteinase-2 activity via the Ras/MEK1/2 signaling pathway in rat vascular smooth muscle cells. Curcumin 0-8 matrix metallopeptidase 2 Rattus norvegicus 45-71 28648614-3 2017 In this study the effects of RA on MMP-2 production in cells of rat uterus were investigated. Tretinoin 29-31 matrix metallopeptidase 2 Rattus norvegicus 35-40 28648614-11 2017 CONCLUSION: RA had negative effects on cell proliferation and cell morphology and inhibited MMP-2 expression. Tretinoin 12-14 matrix metallopeptidase 2 Rattus norvegicus 92-97 27882817-12 2017 NaHS treatment downregulated TGF-beta1, ERK1/2, TIMP1, TIMP2, MMP-2, MMP-7, MMP-8, MMP-11, and MMP-14 expressions in the kidney of these diabetes rats (p<.01). sodium bisulfide 0-4 matrix metallopeptidase 2 Rattus norvegicus 62-67 27882817-13 2017 This result suggests that NaHS treatment could attenuate renal fibrosis by TGF-beta1 signaling, and its mechanisms may be correlated with ERK1/2 expression and modulation of MMPs/TIMPs expression. sodium bisulfide 26-30 matrix metallopeptidase 2 Rattus norvegicus 174-178 28752795-5 2017 The DMN treatment produced a progressive increase in the plasma markers (aspartate aminotransferase, alanine aminotransferase, total bililbin, hyarulonic acid, and matrix metalloproteinase-2) in 28 days after the first DMN injection. Dimethylnitrosamine 4-7 matrix metallopeptidase 2 Rattus norvegicus 164-190 29077163-6 2017 HI group exhibited an enhanced MMP-2 positive staining compared to controls at 24 h, 3 and 7 days post-HI by immunohistochemistry. hi 0-2 matrix metallopeptidase 2 Rattus norvegicus 31-36 28477356-0 2017 Epigallocatechin-3-gallate ameliorates intrahepatic cholestasis of pregnancy by inhibiting matrix metalloproteinase-2 and matrix metalloproteinase-9. epigallocatechin gallate 0-26 matrix metallopeptidase 2 Rattus norvegicus 91-148 28477356-2 2017 Epigallocatechin-3-gallate (EGCG) has been widely reported to inhibit activities of MMP-2 and MMP-9. epigallocatechin gallate 0-26 matrix metallopeptidase 2 Rattus norvegicus 84-89 28477356-2 2017 Epigallocatechin-3-gallate (EGCG) has been widely reported to inhibit activities of MMP-2 and MMP-9. epigallocatechin gallate 28-32 matrix metallopeptidase 2 Rattus norvegicus 84-89 28477356-7 2017 EGCG administration could inhibit the upregulation of MMP-2 and MMP-9 post-transcriptionally. epigallocatechin gallate 0-4 matrix metallopeptidase 2 Rattus norvegicus 54-59 28477356-10 2017 Our study demonstrates that, for the first time, the efficacy of EGCG in ameliorating ICP symptoms by inhibiting both MMP-2 and MMP-9, which supports its potential as a novel drug in ameliorating ICP. epigallocatechin gallate 65-69 matrix metallopeptidase 2 Rattus norvegicus 118-123 28731157-1 2017 The aim of the present study was to examine the effect of curcumin treatment on lipopolysaccharide (LPS)-induced matrix metalloproteinase-2 (MMP-2) activity, and assess whether the effects are mediated by the Ras/mitogen-activated protein kinase kinase 1/2 (MEK1/2) signaling pathway in vascular smooth muscle cells (VSMCs). Curcumin 58-66 matrix metallopeptidase 2 Rattus norvegicus 113-139 28731157-1 2017 The aim of the present study was to examine the effect of curcumin treatment on lipopolysaccharide (LPS)-induced matrix metalloproteinase-2 (MMP-2) activity, and assess whether the effects are mediated by the Ras/mitogen-activated protein kinase kinase 1/2 (MEK1/2) signaling pathway in vascular smooth muscle cells (VSMCs). Curcumin 58-66 matrix metallopeptidase 2 Rattus norvegicus 141-146 28731157-5 2017 Curcumin treatment was demonstrated to inhibit LPS-induced MMP-2 activity in rat VSMCs. Curcumin 0-8 matrix metallopeptidase 2 Rattus norvegicus 59-64 28731157-9 2017 Taken together, these findings suggest that curcumin prevents of LPS-induced MMP-2 activity through Ras/MEK1/2 and NF-kappaB signaling. Curcumin 44-52 matrix metallopeptidase 2 Rattus norvegicus 77-82 28501723-11 2017 CONCLUSION: The present results indicate that tangeretin exerted potent neuroprotective effects against pilocarpine-induced seizures via the activation of PI3K/Akt signaling and the regulation of MMPs. tangeretin 46-56 matrix metallopeptidase 2 Rattus norvegicus 196-200 28501723-11 2017 CONCLUSION: The present results indicate that tangeretin exerted potent neuroprotective effects against pilocarpine-induced seizures via the activation of PI3K/Akt signaling and the regulation of MMPs. Pilocarpine 104-115 matrix metallopeptidase 2 Rattus norvegicus 196-200 28713936-5 2017 The administration of EGCG or Val ameliorated the overproduction of cardiac collagen, inhibited matrix metalloproteinase (MMP) activity, decreased the expression of tissue inhibitor of MMP-2, atrial natriuretic peptide and brain natriuretic peptide. epigallocatechin gallate 22-26 matrix metallopeptidase 2 Rattus norvegicus 122-125 28838258-10 2017 CONCLUSION: The activated BMP/Smad and suppressed transforming growth factor-beta/Smad pathways could suppress silica-induced fibrosis via a MMP-dependent mechanism. Silicon Dioxide 111-117 matrix metallopeptidase 2 Rattus norvegicus 141-144 28397013-5 2017 Treatment of DEK effectively suppressed the NDEA-initiated hepatocarcinogenesis by modulation of XMEs, inducing of apoptosis via the mitochondrial pathway as revealed by modulating the Bcl-2 family proteins, cytochrome C, caspases, and inhibiting invasion, and angiogenesis as evidenced by changes in the activities of MMPs (MMP2/9) and the expression of VEGF. Diethylnitrosamine 44-48 matrix metallopeptidase 2 Rattus norvegicus 319-323 28397013-5 2017 Treatment of DEK effectively suppressed the NDEA-initiated hepatocarcinogenesis by modulation of XMEs, inducing of apoptosis via the mitochondrial pathway as revealed by modulating the Bcl-2 family proteins, cytochrome C, caspases, and inhibiting invasion, and angiogenesis as evidenced by changes in the activities of MMPs (MMP2/9) and the expression of VEGF. Diethylnitrosamine 44-48 matrix metallopeptidase 2 Rattus norvegicus 325-331 28714024-6 2017 Renal iNOS, matrix metalloproteinase (MMP)-2, phosphorylated-signal transducers and activators of transcription 3 (STAT3) and intercellular adhesion molecule-1 (ICAM-1) protein expression levels were suppressed by magnesium isoglycyrrhizinate treatment in RIRI model rats. 18alpha,20beta-hydroxy-11-oxo-norolean-12-en-3beta-yl-2-O-beta-D-glucopyranurosyl-alpha-D-glucopyranosiduronate magnesium tetrahydrate 214-242 matrix metallopeptidase 2 Rattus norvegicus 12-44 28713936-5 2017 The administration of EGCG or Val ameliorated the overproduction of cardiac collagen, inhibited matrix metalloproteinase (MMP) activity, decreased the expression of tissue inhibitor of MMP-2, atrial natriuretic peptide and brain natriuretic peptide. epigallocatechin gallate 22-26 matrix metallopeptidase 2 Rattus norvegicus 185-190 28714024-8 2017 These results implicate magnesium isoglycyrrhizinate pretreatment as a potential approach to protect against RIRI via suppression of the iNOS, ICAM-1, MMP-2 and STAT3 signaling pathways. 18alpha,20beta-hydroxy-11-oxo-norolean-12-en-3beta-yl-2-O-beta-D-glucopyranurosyl-alpha-D-glucopyranosiduronate magnesium tetrahydrate 24-52 matrix metallopeptidase 2 Rattus norvegicus 151-156 28713936-5 2017 The administration of EGCG or Val ameliorated the overproduction of cardiac collagen, inhibited matrix metalloproteinase (MMP) activity, decreased the expression of tissue inhibitor of MMP-2, atrial natriuretic peptide and brain natriuretic peptide. Valsartan 30-33 matrix metallopeptidase 2 Rattus norvegicus 122-125 28713936-5 2017 The administration of EGCG or Val ameliorated the overproduction of cardiac collagen, inhibited matrix metalloproteinase (MMP) activity, decreased the expression of tissue inhibitor of MMP-2, atrial natriuretic peptide and brain natriuretic peptide. Valsartan 30-33 matrix metallopeptidase 2 Rattus norvegicus 185-190 28494022-12 2017 The Adhflex-treated group had a significantly higher MMPs expression than the other treatment groups at all healing stages. adhflex 4-11 matrix metallopeptidase 2 Rattus norvegicus 53-57 28901184-7 2017 Validation studies revealed significantly decreased levels of interleukin 6 (IL-6), monocyte chemoattractant protein 3 (MCP-3), and matrix metallopeptidase 2 (MMP2) in culture supernatants of MMC-treated islets compared with controls. Mitomycin 192-195 matrix metallopeptidase 2 Rattus norvegicus 132-157 28901184-7 2017 Validation studies revealed significantly decreased levels of interleukin 6 (IL-6), monocyte chemoattractant protein 3 (MCP-3), and matrix metallopeptidase 2 (MMP2) in culture supernatants of MMC-treated islets compared with controls. Mitomycin 192-195 matrix metallopeptidase 2 Rattus norvegicus 159-163 28656223-6 2017 In contrast, the CaCl2-induced TAA formation was inhibited by pre-administering rapamycin to CaCl2-treated rats, which demonstrated attenuated mTOR phosphorylation and downregulation of the proinflammatory mediators (i.e., TNF-alpha, IL-6, IL-1beta, matrix metallopeptidases 2 and 9) to the control level. Calcium Chloride 93-98 matrix metallopeptidase 2 Rattus norvegicus 250-282 28680051-4 2017 Overexpression of LDHA in a PA cell line (GH3) promoted glucose uptake through the upregulation of glucose transporter-1 (Glut1), lactate secretion and induced cellular invasion by upregulation of matrix metalloproteinase2 (MMP2). 3'-dGTP 42-45 matrix metallopeptidase 2 Rattus norvegicus 197-222 28680051-4 2017 Overexpression of LDHA in a PA cell line (GH3) promoted glucose uptake through the upregulation of glucose transporter-1 (Glut1), lactate secretion and induced cellular invasion by upregulation of matrix metalloproteinase2 (MMP2). 3'-dGTP 42-45 matrix metallopeptidase 2 Rattus norvegicus 224-228 28680051-6 2017 Accordingly, oxamate-induced inhibition of LDHA suppressed glucose uptake, lactate secretion, invasion and proliferation in GH3 cells via down regulation of Glut1 and MMP2 expression and inhibition of the Akt-GSK-3beta-cyclinD1 pathway. Oxamic Acid 13-20 matrix metallopeptidase 2 Rattus norvegicus 167-171 28177667-11 2017 In rat VSMCs, UA effectively inhibited cell growth and the activity of MMP2 induced by leptin. ursolic acid 14-16 matrix metallopeptidase 2 Rattus norvegicus 71-75 28839358-8 2017 A reduction in MMP-2 and MMP-9 expressions also confirmed the collagen formation efficacy of ZBSO. zbso 93-97 matrix metallopeptidase 2 Rattus norvegicus 15-20 28706418-15 2017 Although zymography assays showed that CCl4 produced an increase in MMP-9 and MMP-2 gelatinase activity; interestingly, NAR administration was associated with normal MMP-9 and MMP-2 activity (P < 0.05). naringenin 120-123 matrix metallopeptidase 2 Rattus norvegicus 176-181 27417412-8 2017 In the HP group, the shortening treatment decreased the expression, but not the activity, of MMP-2, while doxycycline was able to inhibit the increase of expression and activity of MMP-2. Doxycycline 106-117 matrix metallopeptidase 2 Rattus norvegicus 181-186 27417412-9 2017 CONCLUSION: We conclude that the inhibition of MMP-2 by doxycycline, during incisor shortening, was not enough to alter the eruption rate, which suggests that MMP-2 may have an important role in the turnover of extracellular matrix of the periodontal ligament during the tooth-eruption process. Doxycycline 56-67 matrix metallopeptidase 2 Rattus norvegicus 47-52 28859670-4 2017 In this study, we aim to investigate the effect of tetramethylpyrazine (TMP), a natural compound with analgesic effects but unknown mechanisms, on MMP-2/9 in neuropathic pain. tetramethylpyrazine 51-70 matrix metallopeptidase 2 Rattus norvegicus 147-154 28859670-4 2017 In this study, we aim to investigate the effect of tetramethylpyrazine (TMP), a natural compound with analgesic effects but unknown mechanisms, on MMP-2/9 in neuropathic pain. tetramethylpyrazine 72-75 matrix metallopeptidase 2 Rattus norvegicus 147-154 28859670-8 2017 RESULTS: TMP significantly attenuated the maintenance of chronic constrictive injury (CCI)-induced neuropathic pain, inhibited the activation of astrocytes, and decreased the expression of MMP-2/9. tetramethylpyrazine 9-12 matrix metallopeptidase 2 Rattus norvegicus 189-196 28488074-0 2017 All-trans retinoic acid enhances in vitro mesenchymal stem cells migration by targeting matrix metalloproteinases 2 and 9. Tretinoin 10-23 matrix metallopeptidase 2 Rattus norvegicus 88-121 28488074-2 2017 RESULTS: The expression of the MMP-2/-9 was at least five times higher in ATRA-treated MSCs (P < 0.001), and MMP-2/-9 activity was enhanced with increasing doses compared to the control MSCs. Tretinoin 74-78 matrix metallopeptidase 2 Rattus norvegicus 31-39 28488074-2 2017 RESULTS: The expression of the MMP-2/-9 was at least five times higher in ATRA-treated MSCs (P < 0.001), and MMP-2/-9 activity was enhanced with increasing doses compared to the control MSCs. Tretinoin 74-78 matrix metallopeptidase 2 Rattus norvegicus 31-36 28488074-5 2017 CONCLUSION: ATRA increases the in vitro migration capacity of the MSCs through stimulating the expression and activity of MMP-2/-9 and inhibiting caspase three enzyme activity. Tretinoin 12-16 matrix metallopeptidase 2 Rattus norvegicus 122-127 28656223-6 2017 In contrast, the CaCl2-induced TAA formation was inhibited by pre-administering rapamycin to CaCl2-treated rats, which demonstrated attenuated mTOR phosphorylation and downregulation of the proinflammatory mediators (i.e., TNF-alpha, IL-6, IL-1beta, matrix metallopeptidases 2 and 9) to the control level. Calcium Chloride 17-22 matrix metallopeptidase 2 Rattus norvegicus 250-282 28620995-7 2017 Tilianin also mediates a dose-dependent inhibition of migration and the expression of intracellular ICAM-1, VCAM-1, MMP-2 and MMP-9. tilianin 0-8 matrix metallopeptidase 2 Rattus norvegicus 116-121 28755734-5 2017 RESULTS: It was found that epigallocatechin-3-gallate exhibited significant chemopreventive effects and anti-cancer stem cell activity through several pathways, including a significant decrease in the size and number of tumors per rat, significant amelioration of the oxidative stress markers" alterations and significant inhibition of CD44, VEGF, Ki-67 and MMP-2 expression associated with a significantly increased expression of caspase-3. epigallocatechin gallate 27-53 matrix metallopeptidase 2 Rattus norvegicus 358-363 28672904-0 2017 KATP channels in high glucose-induced rat mesangial cell proliferation and release of MMP-2 and fibronectin. Glucose 22-29 matrix metallopeptidase 2 Rattus norvegicus 86-91 28672904-4 2017 The mesangial cell proliferation and the release of matrix metalloproteinase (MMP)-2 and fibronectin in response to high glucose with a selective opener of KATP (diazoxide, DZX), or with a selective inhibitor of KATP (5-hydroxydecanoate, 5-HD) were also measured. Glucose 121-128 matrix metallopeptidase 2 Rattus norvegicus 52-84 28672904-11 2017 Moreover, DZX also inhibited cell proliferation and release of MMP-2 and fibronectin in HG-induced rat mesangial cells, and that was corrected by 5-HD. Deoxy-Galacto-Noeurostegine 10-13 matrix metallopeptidase 2 Rattus norvegicus 63-68 28465251-11 2017 Furthermore, DSI-treated group demonstrated potential regulation of myocardial collagen I and III deposition associated with MMP-2 expression. dsi 13-16 matrix metallopeptidase 2 Rattus norvegicus 125-130 27417412-0 2017 Doxycycline reduces the expression and activity of matrix metalloproteinase-2 in the periodontal ligament of the rat incisor without altering the eruption process. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 51-77 27417412-1 2017 BACKGROUND AND OBJECTIVE: Doxycycline is an antibiotic agent that inhibits the activity of matrix metalloproteinases (MMPs) present in the extracellular matrix. Doxycycline 26-37 matrix metallopeptidase 2 Rattus norvegicus 118-122 28260031-6 2017 As the bilirubin concentration increased, HSCs demonstrated reduced production of reactive oxygen species, reduced protein expression levels of alpha-smooth muscle actin, a decreased mRNA expression ratio of tissue inhibitor of matrix metalloproteinase-1/matrix metalloproteinase-2, decreased proliferation and increased apoptosis. Bilirubin 7-16 matrix metallopeptidase 2 Rattus norvegicus 208-281 28588362-0 2017 Folic Acid Modulates Matrix Metalloproteinase-2 Expression, Alleviates Neuropathic Pain, and Improves Functional Recovery in Spinal Cord-Injured Rats. Folic Acid 0-10 matrix metallopeptidase 2 Rattus norvegicus 21-47 27038334-10 2017 Moreover, this novel tri-ketonic phenylaminocarbonyl curcumin (CMC 2.24) appeared to reduce the pathologically excessive levels of inducible MMPs to near-normal levels, but appeared to have no significant effect on the constitutive MMPs required for physiologic connective tissue turnover. phenylaminocarbonyl curcumin 33-61 matrix metallopeptidase 2 Rattus norvegicus 141-145 28257144-10 2017 KEY RESULTS: In BDL rats, DHI administration attenuated liver necrosis, bile duct proliferation and collagen accumulation and reduced the expression of genes associated with fibrogenesis, including Tgfb1, Mmp-2, Acta2 and Col1a1. dehydrosoyasaponin I 26-29 matrix metallopeptidase 2 Rattus norvegicus 205-210 28260017-4 2017 In UC rats, disease activity and colonic mucosa damage were significantly reduced by the anti-inflammatory effects of D-limonene, via suppression of matrix metalloproteinase (MMP)-2 and -9 gene expression. Limonene 118-128 matrix metallopeptidase 2 Rattus norvegicus 149-188 28245103-2 2017 In this work, we prepared a class of optical interference-free SERS nanotags (CO-nanotags) that can be used for the purpose of multiplex sensing of different MMPs. Serine 63-67 matrix metallopeptidase 2 Rattus norvegicus 158-162 27519589-1 2017 BACKGROUND: Doxycycline, a nonspecific metalloproteinase (MMP) inhibitor, has been demonstrated to impact the strength of the polypropylene (PP) mesh-repaired hernia with an increase in the deposition of collagen type 1. Doxycycline 12-23 matrix metallopeptidase 2 Rattus norvegicus 58-61 27519589-1 2017 BACKGROUND: Doxycycline, a nonspecific metalloproteinase (MMP) inhibitor, has been demonstrated to impact the strength of the polypropylene (PP) mesh-repaired hernia with an increase in the deposition of collagen type 1. Polypropylenes 126-139 matrix metallopeptidase 2 Rattus norvegicus 58-61 28003226-8 2017 CTTHWGFTLC peptide, an MMP inhibitor and small interfering RNA (siRNA) against MMP-2 suppressed the canstatin-induced (250 ng/ml, 24 h) migration. canstatin 100-109 matrix metallopeptidase 2 Rattus norvegicus 79-84 27927649-8 2017 P-cresol increased Axl, proliferating of cell nuclear antigen (PCNA), focal adhesion kinase (FAK), and matrix metalloproteinase-2 (MMP-2) expressions, decreased caspase-3 expression, and was accompanied by increased cell viability and migration. 4-cresol 0-8 matrix metallopeptidase 2 Rattus norvegicus 103-129 27927649-8 2017 P-cresol increased Axl, proliferating of cell nuclear antigen (PCNA), focal adhesion kinase (FAK), and matrix metalloproteinase-2 (MMP-2) expressions, decreased caspase-3 expression, and was accompanied by increased cell viability and migration. 4-cresol 0-8 matrix metallopeptidase 2 Rattus norvegicus 131-136 28003226-13 2017 Y-27632 also suppressed the canstatin-induced (250 ng/ml, 24 h) MMP-2 secretion. Y 27632 0-7 matrix metallopeptidase 2 Rattus norvegicus 64-69 28003226-15 2017 In conclusion, this study revealed a novel function of canstatin for inducing cell migration of adult rat cardiac fibroblasts at least in part by ERK phosphorylation through MMP-2 secretion, possibly via actin cytoskeletal change. canstatin 55-64 matrix metallopeptidase 2 Rattus norvegicus 174-179 27677429-11 2017 Genistein attenuated leptin-induced A10 cell migration by inhibiting MMP-2 activity. Genistein 0-9 matrix metallopeptidase 2 Rattus norvegicus 69-74 27098997-8 2017 Effects of FCEtOH on LPS-induced MMP-2 and MMP-9 expression in H9c2 cells occurred directly through ERK1/2 were determined. fcetoh 11-17 matrix metallopeptidase 2 Rattus norvegicus 33-38 27098997-11 2017 In contrast, MMP-2 and MMP-9 were significantly reduced after FCEtOH administration. fcetoh 62-68 matrix metallopeptidase 2 Rattus norvegicus 13-18 28164126-7 2017 Western blotting showed that MMP2 expression was significantly increased in rats treated with cholecalciferol. Cholecalciferol 94-109 matrix metallopeptidase 2 Rattus norvegicus 29-33 28115189-0 2017 Rosmarinic acid counteracts activation of hepatic stellate cells via inhibiting the ROS-dependent MMP-2 activity: Involvement of Nrf2 antioxidant system. Reactive Oxygen Species 84-87 matrix metallopeptidase 2 Rattus norvegicus 98-103 28115189-2 2017 Matrix metalloproteinase-2 (MMP-2) is required for activation of hepatic stellate cells (HSCs) in response to reactive oxygen species (ROS). Reactive Oxygen Species 110-133 matrix metallopeptidase 2 Rattus norvegicus 0-26 28115189-2 2017 Matrix metalloproteinase-2 (MMP-2) is required for activation of hepatic stellate cells (HSCs) in response to reactive oxygen species (ROS). Reactive Oxygen Species 110-133 matrix metallopeptidase 2 Rattus norvegicus 28-33 28115189-2 2017 Matrix metalloproteinase-2 (MMP-2) is required for activation of hepatic stellate cells (HSCs) in response to reactive oxygen species (ROS). Reactive Oxygen Species 135-138 matrix metallopeptidase 2 Rattus norvegicus 0-26 28115189-2 2017 Matrix metalloproteinase-2 (MMP-2) is required for activation of hepatic stellate cells (HSCs) in response to reactive oxygen species (ROS). Reactive Oxygen Species 135-138 matrix metallopeptidase 2 Rattus norvegicus 28-33 28115189-3 2017 This study was designed to explore the hypothesis that the inhibitory effect of rosmarinic acid (RA) on HSCs activation might mainly result from its antioxidant capability by increasing the synthesis of glutathione (GSH) involved in nuclear factor kappa B (NF-kappaB)-dependent inhibition of MMP-2 activity. rosmarinic acid 80-95 matrix metallopeptidase 2 Rattus norvegicus 292-297 28115189-3 2017 This study was designed to explore the hypothesis that the inhibitory effect of rosmarinic acid (RA) on HSCs activation might mainly result from its antioxidant capability by increasing the synthesis of glutathione (GSH) involved in nuclear factor kappa B (NF-kappaB)-dependent inhibition of MMP-2 activity. rosmarinic acid 97-99 matrix metallopeptidase 2 Rattus norvegicus 292-297 28115189-3 2017 This study was designed to explore the hypothesis that the inhibitory effect of rosmarinic acid (RA) on HSCs activation might mainly result from its antioxidant capability by increasing the synthesis of glutathione (GSH) involved in nuclear factor kappa B (NF-kappaB)-dependent inhibition of MMP-2 activity. Glutathione 216-219 matrix metallopeptidase 2 Rattus norvegicus 292-297 28115189-5 2017 Concomitantly, RA inhibits MMP-2 activity. rosmarinic acid 15-17 matrix metallopeptidase 2 Rattus norvegicus 27-32 27702762-8 2017 In injured vessels, the apoptosis was greater and MMP2 expression was less in the NS + rAd-GLP-1 than in the exenatide or rAd-betaGAL groups. Exenatide 109-118 matrix metallopeptidase 2 Rattus norvegicus 50-54 28123012-9 2017 The induction of t-SP during cued reinstatement depends on activating matrix metalloproteinases (MMPs) and selective chemogenetic stimulation of nNOS interneurons recapitulated MMP activation and t-SP induction (increase in AMPA currents in MSNs). t-sp 17-21 matrix metallopeptidase 2 Rattus norvegicus 97-101 28123012-9 2017 The induction of t-SP during cued reinstatement depends on activating matrix metalloproteinases (MMPs) and selective chemogenetic stimulation of nNOS interneurons recapitulated MMP activation and t-SP induction (increase in AMPA currents in MSNs). t-sp 17-21 matrix metallopeptidase 2 Rattus norvegicus 97-100 28123012-14 2017 Stimulating these glutamate receptors increases nitric oxide (NO) production, which stimulates matrix metalloprotease-2 (MMP-2) and MMP-9 activity in the extracellular space. Nitric Oxide 48-60 matrix metallopeptidase 2 Rattus norvegicus 95-119 28123012-14 2017 Stimulating these glutamate receptors increases nitric oxide (NO) production, which stimulates matrix metalloprotease-2 (MMP-2) and MMP-9 activity in the extracellular space. Nitric Oxide 48-60 matrix metallopeptidase 2 Rattus norvegicus 121-126 27991776-4 2017 CPS also suppressed the DMN-induced increases in alpha-SMA, collagen type I, MMP-2, and TNF-alpha. Dimethylnitrosamine 24-27 matrix metallopeptidase 2 Rattus norvegicus 77-82 28396867-10 2017 MMP-2 was an exception, which was decreased after carvedilol treatment for 2 weeks and upregulated after carvedilol treatment for 4 weeks. Carvedilol 50-60 matrix metallopeptidase 2 Rattus norvegicus 0-5 28396867-10 2017 MMP-2 was an exception, which was decreased after carvedilol treatment for 2 weeks and upregulated after carvedilol treatment for 4 weeks. Carvedilol 105-115 matrix metallopeptidase 2 Rattus norvegicus 0-5 28115189-0 2017 Rosmarinic acid counteracts activation of hepatic stellate cells via inhibiting the ROS-dependent MMP-2 activity: Involvement of Nrf2 antioxidant system. rosmarinic acid 0-15 matrix metallopeptidase 2 Rattus norvegicus 98-103 28101000-0 2016 2-Chloroethanol Induced Upregulation of Matrix Metalloproteinase-2 in Primary Cultured Rat Astrocytes Via MAPK Signal Pathways. Ethylene Chlorohydrin 0-15 matrix metallopeptidase 2 Rattus norvegicus 40-66 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 52-70 matrix metallopeptidase 2 Rattus norvegicus 130-156 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 52-70 matrix metallopeptidase 2 Rattus norvegicus 158-163 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 72-79 matrix metallopeptidase 2 Rattus norvegicus 130-156 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 72-79 matrix metallopeptidase 2 Rattus norvegicus 158-163 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. Ethylene Chlorohydrin 194-209 matrix metallopeptidase 2 Rattus norvegicus 130-156 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. Ethylene Chlorohydrin 194-209 matrix metallopeptidase 2 Rattus norvegicus 158-163 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. Ethylene Chlorohydrin 211-215 matrix metallopeptidase 2 Rattus norvegicus 130-156 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. Ethylene Chlorohydrin 211-215 matrix metallopeptidase 2 Rattus norvegicus 158-163 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 248-255 matrix metallopeptidase 2 Rattus norvegicus 130-156 28101000-1 2016 This study was to explore the mechanisms underlying 1,2-dichloroethane (1,2-DCE) induced brain edema by focusing on alteration of matrix metalloproteinase-2 (MMP-2) in rat astrocytes induced by 2-chloroethanol (2-CE), an intermediate metabolite of 1,2-DCE in vivo. ethylene dichloride 248-255 matrix metallopeptidase 2 Rattus norvegicus 158-163 28966235-4 2017 Real-time RT-PCR demonstrated that ginsenoside Rg1 upregulated the expression of migration-related factors of OECs, including matrix metalloproteinases-2 (MMP-2), MMP-9, and neural cell adhesion molecule 1 (NCAM1). Ginsenosides 35-46 matrix metallopeptidase 2 Rattus norvegicus 126-153 28966235-4 2017 Real-time RT-PCR demonstrated that ginsenoside Rg1 upregulated the expression of migration-related factors of OECs, including matrix metalloproteinases-2 (MMP-2), MMP-9, and neural cell adhesion molecule 1 (NCAM1). Ginsenosides 35-46 matrix metallopeptidase 2 Rattus norvegicus 155-160 28497057-7 2017 The MMP-2 positive area was significantly greater in DN and DN + ES groups compared to the control group. Einsteinium 65-67 matrix metallopeptidase 2 Rattus norvegicus 4-9 27909732-9 2017 RB-222 significantly repressed VEGF expression as well as decreased MMP-2 and MMP-9 expression. rb-222 0-6 matrix metallopeptidase 2 Rattus norvegicus 68-73 28636071-12 2017 CONCLUSIONS: Increased plasma concentration of Hcy accompanied by the accumulation of collagen and upregulation of MMPs in rat seminal vesicles might contribute to the remodeling of seminal vesicles. Homocysteine 47-50 matrix metallopeptidase 2 Rattus norvegicus 115-119 28895768-0 2017 Protective effects of taurine against renal ischemia/reperfusion injury in rats by inhibition of gelatinases, MMP-2 and MMP-9, and p38 mitogen-activated protein kinase signaling. Taurine 22-29 matrix metallopeptidase 2 Rattus norvegicus 110-115 28895768-3 2017 Increased ROS production causes activation of p38 mitogen-activated protein kinase (MAPK) signaling, which participates in gene regulation of MMPs, especially MMP-2 and MMP-9 (gelatinases). Reactive Oxygen Species 10-13 matrix metallopeptidase 2 Rattus norvegicus 142-146 28895768-3 2017 Increased ROS production causes activation of p38 mitogen-activated protein kinase (MAPK) signaling, which participates in gene regulation of MMPs, especially MMP-2 and MMP-9 (gelatinases). Reactive Oxygen Species 10-13 matrix metallopeptidase 2 Rattus norvegicus 159-164 28895768-18 2017 Taurine pretreatment also decreased significantly both MMP-2 and MMP-9 mRNA expression and MMP-9 activity induced by I/R. Taurine 0-7 matrix metallopeptidase 2 Rattus norvegicus 55-60 28895768-20 2017 Inhibition of MMP-2 and MMP-9 expression and MMP-9 activity caused by taurine may be associated with suppression of p38 MAPK activation during I/R induced renal injury in rats. Taurine 70-77 matrix metallopeptidase 2 Rattus norvegicus 14-19 28002484-9 2016 Matrix metalloproteinase-2 (MMP2), CD44, and nephroblastoma overexpressed gene (NOV) were overexpressed in the medulla and cortex of lithium-fed rats compared to the control group. Lithium 133-140 matrix metallopeptidase 2 Rattus norvegicus 0-26 26746667-12 2017 ProTDeltaNLS suppresses expression of TNF-alpha, MPO, and activity of MMPs in ischemic brain tissue. protdeltanls 0-12 matrix metallopeptidase 2 Rattus norvegicus 70-74 27729285-8 2016 TGF-beta1 protein and fibrosis-related proteins MMP-2 and MMP-9 were up-regulated after MI, and they were significantly suppressed by the administration of DHI(p<0.05 and p<0.01, respectively). dehydrosoyasaponin I 156-159 matrix metallopeptidase 2 Rattus norvegicus 48-53 28002484-9 2016 Matrix metalloproteinase-2 (MMP2), CD44, and nephroblastoma overexpressed gene (NOV) were overexpressed in the medulla and cortex of lithium-fed rats compared to the control group. Lithium 133-140 matrix metallopeptidase 2 Rattus norvegicus 28-32 27991501-12 2016 In conclusion, the higher levels of IL-1, TNF-alpha and MMP-2 in collagen-coated polypropylene mesh imply greater inflammation than the non-coated polypropylene mesh. Polypropylenes 81-94 matrix metallopeptidase 2 Rattus norvegicus 56-61 27720765-7 2016 With 1 nanomolar MMP-2 treatment, product formation was observed to increase over a three day period, with (RADA)4/(RADA)4-CP1/CP2 mixture, however there was little difference between groups. 4-cp1 121-126 matrix metallopeptidase 2 Rattus norvegicus 17-22 27720765-7 2016 With 1 nanomolar MMP-2 treatment, product formation was observed to increase over a three day period, with (RADA)4/(RADA)4-CP1/CP2 mixture, however there was little difference between groups. cp2 127-130 matrix metallopeptidase 2 Rattus norvegicus 17-22 27317634-2 2016 Herein, a novel class sulphonamides-1,3,5-triazine conjugates have been synthesized and tested for inhibitory activity against MMP-2 and MMP-9. sulphonamides-1,3,5-triazine 22-50 matrix metallopeptidase 2 Rattus norvegicus 127-132 27769178-0 2016 Autonomic remodeling may be responsible for decreased incidence of aortic dissection in STZ-induced diabetic rats via down-regulation of matrix metalloprotease 2. Streptozocin 88-91 matrix metallopeptidase 2 Rattus norvegicus 137-161 26349680-10 2016 The results of Western blot analysis showed that all of the treatments significantly reduced MMP2 and MMP9 protein levels compared with the PBS control group (p < 0.05) and that the levels of these proteins displayed the largest decrease in the bFGF + ADSC group (p < 0.05). Lead 140-143 matrix metallopeptidase 2 Rattus norvegicus 93-97 27451961-7 2016 The CD147+DOX group also received doxycycline, an inhibitor of MMPs (daily, 30 mg/kg in 1.5 mL saline, iG). Doxycycline 34-45 matrix metallopeptidase 2 Rattus norvegicus 63-67 27769178-15 2016 CONCLUSIONS: STZ-induced diabetic rats have a lower incidence of AD after URAS and BAPN treatment, this protective effect could be possibly attributed to autonomic innervation modification and possible related down-regulation of MMP2. Streptozocin 13-16 matrix metallopeptidase 2 Rattus norvegicus 229-233 27769178-15 2016 CONCLUSIONS: STZ-induced diabetic rats have a lower incidence of AD after URAS and BAPN treatment, this protective effect could be possibly attributed to autonomic innervation modification and possible related down-regulation of MMP2. Aminopropionitrile 83-87 matrix metallopeptidase 2 Rattus norvegicus 229-233 27531060-6 2016 Increased activity of MMP-2 was observed in aortas from 2K1C at 1 and 2weeks of hypertension, followed by increased VSMC proliferation, and those effects were abolished by treating 2K1C rats with doxycycline (p<0.05). Doxycycline 196-207 matrix metallopeptidase 2 Rattus norvegicus 22-27 27575818-12 2016 Compared with STZ group, the expressions of CX40, CX43, CX45, MMP-1 and MMP-2 were significantly increased (P < 0.01), while the content of type II collagen, kidney hydroxyproline and timp-2 expression were markedly deceased in STZ+H2S group. Streptozocin 14-17 matrix metallopeptidase 2 Rattus norvegicus 72-77 27420584-10 2016 TQ also blocked MCT-induced pulmonary arterial remodeling, proliferation of PASMCs, elevation of MMP2 and downregulation of ratio of Bax/Bcl-2, cleaved caspase-3 and cleaved PARP. thymoquinone 0-2 matrix metallopeptidase 2 Rattus norvegicus 97-101 27420584-10 2016 TQ also blocked MCT-induced pulmonary arterial remodeling, proliferation of PASMCs, elevation of MMP2 and downregulation of ratio of Bax/Bcl-2, cleaved caspase-3 and cleaved PARP. mct 16-19 matrix metallopeptidase 2 Rattus norvegicus 97-101 27481456-14 2016 The TGF-beta and MMP-2 levels were lower in the CDDP group than in the letrozole group. Cisplatin 48-52 matrix metallopeptidase 2 Rattus norvegicus 17-22 27481456-14 2016 The TGF-beta and MMP-2 levels were lower in the CDDP group than in the letrozole group. Letrozole 71-80 matrix metallopeptidase 2 Rattus norvegicus 17-22 27239047-0 2016 Whey peptide Isoleucine-Tryptophan inhibits expression and activity of matrix metalloproteinase-2 in rat aorta. isoleucine-tryptophan 13-34 matrix metallopeptidase 2 Rattus norvegicus 71-97 27280587-10 2016 Additionally, exogenous PLGF-induced activation of MMPs in rat RLE-6TN alveolar epithelial cells was suppressed by NFkappaB inhibitor pyrrolidine dithiocarbamate. pyrrolidine dithiocarbamic acid 134-161 matrix metallopeptidase 2 Rattus norvegicus 51-55 27236325-10 2016 Icilin also antagonized the activation of p38 and MMP-2 and the repression of p21 caused by FBS. icilin 0-6 matrix metallopeptidase 2 Rattus norvegicus 50-55 27075430-7 2016 The administration of NAC blocked the maturation of interleukin-1beta, which is a critical substrate of MMPs, and markedly suppressed the neuronal activation induced by CCI, including inhibiting the phosphorylation of protein kinase Cgamma, NMDAR1, and mitogen-activated protein kinases. Acetylcysteine 22-25 matrix metallopeptidase 2 Rattus norvegicus 104-108 27239047-10 2016 Signaling pathways regulating MMP2 expression in ECs and SMCs were similarly inhibited after treatment with IW or captopril. Captopril 114-123 matrix metallopeptidase 2 Rattus norvegicus 30-34 27279123-3 2016 Nobiletin, a polymethoxy citrus flavone, has potent MMP-2 and MMP-9 inhibitory activity in addition to antioxidant activity. nobiletin 0-9 matrix metallopeptidase 2 Rattus norvegicus 52-57 27279123-3 2016 Nobiletin, a polymethoxy citrus flavone, has potent MMP-2 and MMP-9 inhibitory activity in addition to antioxidant activity. polymethoxy citrus flavone 13-39 matrix metallopeptidase 2 Rattus norvegicus 52-57 27279123-4 2016 We hypothesized that nobiletin due to its MMP-2 & MMP-9 inhibitory and antioxidant effects may ameliorate the cardiovascular dysfunction of diabetes. nobiletin 21-30 matrix metallopeptidase 2 Rattus norvegicus 42-47 27279123-10 2016 Treatment with 25 mg kg(-1) nobiletin ameliorated the hemodynamic parameters, oxidative stress, collagen level, MMP-2 and MMP-9 levels, and vascular reactivity significantly compared with vehicle treated diabetic group. nobiletin 28-37 matrix metallopeptidase 2 Rattus norvegicus 112-117 27279123-11 2016 Thus, this study suggests that nobiletin ameliorates the CVD of diabetes by inhibiting oxidative stress, MMP-2 & MMP-9 and can be used as a potential therapeutic approach. nobiletin 31-40 matrix metallopeptidase 2 Rattus norvegicus 105-110 27508250-1 2016 The present data are related to the research article entitled "Whey peptide isoleucine-tryptophan inhibits expression and activity of matrix metalloproteinase-2 in rat aorta" [1]. Peptides 68-75 matrix metallopeptidase 2 Rattus norvegicus 134-160 27508250-1 2016 The present data are related to the research article entitled "Whey peptide isoleucine-tryptophan inhibits expression and activity of matrix metalloproteinase-2 in rat aorta" [1]. isoleucine-tryptophan 76-97 matrix metallopeptidase 2 Rattus norvegicus 134-160 27508250-0 2016 Data of the natural and pharmaceutical angiotensin-converting enzyme inhibitor isoleucine-tryptophan as a potent blocker of matrix metalloproteinase-2 expression in rat aorta. isoleucine-tryptophan 79-100 matrix metallopeptidase 2 Rattus norvegicus 124-150 27508250-2 2016 Here we present data on removal of endothelium from aorta, endothelium dependent aortic relaxation and inhibition of expression of pro-MMP2 by di-peptide isoleucine-tryptophan (IW). di-peptide isoleucine-tryptophan 143-175 matrix metallopeptidase 2 Rattus norvegicus 135-139 27508250-9 2016 Similarly, captopril (CA) inhibited ANGI-induced MMP2 protein expression in both in vitro and ex vivo. Captopril 11-20 matrix metallopeptidase 2 Rattus norvegicus 49-53 27323108-7 2016 Artesunate treatment also led to decreased collagen-IV protein levels, which might be a result of its downregulated expression and increased MMP-2 and MMP-9 protein and mRNA levels. Artesunate 0-10 matrix metallopeptidase 2 Rattus norvegicus 141-146 27314760-9 2016 BET treatment diminished TG and HYP levels; prooxidant status and fibrotic changes; alpha-SMA, COL1A1 and TGF-beta protein expressions; MMP-2, TIMP-1 and TIMP-2 mRNA expressions in the liver of fibrotic rats. Betaine 0-3 matrix metallopeptidase 2 Rattus norvegicus 136-141 27323108-8 2016 Increased TIMP-1 and TIMP- 2 protein and mRNA levels were detected after artesunate treatment in lung tissues and primary lung fibroblast cells and may contribute to enhanced activity of MMP-2 and -9. Artesunate 73-83 matrix metallopeptidase 2 Rattus norvegicus 187-199 27323108-9 2016 These findings suggested that artesunate attenuates alveolitis and pulmonary fibrosis by regulating expression of collagen-IV, TIMP-1 and 2, as well as MMP-2 and -9, to reduce ECM accumulation. Artesunate 30-40 matrix metallopeptidase 2 Rattus norvegicus 152-164 27112177-8 2016 Reduction of host angiogenesis, cardiomyocyte cycling, and MMP-2 activities was evident in animals treated with GM6001. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 112-118 matrix metallopeptidase 2 Rattus norvegicus 59-64 27050838-9 2016 Clofibrate treatment prevented MI-induced changes in iNOS, MMP-2 and MMP-9, ICAM-1, IL-6, NF-kappaB, and IkappaB. Clofibrate 0-10 matrix metallopeptidase 2 Rattus norvegicus 59-64 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Homocysteine 81-84 matrix metallopeptidase 2 Rattus norvegicus 176-181 27138327-12 2016 The active isoform of MMP-2 was higher activity in TG at 14 days. Thioguanine 51-53 matrix metallopeptidase 2 Rattus norvegicus 22-27 27274199-12 2016 Compared with the control group, the UA-treated groups exhibited reduced protein levels of MMP2, MMP9, and activated MAPKs (P<0.01) but an increased level of TIMP1 (P<0.01). ursolic acid 37-39 matrix metallopeptidase 2 Rattus norvegicus 91-95 27261860-0 2016 Influence of hydrogen sulfide on zymogen activation of homocysteine-induced matrix metalloproteinase-2 in H9C2 cardiocytes. Hydrogen Sulfide 13-29 matrix metallopeptidase 2 Rattus norvegicus 76-102 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Hydrogen Sulfide 90-106 matrix metallopeptidase 2 Rattus norvegicus 148-174 27261860-0 2016 Influence of hydrogen sulfide on zymogen activation of homocysteine-induced matrix metalloproteinase-2 in H9C2 cardiocytes. Homocysteine 55-67 matrix metallopeptidase 2 Rattus norvegicus 76-102 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Hydrogen Sulfide 90-106 matrix metallopeptidase 2 Rattus norvegicus 176-181 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Homocysteine 67-79 matrix metallopeptidase 2 Rattus norvegicus 148-174 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Homocysteine 67-79 matrix metallopeptidase 2 Rattus norvegicus 176-181 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Hydrogen Sulfide 108-111 matrix metallopeptidase 2 Rattus norvegicus 148-174 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Homocysteine 81-84 matrix metallopeptidase 2 Rattus norvegicus 148-174 27261860-1 2016 OBJECTIVE: To observe the influence of different concentrations of homocysteine (Hcy) and hydrogen sulfide (H2S) on the secretion and activation of matrix metalloproteinase-2 (MMP-2) in cardiocytes so as to search for new ways to fight against myocardial tissue fibrosis. Hydrogen Sulfide 108-111 matrix metallopeptidase 2 Rattus norvegicus 176-181 27261860-4 2016 ELISA and MTT were employed to detect the expression and enzymatic activity of MMP-2. monooxyethylene trimethylolpropane tristearate 10-13 matrix metallopeptidase 2 Rattus norvegicus 79-84 27261860-7 2016 Hcy with concentrations of 10, 50 and 100 mumol/L could increase the quantity of MMP-2 secreted by cardiocytes H9C2, and the interaction strength was concentration-dependent (P < 0.05). Homocysteine 0-3 matrix metallopeptidase 2 Rattus norvegicus 81-86 27261860-8 2016 After interacting with 100 mumol/L of Hcy for 6 h, the zymogen activation effect of MMP-2 was stronger than that of the 2.5-25 mumol/L group (P < 0.05). Homocysteine 38-41 matrix metallopeptidase 2 Rattus norvegicus 84-89 27261860-9 2016 After interacting with Hcy and H2S (1.0 mmol/L) for 6 h and 24 h, the activation effect of MMP-2 was stronger than those interacted with 10, 25, 50 and 100 mumol/L of Hcy (P < 0.05). Homocysteine 23-26 matrix metallopeptidase 2 Rattus norvegicus 91-96 27261860-9 2016 After interacting with Hcy and H2S (1.0 mmol/L) for 6 h and 24 h, the activation effect of MMP-2 was stronger than those interacted with 10, 25, 50 and 100 mumol/L of Hcy (P < 0.05). Hydrogen Sulfide 31-34 matrix metallopeptidase 2 Rattus norvegicus 91-96 27261860-9 2016 After interacting with Hcy and H2S (1.0 mmol/L) for 6 h and 24 h, the activation effect of MMP-2 was stronger than those interacted with 10, 25, 50 and 100 mumol/L of Hcy (P < 0.05). Homocysteine 167-170 matrix metallopeptidase 2 Rattus norvegicus 91-96 27261860-11 2016 Besides, the interaction strength is concentration-dependent; while H2S can up-regulate the activation of MMP-2 and co-promote the activation of MMP-2 with Hcy as well. Hydrogen Sulfide 68-71 matrix metallopeptidase 2 Rattus norvegicus 106-111 27261860-11 2016 Besides, the interaction strength is concentration-dependent; while H2S can up-regulate the activation of MMP-2 and co-promote the activation of MMP-2 with Hcy as well. Hydrogen Sulfide 68-71 matrix metallopeptidase 2 Rattus norvegicus 145-150 27261860-11 2016 Besides, the interaction strength is concentration-dependent; while H2S can up-regulate the activation of MMP-2 and co-promote the activation of MMP-2 with Hcy as well. Homocysteine 156-159 matrix metallopeptidase 2 Rattus norvegicus 145-150 26333546-6 2016 RESULTS: High-dose calcitriol treatment of uraemic rats given a high phosphate diet induced massive calcifications, apoptosis and increased gene expressions of MMP-2, MMP-9 and of osteogenic transcription factors and proteins in aortic VSMC. Calcitriol 19-29 matrix metallopeptidase 2 Rattus norvegicus 160-165 26333546-6 2016 RESULTS: High-dose calcitriol treatment of uraemic rats given a high phosphate diet induced massive calcifications, apoptosis and increased gene expressions of MMP-2, MMP-9 and of osteogenic transcription factors and proteins in aortic VSMC. Phosphates 69-78 matrix metallopeptidase 2 Rattus norvegicus 160-165 26638897-6 2016 These findings indicate that heparanase and MMP2 might play an important role in the development of MCT-induced cardiac hypertrophy. Monocrotaline 100-103 matrix metallopeptidase 2 Rattus norvegicus 44-48 27143852-7 2016 RESULTS AND DISCUSSION: Using isolated rat VSMCs in culture, zoledronate (100 muM) increased MMP-9 and -13 mRNA expressions but inhibited MMP-2 expression. Zoledronic Acid 61-72 matrix metallopeptidase 2 Rattus norvegicus 138-143 26179445-14 2016 The results of the western blot analyses revealed that both 30 and 60 mg/kg of paeoniflorin significantly down-regulated the levels of MMP-2, MMP-9, iNOS and COX-2. peoniflorin 79-91 matrix metallopeptidase 2 Rattus norvegicus 135-140 26179445-16 2016 The anti-inflammatory mechanism of paeoniflorin was further supported, in part, by its inhibitory effect on MMP-2, MMP-9, iNOS and COX-2. peoniflorin 35-47 matrix metallopeptidase 2 Rattus norvegicus 108-113 26753695-10 2016 This model of 6 weeks high-fat high-cholesterol diet showed minimal fibrosis as noticed by increase MMP2 and Masson trichrome satin. Cholesterol 36-47 matrix metallopeptidase 2 Rattus norvegicus 100-104 26988435-9 2016 RESULTS: Treatment with CTJ for 24 h dose-dependently inhibited the proliferation and migration of HASMCs and expression of MMP-2 in HASMCs. ctj 24-27 matrix metallopeptidase 2 Rattus norvegicus 124-129 26998126-0 2016 Effect of photodynamic therapy combined with torasemide on the expression of matrix metalloproteinase 2 and sodium-potassium-chloride cotransporter 1 in rat peritumoral edema and glioma. Torsemide 45-55 matrix metallopeptidase 2 Rattus norvegicus 77-149 26998126-3 2016 The present study evaluated the effects of PDT combined with torasemide on the levels of matrix metalloproteinase (MMP) 2 and sodium-potassium-chloride cotransporter (NKCC) 1 in peritumoral edema regions of rat glioma. Torsemide 61-71 matrix metallopeptidase 2 Rattus norvegicus 89-121 26998126-12 2016 In conclusion, PDT combined with torasemide prolonged the survival time of rats by inhibiting the growth of glioma through a reduction in the expression of MMP2, and by reducing peritumoral edema through a reduction in the expression levels of NKCC1. Torsemide 33-43 matrix metallopeptidase 2 Rattus norvegicus 156-160 27199659-6 2016 The AT1 antagonist candesartan restored MMP/TIMP equilibrium and modulated expression of Occludin and laminin, but not ZO-1, thereby improving BBB permeability. candesartan 19-30 matrix metallopeptidase 2 Rattus norvegicus 40-43 27095762-9 2016 RESULTS: (1) The expression ofalpha-SMA and MMP-2 increased significantly after HSC-T6 cells were treated with PA at a concentration of 300mumol/L for 24 hours (P< 0.05). Palmitic Acid 111-113 matrix metallopeptidase 2 Rattus norvegicus 44-49 27095762-12 2016 (4) Compared with the HSC-T6 cells in the PA group, the HSC-T6 cells treated with PA+HMGB1-siRNA for 24 hours showed significant reductions in the expression of HMGB1,alpha-SMA, and MMP-2 (P< 0.05). Palmitic Acid 82-84 matrix metallopeptidase 2 Rattus norvegicus 182-187 26773360-7 2016 While fipronil resulted in higher concentrations of endothelin-1, reduced antioxidant capacity and lower levels of circulating matrix metalloproteinase 2 (MMP-2) and nitric oxide (NO) metabolites compared to Control group, no alteration was observed in serum biomarkers of renal and hepatic/biliary functional abilities. fipronil 6-14 matrix metallopeptidase 2 Rattus norvegicus 127-153 26773360-7 2016 While fipronil resulted in higher concentrations of endothelin-1, reduced antioxidant capacity and lower levels of circulating matrix metalloproteinase 2 (MMP-2) and nitric oxide (NO) metabolites compared to Control group, no alteration was observed in serum biomarkers of renal and hepatic/biliary functional abilities. fipronil 6-14 matrix metallopeptidase 2 Rattus norvegicus 155-160 26773360-9 2016 Also, these findings suggest that reductions of both MMP-2 and NO may contribute with the elevation of systolic blood pressure observed with fipronil. fipronil 141-149 matrix metallopeptidase 2 Rattus norvegicus 53-58 26872030-7 2016 An increased level of miRNA-21 by mimics promoted the survival, migration and tube formation of endothelial cells, which simultaneously inhibited tissue inhibitor of metalloproteinase-3 (TIMP3) expression and promoted matrix metalloproteinase-2 (MMP2) and matrix metalloproteinase-9 (MMP9) expression and secretion. mirna-21 22-30 matrix metallopeptidase 2 Rattus norvegicus 218-244 26872030-7 2016 An increased level of miRNA-21 by mimics promoted the survival, migration and tube formation of endothelial cells, which simultaneously inhibited tissue inhibitor of metalloproteinase-3 (TIMP3) expression and promoted matrix metalloproteinase-2 (MMP2) and matrix metalloproteinase-9 (MMP9) expression and secretion. mirna-21 22-30 matrix metallopeptidase 2 Rattus norvegicus 246-250 26872030-13 2016 In summary, these findings suggest that miRNA-21 has a protective effect on angiogenesis by reducing cell death and promoting cell survival, migration and tube formation via partially targeting the TIMP3 by potentially regulating MMP2 and MMP9. mirna-21 40-48 matrix metallopeptidase 2 Rattus norvegicus 230-234 27322513-0 2016 Amlodipine and Atorvastatin Improved Hypertensive Cardiac Remodeling through Regulation of MMPs/TIMPs in SHR Rats. Amlodipine 0-10 matrix metallopeptidase 2 Rattus norvegicus 91-95 27322513-18 2016 CONCLUSION: Amlodipine and Atorvastatin could improve ventricular remodeling in SHR rats through intervention with the imbalance of MMP-2/TIMP-2 and MMP-9/TIMP-1 system. Atorvastatin 27-39 matrix metallopeptidase 2 Rattus norvegicus 132-137 26424219-8 2016 In conclusion, repeated dose topical application of trans-resveratrol produces sustained IOP lowering effect, which is associated with increased level of aqueous humor MMP-2, normalization of TM and retinal morphology and restoration of retinal redox status. Resveratrol 52-69 matrix metallopeptidase 2 Rattus norvegicus 168-173 26501493-4 2016 The aim of the study was to investigate the role of MMPs and their inhibitors (TIMPs), in the pathogenesis of choline deficiency-induced cardiomyopathy, and the way they are affected by carnitine supplementation. Choline 110-117 matrix metallopeptidase 2 Rattus norvegicus 52-56 26501493-4 2016 The aim of the study was to investigate the role of MMPs and their inhibitors (TIMPs), in the pathogenesis of choline deficiency-induced cardiomyopathy, and the way they are affected by carnitine supplementation. Carnitine 186-195 matrix metallopeptidase 2 Rattus norvegicus 52-56 27010902-14 2016 Genistein was also able to salvage the testicular structure and function through restoring the MMP-TIMP anti-proteolytic balance, suppressing spermatogenic damage, alleviating oxidative stress and apoptosis. Genistein 0-9 matrix metallopeptidase 2 Rattus norvegicus 95-98 27889760-10 2016 RESULTS: Doxorubicin-induced acute cardiotoxicity showed increased matrix metalloproteinases (MMP)-2 activation, oxidative damage and induced alterations in myocardial energetic metabolism. Doxorubicin 9-20 matrix metallopeptidase 2 Rattus norvegicus 67-100 27322513-0 2016 Amlodipine and Atorvastatin Improved Hypertensive Cardiac Remodeling through Regulation of MMPs/TIMPs in SHR Rats. Atorvastatin 15-27 matrix metallopeptidase 2 Rattus norvegicus 91-95 27322513-1 2016 BACKGROUND: MMPs/TIMPs system is well known to play important roles in pressure overload-induced cardiac remodeling, and Amlodipine and Atorvastatin have been showed to exert favourable protective effects on cardiovascular disease, however, it is not clear whether Amlodipine and Atorvastatin can improve hypertensive cardiac remodeling and whether the MMPs/TIMPs system is involved. Amlodipine 121-131 matrix metallopeptidase 2 Rattus norvegicus 353-357 27322513-1 2016 BACKGROUND: MMPs/TIMPs system is well known to play important roles in pressure overload-induced cardiac remodeling, and Amlodipine and Atorvastatin have been showed to exert favourable protective effects on cardiovascular disease, however, it is not clear whether Amlodipine and Atorvastatin can improve hypertensive cardiac remodeling and whether the MMPs/TIMPs system is involved. Atorvastatin 136-148 matrix metallopeptidase 2 Rattus norvegicus 12-16 27322513-1 2016 BACKGROUND: MMPs/TIMPs system is well known to play important roles in pressure overload-induced cardiac remodeling, and Amlodipine and Atorvastatin have been showed to exert favourable protective effects on cardiovascular disease, however, it is not clear whether Amlodipine and Atorvastatin can improve hypertensive cardiac remodeling and whether the MMPs/TIMPs system is involved. Atorvastatin 136-148 matrix metallopeptidase 2 Rattus norvegicus 353-357 27322513-1 2016 BACKGROUND: MMPs/TIMPs system is well known to play important roles in pressure overload-induced cardiac remodeling, and Amlodipine and Atorvastatin have been showed to exert favourable protective effects on cardiovascular disease, however, it is not clear whether Amlodipine and Atorvastatin can improve hypertensive cardiac remodeling and whether the MMPs/TIMPs system is involved. Amlodipine 265-275 matrix metallopeptidase 2 Rattus norvegicus 12-16 27322513-1 2016 BACKGROUND: MMPs/TIMPs system is well known to play important roles in pressure overload-induced cardiac remodeling, and Amlodipine and Atorvastatin have been showed to exert favourable protective effects on cardiovascular disease, however, it is not clear whether Amlodipine and Atorvastatin can improve hypertensive cardiac remodeling and whether the MMPs/TIMPs system is involved. Atorvastatin 280-292 matrix metallopeptidase 2 Rattus norvegicus 12-16 27322513-15 2016 Amlodipine alone, Atorvastatin alone, and combination of the two all reduced MMP-2 and MMP-9 mRNA, protein and enzyme activity, with the best effects seen in the combination. Amlodipine 0-10 matrix metallopeptidase 2 Rattus norvegicus 77-82 27322513-15 2016 Amlodipine alone, Atorvastatin alone, and combination of the two all reduced MMP-2 and MMP-9 mRNA, protein and enzyme activity, with the best effects seen in the combination. Atorvastatin 18-30 matrix metallopeptidase 2 Rattus norvegicus 77-82 27322513-18 2016 CONCLUSION: Amlodipine and Atorvastatin could improve ventricular remodeling in SHR rats through intervention with the imbalance of MMP-2/TIMP-2 and MMP-9/TIMP-1 system. Amlodipine 12-22 matrix metallopeptidase 2 Rattus norvegicus 132-137 26597542-10 2016 In addition, 5-Aza significantly increased HIF-1alpha mRNA and protein abundance as well as matrix metalloproteinase (MMP)-2 and MMP-9, but decreased MMP-13 protein abundance in neonatal brains. Decitabine 13-18 matrix metallopeptidase 2 Rattus norvegicus 92-124 26597542-12 2016 Inhibition of HIF-1alpha blocked 5-Aza-mediated changes in MMPs and abrogated 5-Aza-induced increase in HI-mediated brain injury. Decitabine 33-38 matrix metallopeptidase 2 Rattus norvegicus 59-63 27910782-7 2016 Analysis by immunofluorescence and western blotting shows that the expression of VEGF, MMP-2, and MMP-9 was found to be significantly elevated in the DMH- treated group and notably lowered by NSAID coadministration. 1,2-Dimethylhydrazine 150-153 matrix metallopeptidase 2 Rattus norvegicus 87-92 26549213-0 2016 Osthole ameliorates acute myocardial infarction in rats by decreasing the expression of inflammatory-related cytokines, diminishing MMP-2 expression and activating p-ERK. osthol 0-7 matrix metallopeptidase 2 Rattus norvegicus 132-137 26549213-8 2016 Our results revealed that osthole markedly reduced the infarct size, and the levels of CK, CK-MB, LDH and cTnT in the rats with AMI, and that these cardioprotective effects may be associated with the inhibition of inflammatory reactions, the reduction in MMP-2 activity and the activation of MAPK cascades. osthol 26-33 matrix metallopeptidase 2 Rattus norvegicus 255-260 27910782-10 2016 Results from the present study indicate the potential role of these chemokines along with VEGF and MMPs against angiogenesis in DMH-induced cancer. 1,2-Dimethylhydrazine 128-131 matrix metallopeptidase 2 Rattus norvegicus 99-103 26690114-0 2015 Possible Mechanisms of Di(2-ethylhexyl) Phthalate-Induced MMP-2 and MMP-9 Expression in A7r5 Rat Vascular Smooth Muscle Cells. Diethylhexyl Phthalate 23-49 matrix metallopeptidase 2 Rattus norvegicus 58-63 26717918-9 2015 After rats were fed TCMs we found that SMB extraction not only induced HGF, FAK, Cyclin D1, and pRb protein expression and Cyclin D1 mRNA increases, but also reduced MMP-2 and MMP-9 after 24 and 72 h post injury. (S)-2-methylbutanoic acid 39-42 matrix metallopeptidase 2 Rattus norvegicus 166-171 25645818-13 2015 Western blot analysis showed that puerarin (200 mg/kg) inhibited the activation of nuclear factor-kappa B p65, which is associated with lower IL-1beta and TNF-alpha production, and reduced the glycosylation of extracellular matrix metalloproteinase inducer, which is associated with lower levels of MMP-2 and MMP-9. puerarin 34-42 matrix metallopeptidase 2 Rattus norvegicus 299-304 26297928-14 2015 Moreover, isoleucine-tryptophan blunts tissue ACE activity, reduces matrix metalloproteinase-2 activity and improves coronary flow reserve. isoleucine-tryptophan 10-31 matrix metallopeptidase 2 Rattus norvegicus 68-94 25645818-14 2015 CONCLUSIONS: Puerarin reduced the alveolar bone loss and collagen destruction in rats with ligature-induced periodontitis by inhibiting the production of RANKL, IL-1beta, TNF-alpha, MMP-2 and MMP-9. puerarin 13-21 matrix metallopeptidase 2 Rattus norvegicus 182-187 26884932-0 2015 Levofloxacin increases apoptosis of rat annulus fibrosus cells via the mechanism of upregulating MMP-2 and MMP-13. Levofloxacin 0-12 matrix metallopeptidase 2 Rattus norvegicus 97-102 26343345-0 2015 Atorvastatin and sildenafil decrease vascular TGF-beta levels and MMP-2 activity and ameliorate arterial remodeling in a model of renovascular hypertension. Atorvastatin 0-12 matrix metallopeptidase 2 Rattus norvegicus 66-71 26343345-0 2015 Atorvastatin and sildenafil decrease vascular TGF-beta levels and MMP-2 activity and ameliorate arterial remodeling in a model of renovascular hypertension. Sildenafil Citrate 17-27 matrix metallopeptidase 2 Rattus norvegicus 66-71 26343345-3 2015 We hypothesized that atorvastatin and sildenafil alone or in association exert antiproliferative effects by down-regulating MMP-2 and TGF-beta, thus reducing the vascular hypertrophy induced by two kidney, one clip (2K1C) hypertension. Atorvastatin 21-33 matrix metallopeptidase 2 Rattus norvegicus 124-129 26343345-3 2015 We hypothesized that atorvastatin and sildenafil alone or in association exert antiproliferative effects by down-regulating MMP-2 and TGF-beta, thus reducing the vascular hypertrophy induced by two kidney, one clip (2K1C) hypertension. Sildenafil Citrate 38-48 matrix metallopeptidase 2 Rattus norvegicus 124-129 26343345-15 2015 Atorvastatin and sildenafil was associated with decreased vascular TGF-beta levels and MMP-2 activity in renovascular hypertensive rats, thus ameliorating the vascular remodeling. Atorvastatin 0-12 matrix metallopeptidase 2 Rattus norvegicus 87-92 26343345-15 2015 Atorvastatin and sildenafil was associated with decreased vascular TGF-beta levels and MMP-2 activity in renovascular hypertensive rats, thus ameliorating the vascular remodeling. Sildenafil Citrate 17-27 matrix metallopeptidase 2 Rattus norvegicus 87-92 26476374-7 2015 Additionally, quercetin altered the Bax/Bcl-2 ratio and reduced MMP2, MMP9, CXCR4, integrin beta1, and integrin alpha5 expression. Quercetin 14-23 matrix metallopeptidase 2 Rattus norvegicus 64-68 26884932-3 2015 The purpose of this study was to further explore the changes in extracellular matrix and MMPs of rat AF cells based on levofloxacin-induced apoptosis. Levofloxacin 119-131 matrix metallopeptidase 2 Rattus norvegicus 89-93 26884932-9 2015 Both RT-qPCR and western blot revealed that MMP-2 and MMP-13 expression were upregulated by levofloxacin treatment in a time- and dose-dependent manner. Levofloxacin 92-104 matrix metallopeptidase 2 Rattus norvegicus 44-49 26884932-11 2015 In conclusion, the results above suggest that the possible cytotoxic effects of levofloxacin on AF cells in vitro may be attributed to the decreased cell binding to type I collagen and up-regulated expression of MMP-2 and MMP-13. Levofloxacin 80-92 matrix metallopeptidase 2 Rattus norvegicus 212-217 26332145-8 2015 RESULTS: DFO remarkably enhanced expression of noted genes by mRNA and protein levels and restored activity of matrix metalloproteinases -2 and -9. Deferoxamine 9-12 matrix metallopeptidase 2 Rattus norvegicus 111-146 26260480-11 2015 MMP2 was significantly increased for PVDF on days 3 and 5 and for GPVDF on day 5. polyvinylidene fluoride 37-41 matrix metallopeptidase 2 Rattus norvegicus 0-4 26192633-0 2015 Renoprotective effects of berberine through regulation of the MMPs/TIMPs system in streptozocin-induced diabetic nephropathy in rats. Berberine 26-35 matrix metallopeptidase 2 Rattus norvegicus 62-66 26192633-2 2015 Hence, we aimed to explore the renoprotective mechanism of berberine on the accumulation of extracellular matrix, alterations of its major components and corresponding changes in the regulatory system, including the matrix metalloproteinases/tissue inhibitor of matrix metalloproteinases (MMPs/TIMPs) system, in diabetic nephropathy rats. Berberine 59-68 matrix metallopeptidase 2 Rattus norvegicus 289-293 26192633-9 2015 Berberine (100 and 200 mg/kg) could significantly improve the abnormal changes in the MMPs/TIMPs system. Berberine 0-9 matrix metallopeptidase 2 Rattus norvegicus 86-90 26192633-11 2015 Therefore, the renoprotective effects of berberine on diabetic nephropathy might be associated with changes in the extracellular matrix through the regulation of the MMPs/TIMPs system in the rat kidney. Berberine 41-50 matrix metallopeptidase 2 Rattus norvegicus 166-170 26407229-5 2015 The expression of both MMP-2 and MMP-9 was significantly inversely correlated with As2O3 concentration. Arsenic Trioxide 83-88 matrix metallopeptidase 2 Rattus norvegicus 23-28 26407229-7 2015 Thus, the inhibitory effect of As2O3 on the migration of primary neurons might be related to the reduction in MMP-2 and MMP-9 activities and decrease in beta-actin and DCX expression. Arsenic Trioxide 31-36 matrix metallopeptidase 2 Rattus norvegicus 110-115 26285173-0 2015 The anti-angiogenic action of 2-deoxyglucose involves attenuation of VEGFR2 signaling and MMP-2 expression in HUVECs. Deoxyglucose 30-44 matrix metallopeptidase 2 Rattus norvegicus 90-95 26285173-5 2015 2-DG (0.1-1.0mM) also significantly inhibited cell invasion and migration, as well as the activity and mRNA and protein expression of matrix metalloproteinase (MMP)-2 in HUVECs. Deoxyglucose 0-4 matrix metallopeptidase 2 Rattus norvegicus 134-166 26285173-8 2015 The effects of 2-DG on tube formation, MMP-2 activity, and VEGFR2 protein expression in HUVECs were reversed by mannose, an N-linked glycosylation precursor. Deoxyglucose 15-19 matrix metallopeptidase 2 Rattus norvegicus 39-44 26285173-8 2015 The effects of 2-DG on tube formation, MMP-2 activity, and VEGFR2 protein expression in HUVECs were reversed by mannose, an N-linked glycosylation precursor. Mannose 112-119 matrix metallopeptidase 2 Rattus norvegicus 39-44 26285173-10 2015 SIGNIFICANCE: This ex vivo and in vitro study demonstrates that 2-DG inhibits angiogenesis with an action involving attenuation of VEGFR2 signaling and MMP-2 expression, possibly resulting from interference with N-linked glycosylation of VEGFR2. Deoxyglucose 64-68 matrix metallopeptidase 2 Rattus norvegicus 152-157 26285173-10 2015 SIGNIFICANCE: This ex vivo and in vitro study demonstrates that 2-DG inhibits angiogenesis with an action involving attenuation of VEGFR2 signaling and MMP-2 expression, possibly resulting from interference with N-linked glycosylation of VEGFR2. Nitrogen 3-4 matrix metallopeptidase 2 Rattus norvegicus 152-157 25816715-0 2015 The Nuclear Factor kappaB Inhibitor Pyrrolidine Dithiocarbamate Prevents Cardiac Remodelling and Matrix Metalloproteinase-2 Up-Regulation in Renovascular Hypertension. pyrrolidine dithiocarbamic acid 36-63 matrix metallopeptidase 2 Rattus norvegicus 97-123 26211444-10 2015 Minocycline administration significantly reduced HIF-1alpha expression, protein and mRNA expression of MMP-2, MMP-9 and Vascular Endothelial Growth Factor (VEGF) (P<0.05), and increased TJs (ZO-1, claudin-5 and occluding) (P<0.05) in HBMECs after hypoxia. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 103-108 26409033-0 2015 Pterostilbene Inhibits Vascular Smooth Muscle Cells Migration and Matrix Metalloproteinase-2 through Modulation of MAPK Pathway. pterostilbene 0-13 matrix metallopeptidase 2 Rattus norvegicus 66-92 26409033-5 2015 Pterostilbene was also found to significantly decreased MMP-2 activity and expression by gelatin zymography and western blot assay in SMC. pterostilbene 0-13 matrix metallopeptidase 2 Rattus norvegicus 56-61 26409033-7 2015 Moreover, inhibition of Erk1/2 by specific inhibitors significantly abolished the pterostilbene-decreased expression of MMP-2 and migration/invasion capacities. pterostilbene 82-95 matrix metallopeptidase 2 Rattus norvegicus 120-125 26409033-11 2015 In this study, we found that pterostilbene could inhibit SMCs migration via down-regulation of MMP-2. pterostilbene 29-42 matrix metallopeptidase 2 Rattus norvegicus 95-100 26827542-4 2015 RESULTS: (1) High glucose promoted the phenotype transformation of VSMCs and up-regulated the expression of MMP-2 and MMP-9. Glucose 18-25 matrix metallopeptidase 2 Rattus norvegicus 108-113 26827542-6 2015 (3) SB203580, the inhibitor of P38/MAPK signal pathway, inhibited the effects of high glucose on phenotype transformation and expression of MMP-2 and MMP-9. SB 203580 4-12 matrix metallopeptidase 2 Rattus norvegicus 140-145 26827537-8 2015 Compared with Hcy group, the proliferation, migration and the expression and activity of MMP-2/9 of VSMCs were significantly decreases in the VSMCs of polypeptides group, polyphenols group and Chinese yellow wine group. Polyphenols 171-182 matrix metallopeptidase 2 Rattus norvegicus 89-96 26827542-6 2015 (3) SB203580, the inhibitor of P38/MAPK signal pathway, inhibited the effects of high glucose on phenotype transformation and expression of MMP-2 and MMP-9. Glucose 86-93 matrix metallopeptidase 2 Rattus norvegicus 140-145 26286041-8 2015 FLU has a function similar to KJ in behavior, regulation of BDNF, TrkB, MMP-2, occludin and apoptotic rates of cells. Fluoxetine 0-3 matrix metallopeptidase 2 Rattus norvegicus 72-77 25987498-0 2015 Vascular smooth muscle cell differentiation to an osteogenic phenotype involves matrix metalloproteinase-2 modulation by homocysteine. Homocysteine 121-133 matrix metallopeptidase 2 Rattus norvegicus 80-106 25987498-5 2015 MTT assays were performed to determine the cytotoxicity of the MMP-2 inhibitor in calcification medium containing 200 mumol/L HCY. Homocysteine 126-129 matrix metallopeptidase 2 Rattus norvegicus 63-68 25987498-10 2015 MMP-2 expression was increased by HCY in a dose-dependent manner in VSMCs exposed to both control and calcification medium. Homocysteine 34-37 matrix metallopeptidase 2 Rattus norvegicus 0-5 25987498-11 2015 The MMP-2 inhibitor decreased the calcium content and ALP activity, and attenuated the osteoblastic phenotype of VSMCs. Calcium 34-41 matrix metallopeptidase 2 Rattus norvegicus 4-9 25987498-11 2015 The MMP-2 inhibitor decreased the calcium content and ALP activity, and attenuated the osteoblastic phenotype of VSMCs. vsmcs 113-118 matrix metallopeptidase 2 Rattus norvegicus 4-9 25701126-4 2015 Expression of gelatinases MMP2 and MMP9, their activator MMP14 and their inhibitor tissue inhibitor of MMP (TIMP)1 in the CNS of AO and DA rats immunized with SCH+CFA was determined. sch 159-162 matrix metallopeptidase 2 Rattus norvegicus 26-30 26244437-1 2015 AIMS: To study the effects of a novel matrix metalloproteinase-2 (MMP-2) and MMP-9 inhibitor, AQU-118, on mechanical allodynia in the spinal nerve ligation (SNL) model of neuropathic pain and the chronic constriction injury of the infraorbital nerve (CCI-IoN) model of neuropathic orofacial pain. AQU-118 94-101 matrix metallopeptidase 2 Rattus norvegicus 38-64 26093650-9 2015 Aspirin-treated rats exhibited a significant decrease in degradation of internal elastic lamina (IEL), medial layer thinning, CA size and macrophages infiltration with reduced expression of MMP-2 and 9 compared with rats in the CA group. Aspirin 0-7 matrix metallopeptidase 2 Rattus norvegicus 190-195 25308714-4 2015 Here, we expand previous findings and examine whether doxycycline (a MMPs inhibitor) affects these alterations. Doxycycline 54-65 matrix metallopeptidase 2 Rattus norvegicus 69-73 25770246-12 2015 In conclusion, the present results suggest that eEF2K at least partly mediates MCT-induced PAH via stimulation of vascular structural remodeling perhaps through NADPH oxidase-1/ROS/matrix metalloproteinase-2 pathway. p-Aminohippuric Acid 91-94 matrix metallopeptidase 2 Rattus norvegicus 181-207 25623089-0 2015 STAT3-mediated MMP-2 expression is required for 15-HETE-induced vascular adventitial fibroblast migration. Hydroxyeicosatetraenoic Acids 51-55 matrix metallopeptidase 2 Rattus norvegicus 15-20 25623089-5 2015 15-HETE-induced MMP-2 expression and secretion were analyzed by Western blot and ELISA, respectively. 15-hydroxy-5,8,11,13-eicosatetraenoic acid 0-7 matrix metallopeptidase 2 Rattus norvegicus 16-21 25623089-13 2015 CONCLUSION: These results reveal that STAT3-mediated MMP-2 expression is required for 15-HETE induced-VAF migration. 15-hydroxy-5,8,11,13-eicosatetraenoic acid 86-93 matrix metallopeptidase 2 Rattus norvegicus 53-58 28962467-7 2015 GA co-treatment markedly suppressed the GO-induced elevation in mRNA expression of collagenIand III, MMP-2, MMP-9 and NOX (p < 0.05, respectively) genes as compared with GO alone infused rats. Gallic Acid 0-2 matrix metallopeptidase 2 Rattus norvegicus 101-106 25996167-12 2015 CONCLUSION: Peroxynitrite decomposition catalyst could prevent hemorrhagic transformation and improve neurological outcome ischemic rat brains with delayed t-PA treatment via inhibiting peroxynitrite-mediated MMP activation. Peroxynitrous Acid 12-25 matrix metallopeptidase 2 Rattus norvegicus 209-212 25996167-12 2015 CONCLUSION: Peroxynitrite decomposition catalyst could prevent hemorrhagic transformation and improve neurological outcome ischemic rat brains with delayed t-PA treatment via inhibiting peroxynitrite-mediated MMP activation. Peroxynitrous Acid 186-199 matrix metallopeptidase 2 Rattus norvegicus 209-212 26053757-1 2015 The aim of this study was to evaluate whether water soluble compounds present in aqueous extracts from seven Mediterranean demosponges exert biological activity towards matrix metalloproteinases (MMPs), which represent important pathogenic factors of human diseases. Water 46-51 matrix metallopeptidase 2 Rattus norvegicus 196-200 26053757-3 2015 Our results demonstrated that the studied extracts contain water soluble compounds able to inhibit MMP-2 and MMP-9 activity and expression. Water 59-64 matrix metallopeptidase 2 Rattus norvegicus 99-104 26053757-6 2015 Taken together, our results indicate that the aqueous extracts from the selected Mediterranean demosponges possess a variety of water-soluble bioactive compounds, which are able to inhibit MMPs at different levels. Water 128-133 matrix metallopeptidase 2 Rattus norvegicus 189-193 26191209-8 2015 Treatment with budesonide resulted in an obvious decrease in the MMP-1 but not MMP-2 and TIMP-2 productions (P<0.05). Budesonide 15-25 matrix metallopeptidase 2 Rattus norvegicus 79-84 25872140-0 2015 Quercetin improves postischemic recovery of heart function in doxorubicin-treated rats and prevents doxorubicin-induced matrix metalloproteinase-2 activation and apoptosis induction. Quercetin 0-9 matrix metallopeptidase 2 Rattus norvegicus 120-146 25872140-0 2015 Quercetin improves postischemic recovery of heart function in doxorubicin-treated rats and prevents doxorubicin-induced matrix metalloproteinase-2 activation and apoptosis induction. Doxorubicin 100-111 matrix metallopeptidase 2 Rattus norvegicus 120-146 25872140-6 2015 Our results showed that QCT prevented several negative chronic effects of DOX: (I) reversed DOX-induced blood pressure increase; (II) mediated improvement of deleterious effects of DOX on ultrastructure of left ventricle; (III) prevented DOX-induced effects on tissue MMP-2 activation; and (iv) reversed effects of DOX on apoptosis induction and superoxide dismutase inhibition. Doxorubicin 74-77 matrix metallopeptidase 2 Rattus norvegicus 268-273 25576297-7 2015 Further, VPA treatment significantly increased histone H3 acetylation and MMP-2 expression. Valproic Acid 9-12 matrix metallopeptidase 2 Rattus norvegicus 74-79 25872140-9 2015 Taken together, these results demonstrate that prolonged treatment with QCT prevented negative chronic effects of DOX on blood pressure, cellular damage, MMP-2 activation, and apoptosis induction. Doxorubicin 114-117 matrix metallopeptidase 2 Rattus norvegicus 154-159 25789487-8 2015 Polysaccharide and MSCs acted additively to increase the expression of anti-inflammatory cytokine (TGF-beta), antiangiogenic cytokine (TSP-1) and decrease those promoting inflammation (TNF-alpha), chemotaxis (MIP-1alpha and MCP-1) and angiogenesis (VEGF and MMP-2). Polysaccharides 0-14 matrix metallopeptidase 2 Rattus norvegicus 258-263 25389122-6 2015 MiR-29b significantly suppressed the proliferation and migration of SMCs through the inhibition of the signaling pathway related to Mcl-1 and MMP2. mir-29b 0-7 matrix metallopeptidase 2 Rattus norvegicus 142-146 25822152-6 2015 In isolated rat cardiomyocytes, mitochondrial reactive oxygen species (mitoROS) upregulated MMP-2 and MMP-9 expression, and human TFAM (hTFAM) overexpression suppressed mitoROS and their upregulation. Reactive Oxygen Species 46-69 matrix metallopeptidase 2 Rattus norvegicus 92-97 25867313-1 2015 This study investigated the effects of angiotensin II (AngII) intervention, using captopril and losartan, on the expression of matrix metalloproteinase-2 (MMP-2), MMP-9, tissue inhibitor of metalloproteinase-1 (TIMP-1), and collagen in rats with pulmonary hypertension, in an effort to understand mechanisms underlying pulmonary vascular remodeling. Captopril 82-91 matrix metallopeptidase 2 Rattus norvegicus 127-153 25867313-1 2015 This study investigated the effects of angiotensin II (AngII) intervention, using captopril and losartan, on the expression of matrix metalloproteinase-2 (MMP-2), MMP-9, tissue inhibitor of metalloproteinase-1 (TIMP-1), and collagen in rats with pulmonary hypertension, in an effort to understand mechanisms underlying pulmonary vascular remodeling. Losartan 96-104 matrix metallopeptidase 2 Rattus norvegicus 127-153 25661317-13 2015 In addition, paeoniflorin increased the phosphorylation of Src kinase and activation of MMP-2 in HEK293/A1R cells. peoniflorin 13-25 matrix metallopeptidase 2 Rattus norvegicus 88-93 25661317-14 2015 Both Src inhibitor PP2 and MMP-2/MMP-9 inhibitor BiPs not only blocked paeoniflorin-induced phosphorylation of ERK1/2 (and Akt) in HEK293/A1R cells, but also paeoniflorin-increased survival of neurons subjected to OGD/R. peoniflorin 158-170 matrix metallopeptidase 2 Rattus norvegicus 27-32 25661317-14 2015 Both Src inhibitor PP2 and MMP-2/MMP-9 inhibitor BiPs not only blocked paeoniflorin-induced phosphorylation of ERK1/2 (and Akt) in HEK293/A1R cells, but also paeoniflorin-increased survival of neurons subjected to OGD/R. peoniflorin 71-83 matrix metallopeptidase 2 Rattus norvegicus 27-32 25559243-7 2015 Not only yuzu but also hesperidin inhibited caspase-3 activity, myeloperoxidase expression, alpha-smooth muscle actin expression, and matrix metalloproteinase-2 activity in a permanent LAD occlusion rat model. Hesperidin 23-33 matrix metallopeptidase 2 Rattus norvegicus 134-160 25804229-12 2015 In turn, activation of MMPs via superoxide-depending regulation allows tumor cells to facilitate migration, invasion and finally - formation of metastatic centers. Superoxides 32-42 matrix metallopeptidase 2 Rattus norvegicus 23-27 25728227-2 2015 The results of the present study revealed that treatment with gamma-irradiation and/or ethanol showed a significant increase in ulcers number, total acidity, peptic, H(+)K(+)ATPase, MMP-2 and MMP-9 activities and MDA level, which were accompanied by a significant decrease in the mucus content, the stomach GSH level, the GSH-Px activity and DNA damage. Ethanol 87-94 matrix metallopeptidase 2 Rattus norvegicus 182-187 25671581-6 2015 Real-time RT-PCR analysis along with zymography revealed that the wound area of the hot spring water group exhibited a higher expression of matrix metalloproteinases-2 and -9 compared to the two other control groups. Water 95-100 matrix metallopeptidase 2 Rattus norvegicus 140-174 25466491-2 2015 Doxycycline has been reported to control the progression of AAA by regulation of MMP. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 81-84 25466491-3 2015 We hypothesized that doxycycline pretreatment in a rat model of AAA would cause reduction in gelatinolytic activity of MMP-2 and -9 and the inflammatory response in the wall of an aneurysm, consequently decreasing the formation and development of AAAs. Doxycycline 21-32 matrix metallopeptidase 2 Rattus norvegicus 119-131 25466491-10 2015 However, the animals treated with doxycycline showed a 85% decrease in AAA development, which was associated with a large reduction in gelatinolytic activity of MMP-2 and -9, and decreased inflammatory response (P<.05). Doxycycline 34-45 matrix metallopeptidase 2 Rattus norvegicus 161-173 25466491-11 2015 CONCLUSIONS: These results suggest that pretreatment with doxycycline before surgery inhibited the activity of MMP-2 and -9, as well as the inflammatory response, and may play an important role in the prevention of the development of AAAs. Doxycycline 58-69 matrix metallopeptidase 2 Rattus norvegicus 111-123 25600809-0 2015 Cadmium exposure inhibits MMP2 and MMP9 activities in the prostate and testis. Cadmium 0-7 matrix metallopeptidase 2 Rattus norvegicus 26-30 25600809-1 2015 Matrix metalloproteinases (MMPs) are zinc (Zn(2+)) and calcium (Ca(2+)) dependant endopeptidases, capable of degradation of numerous components of the extracellular matrix. Zinc 43-49 matrix metallopeptidase 2 Rattus norvegicus 27-31 25600809-1 2015 Matrix metalloproteinases (MMPs) are zinc (Zn(2+)) and calcium (Ca(2+)) dependant endopeptidases, capable of degradation of numerous components of the extracellular matrix. Calcium 55-62 matrix metallopeptidase 2 Rattus norvegicus 27-31 25600809-2 2015 Cadmium (Cd(2+)) is a well known environmental contaminant which could impair the activity of MMPs. Cadmium 0-7 matrix metallopeptidase 2 Rattus norvegicus 94-98 25600809-7 2015 Additionally, we performed an experiment of gelatin zymography in which 5 muM or 2 mM cadmium chloride (CdCl2) was directly dissolved at the incubation buffer, using the prostatic tissue samples from untreated animals that exhibited the highest MMP2 and MMP9 activities in the previous experiment. Cadmium Chloride 104-109 matrix metallopeptidase 2 Rattus norvegicus 245-249 25600809-8 2015 We have found that CdCl2 intake in the drinking water led to the inhibition of 35% and 30% of MMP2 and MMP9 (p < 0.05) at the ventral prostate and testis, respectively, in Cd(2+) treated animals when compared to controls. Cadmium Chloride 19-24 matrix metallopeptidase 2 Rattus norvegicus 94-98 25600809-8 2015 We have found that CdCl2 intake in the drinking water led to the inhibition of 35% and 30% of MMP2 and MMP9 (p < 0.05) at the ventral prostate and testis, respectively, in Cd(2+) treated animals when compared to controls. Water 48-53 matrix metallopeptidase 2 Rattus norvegicus 94-98 25600809-8 2015 We have found that CdCl2 intake in the drinking water led to the inhibition of 35% and 30% of MMP2 and MMP9 (p < 0.05) at the ventral prostate and testis, respectively, in Cd(2+) treated animals when compared to controls. Cadmium 19-21 matrix metallopeptidase 2 Rattus norvegicus 94-98 25600809-10 2015 These important findings demonstrate that environmental cadmium contamination may deregulate the natural balance in the extracellular matrix turnover, through MMPs downregulation, which could contribute to the toxic effects observed in prostatic and testicular tissue after its exposure. Cadmium 56-63 matrix metallopeptidase 2 Rattus norvegicus 159-163 25889169-1 2015 BACKGROUND: Minocycline reduces reperfusion injury by inhibiting matrix metalloproteinases (MMPs) and microglia activity after cerebral ischemia. Minocycline 12-23 matrix metallopeptidase 2 Rattus norvegicus 92-96 25204979-8 2015 The treatments also reduced concentrations of interleukin-1beta, granulocyte colony-stimulating factor, and matrix metalloproteinase 2 in STZ-induced diabetic bone marrow supernatant and decreased the expression of NADPH oxidase 2, nitric oxide synthase 2, and nuclear factor-kappaB1 mRNA in bone marrow progenitor cells. Streptozocin 138-141 matrix metallopeptidase 2 Rattus norvegicus 108-134 25595313-7 2015 Moreover, we found that cordycepin, a known inhibitor of VSMC migration, caused significant downregulation of MMP2, 9, and 13 expression in PDGF-treated RAoSMCs. cordycepin 24-34 matrix metallopeptidase 2 Rattus norvegicus 110-114 26258010-1 2015 We investigated whether chronic ethanol intake is capable of altering the MMP-2 and MMP-9 activities and TIMP-2 and TIMP-1 expression in the dorsal and lateral prostatic lobes of low (UChA) and high (UChB) ethanol-preferring rats. Ethanol 32-39 matrix metallopeptidase 2 Rattus norvegicus 74-79 26258010-2 2015 MMP-2 and MMP-9 activities and TIMP-1 and TIMP-2 expression were significantly reduced in the lateral prostatic lobe of the ethanol drinking animals. Ethanol 124-131 matrix metallopeptidase 2 Rattus norvegicus 0-5 26258010-4 2015 These important findings demonstrate that chronic ethanol intake impairs the physiological balance of the prostate extracellular matrix turnover, through downregulation of MMPs, which may contribute to the development of prostatic diseases. Ethanol 50-57 matrix metallopeptidase 2 Rattus norvegicus 172-176 26258010-5 2015 Furthermore, since these proteins are also components of prostate secretion, the negative impact of chronic ethanol intake on fertility may also involve reduction of MMPs and TIMPs in the seminal fluid. Ethanol 108-115 matrix metallopeptidase 2 Rattus norvegicus 166-170 26405980-3 2015 This suggests that H2S could attenuate cardiac fibrosis induced by diabetes and its mechanisms may be related to its modulation of MMPs/TIMPs expression and regulation of TGFbeta1. Hydrogen Sulfide 19-22 matrix metallopeptidase 2 Rattus norvegicus 131-135 26027825-10 2015 In conclusion, our data show that berberine improves vascular inflammation and remodeling in the MS condition, and this is correlated with the ability of berberine to inhibit p38 MAPK activation, ATF-2 phosphorylation, and MMP-2 expression. Berberine 154-163 matrix metallopeptidase 2 Rattus norvegicus 223-228 26027825-9 2015 In addition, the levels of p38 mitogen-activated protein kinase (p38 MAPK), activating transcription factor 2 (ATF-2) and matrix metalloproteinase 2 (MMP-2) were significantly decreased in the MSB group compared to the MS group. 4-Methoxybenzenesulfonamide 193-196 matrix metallopeptidase 2 Rattus norvegicus 122-148 26027825-9 2015 In addition, the levels of p38 mitogen-activated protein kinase (p38 MAPK), activating transcription factor 2 (ATF-2) and matrix metalloproteinase 2 (MMP-2) were significantly decreased in the MSB group compared to the MS group. 4-Methoxybenzenesulfonamide 193-196 matrix metallopeptidase 2 Rattus norvegicus 150-155 25871735-0 2015 Acute doxorubicin-induced cardiotoxicity is associated with matrix metalloproteinase-2 alterations in rats. Doxorubicin 6-17 matrix metallopeptidase 2 Rattus norvegicus 60-86 26770971-5 2015 Effluent matrix metalloproteinase-2 (MMP-2) levels increased in both the MGO- and FA-treated rats. Pyruvaldehyde 73-76 matrix metallopeptidase 2 Rattus norvegicus 9-35 26770971-5 2015 Effluent matrix metalloproteinase-2 (MMP-2) levels increased in both the MGO- and FA-treated rats. Pyruvaldehyde 73-76 matrix metallopeptidase 2 Rattus norvegicus 37-42 26770971-8 2015 From the PET results, the D/P Cr ratio was correlated with effluent levels of TN-C (rho = 0.57, p < 0.001) and MMP-2 (rho = 0.73, p < 0.001). Chromium 30-32 matrix metallopeptidase 2 Rattus norvegicus 114-119 25871735-9 2015 MMP-2 activity, evaluated by zymography, was increased in Doxo (Control 141338 +- 8924; Doxo 188874 +- 7652 arbitrary units; p < 0.001). Doxorubicin 58-62 matrix metallopeptidase 2 Rattus norvegicus 0-5 25871735-9 2015 MMP-2 activity, evaluated by zymography, was increased in Doxo (Control 141338 +- 8924; Doxo 188874 +- 7652 arbitrary units; p < 0.001). Doxorubicin 88-92 matrix metallopeptidase 2 Rattus norvegicus 0-5 25603456-1 2015 AIM: To study the effects of estrogen therapy, alone or combined with progestogens, and of tibolone on the expression of heparanase (HSPE), extracellular matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9), perlecan and proliferating cell nuclear antigen (PCNA) in normal breast tissue. tibolone 91-99 matrix metallopeptidase 2 Rattus norvegicus 189-194 26088607-8 2015 RESULT: In vivo, NaHS treatment inhibited hyperglycemia-induced expression of type I and III collagen, MMP-2 and MMP-9 in diabetic hearts. sodium bisulfide 17-21 matrix metallopeptidase 2 Rattus norvegicus 103-108 26088607-11 2015 ROS production, ERK1/2 phosphorylation and MMP-2 and 9 expression were decreased in rat neonatal cardiac fibroblasts treated with GYY4137 and NOX4 siRNA. GYY 4137 130-137 matrix metallopeptidase 2 Rattus norvegicus 43-48 25791818-11 2015 CONCLUSIONS: These findings indicate that (-)-DHMEQ suppressed mast cell migration via the inhibition of NF-kappaB-regulated MMP-2 expression. dehydroxymethylepoxyquinomicin 42-51 matrix metallopeptidase 2 Rattus norvegicus 125-130 26662652-9 2015 L-arg supplementation protected against increases in MMP-2 and MMP-9 in Group 3 (A) and 4 (AC). Arginine 0-5 matrix metallopeptidase 2 Rattus norvegicus 53-58 26662652-10 2015 CONCLUSIONS: L-arginine could protect from an increase in visceral fat through a change in the activity of MMPs and amelioration of insulin sensitivity in rats fed a HFD. Arginine 13-23 matrix metallopeptidase 2 Rattus norvegicus 107-111 26199464-6 2015 The inhibition of MMPs by dexamethasone was significantly lower than that by doxycycline, while the rescue of syndecan-1 expression from LPS-induced endotoxemic rat thoracic aorta was significantly higher in the dexamethasone-treated compared to the doxycycline-treated (p = 0.03). Dexamethasone 26-39 matrix metallopeptidase 2 Rattus norvegicus 18-22 25791818-0 2015 Inhibition of MMP-2-Mediated Mast Cell Invasion by NF-kappaB Inhibitor DHMEQ in Mast Cells. dehydroxymethylepoxyquinomicin 71-76 matrix metallopeptidase 2 Rattus norvegicus 14-19 25791818-8 2015 (-)-DHMEQ was found to lower the expression of matrix metalloproteinase (MMP)-2. dehydroxymethylepoxyquinomicin 0-9 matrix metallopeptidase 2 Rattus norvegicus 47-79 25119556-10 2015 CONCLUSIONS: CsA inhibited the expressions of gelatinase MMPs and EMMPRIN and partially prevented the periodontal breakdown in ligature-induced experimental periodontitis. Cyclosporine 13-16 matrix metallopeptidase 2 Rattus norvegicus 57-61 25119556-11 2015 The CsA-induced attenuation of periodontal bone loss was strongly correlated positively with the expressions of MMP-2, MMP-9, and EMMPRIN in gingiva. Cyclosporine 4-7 matrix metallopeptidase 2 Rattus norvegicus 112-117 26199464-6 2015 The inhibition of MMPs by dexamethasone was significantly lower than that by doxycycline, while the rescue of syndecan-1 expression from LPS-induced endotoxemic rat thoracic aorta was significantly higher in the dexamethasone-treated compared to the doxycycline-treated (p = 0.03). Dexamethasone 212-225 matrix metallopeptidase 2 Rattus norvegicus 18-22 26199464-3 2015 Animals of treatment groups were also given either dexamethasone (4 mg/kg, 30 min prior to LPS injection) or the matrix metalloproteinases (MMPs) inhibitor doxycycline (4 mg/kg, 30 min after LPS injection). Doxycycline 156-167 matrix metallopeptidase 2 Rattus norvegicus 140-144 26199464-8 2015 Both dexamethasone and doxycycline inhibit activation of MMPs that may contribute to the rescue of ZO-1 and syndecan-1 expression. Dexamethasone 5-18 matrix metallopeptidase 2 Rattus norvegicus 57-61 26199464-5 2015 Both dexamethasone and doxycycline could significantly inhibit MMPs activity and reserve the expressions of ZO-1 and syndecan-1. Dexamethasone 5-18 matrix metallopeptidase 2 Rattus norvegicus 63-67 26199464-8 2015 Both dexamethasone and doxycycline inhibit activation of MMPs that may contribute to the rescue of ZO-1 and syndecan-1 expression. Doxycycline 23-34 matrix metallopeptidase 2 Rattus norvegicus 57-61 26199464-5 2015 Both dexamethasone and doxycycline could significantly inhibit MMPs activity and reserve the expressions of ZO-1 and syndecan-1. Doxycycline 23-34 matrix metallopeptidase 2 Rattus norvegicus 63-67 25362529-11 2014 CONCLUSION: Diclofenac has an impact on the levels of MMP-2, MMP-3 and MMP-13, which are needed for normal healing process, and it can also lead to disruption of tendon healing. Diclofenac 12-22 matrix metallopeptidase 2 Rattus norvegicus 54-59 25501750-9 2014 Moreover, L-ARG increased MMP-2 expression in addition to its protein content while decreasing expression of PAI-1. Arginine 10-15 matrix metallopeptidase 2 Rattus norvegicus 26-31 26016225-12 2015 Tamoxifen induced an inhibition of myocardial MMP-2 and MMP-9 activity in the control and diabetic rats. Tamoxifen 0-9 matrix metallopeptidase 2 Rattus norvegicus 46-51 26016225-14 2015 Tamoxifen inhibits myocardial CD147 glycosylation and further depress the activity of MMPs. Tamoxifen 0-9 matrix metallopeptidase 2 Rattus norvegicus 86-90 25415648-5 2014 Hydantoin 13 had excellent selectivity over other zinc metalloproteases such as TACE, MMP2, MMP3, MMP13, and MMP14. hydantoin 13 0-12 matrix metallopeptidase 2 Rattus norvegicus 86-90 25281199-8 2014 The final results indicated that Artesunate could dramatically attenuate the extent of hepatic fibrosis showed by histopathological sections of hepatic tissues, significantly decrease the content of hydroxyproline and efficiently inhibit the protein expression of MMP-2, MMP-9, alpha-SMA and type I collagen. Artesunate 33-43 matrix metallopeptidase 2 Rattus norvegicus 264-269 25281199-10 2014 In conclusion, the results not only suggested that Artesunate could ameliorate hepatic fibrosis, but also suggested the anti-fibrogenic mechanisms of Artesunate might be associated with inhibiting the activation of HSCs, decreasing the expression of MMP-2, MMP-9 and increasing the expression of MMP-13.These results would bring new insights for the treatment for hepatic fibrosis. Artesunate 150-160 matrix metallopeptidase 2 Rattus norvegicus 250-255 25362529-2 2014 Use of diclofenac sodium following rotator cuff repair can disrupt healing of tendon through acting on MMPs. Diclofenac 7-24 matrix metallopeptidase 2 Rattus norvegicus 103-107 25300058-10 2014 There were also significant reductions in VEGF immunoreactivity scores and both stroma and epithelium MMP-2 and MMP-9 immunoreactivity scores in the propranolol-treated group compared with the control group (p<0.005 for all scores). Propranolol 149-160 matrix metallopeptidase 2 Rattus norvegicus 102-107 25326689-2 2014 We found enduring increases in MMP-2 activity in rats after withdrawal from self-administered cocaine and transient increases in MMP-9 during cue-induced cocaine relapse. Cocaine 94-101 matrix metallopeptidase 2 Rattus norvegicus 31-36 25636275-11 2014 High glucose condition could inhibit the secretion of CXCR-4 and mRNA expression of CXCR-4 and MMP-2. Glucose 5-12 matrix metallopeptidase 2 Rattus norvegicus 95-100 25300058-11 2014 CONCLUSIONS: Propranolol may suppress endometrial tissue by its antiangiogenic activity through inhibitory actions on VEGF, MMP-2, and MMP-9. Propranolol 13-24 matrix metallopeptidase 2 Rattus norvegicus 124-129 24909904-9 2014 Compared with those in TAA group, celecoxib significantly downregulated the hepatic expressions of TNF-alpha, IL-6, COX-2, PGE2 , MMP-2, MMP-9, TGF-beta1, Phospho-Smad2/3, Snail1, alpha-SMA, FSP-1, and vimentin while greatly restoring the levels of E-cadherin. Celecoxib 34-43 matrix metallopeptidase 2 Rattus norvegicus 130-135 25158309-0 2014 Matrix metalloproteinase-2 is downregulated in sciatic nerve by streptozotocin induced diabetes and/or treatment with minocycline: Implications for nerve regeneration. Streptozocin 64-78 matrix metallopeptidase 2 Rattus norvegicus 0-26 25158309-0 2014 Matrix metalloproteinase-2 is downregulated in sciatic nerve by streptozotocin induced diabetes and/or treatment with minocycline: Implications for nerve regeneration. Minocycline 118-129 matrix metallopeptidase 2 Rattus norvegicus 0-26 25158309-1 2014 Minocycline is an inhibitor of matrix metalloproteinases (MMPs) and has been shown to have analgesic effects. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 58-62 25158309-5 2014 We show that MMP-2 is expressed constitutively in the sciatic nerve in vivo and treatment with minocycline or diabetes leads to downregulation of MMP-2 expression and activity. Minocycline 95-106 matrix metallopeptidase 2 Rattus norvegicus 13-18 25158309-5 2014 We show that MMP-2 is expressed constitutively in the sciatic nerve in vivo and treatment with minocycline or diabetes leads to downregulation of MMP-2 expression and activity. Minocycline 95-106 matrix metallopeptidase 2 Rattus norvegicus 146-151 25158309-7 2014 Minocycline reduces levels of MMP-2 mRNA and nerve growth factor-induced neurite outgrowth. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 30-35 25158309-11 2014 Minocycline treatment also downregulates MMP-2 activity and is associated with inhibitory effects on sensory neurons. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 41-46 25151216-10 2014 Further, tangeretin treatment arrested the cancer cell division at the G1/S phase via p53/p21 up-regulation and inhibited metastasis by suppressing matrix metalloproteinase (MMP)-2, MMP-9 and vascular endothelial growth factor. tangeretin 9-19 matrix metallopeptidase 2 Rattus norvegicus 148-180 25047892-6 2014 Moreover, the same pretreatment with MMP-2 inhibitor reduced thrombin-induced VSMC proliferation by 45 %. vsmc 78-82 matrix metallopeptidase 2 Rattus norvegicus 37-42 25047892-8 2014 These results further suggest that thrombin acts through EGFR and ERK 1/2 signaling pathways involving MMP-2 to upregulate proliferation of VSMC. vsmc 140-144 matrix metallopeptidase 2 Rattus norvegicus 103-108 24880485-0 2014 Carvacrol modulates instability of xenobiotic metabolizing enzymes and downregulates the expressions of PCNA, MMP-2, and MMP-9 during diethylnitrosamine-induced hepatocarcinogenesis in rats. carvacrol 0-9 matrix metallopeptidase 2 Rattus norvegicus 110-115 25333278-7 2014 However, Antioxidant N-acetylcysteine (NAC) treatment inhibited MMP2 expression and activity, and partially reversed cell apoptosis and insulin secretion dysfunction induced by AGE. Acetylcysteine 21-37 matrix metallopeptidase 2 Rattus norvegicus 64-68 25333278-7 2014 However, Antioxidant N-acetylcysteine (NAC) treatment inhibited MMP2 expression and activity, and partially reversed cell apoptosis and insulin secretion dysfunction induced by AGE. Acetylcysteine 39-42 matrix metallopeptidase 2 Rattus norvegicus 64-68 24988912-4 2014 The DP group also exhibited hyperglycaemia and hypotestosteronemia, higher cell proliferation and AR expression, a reduction in alpha-actin (possibly interfering with the reproductive function of the prostate), and enhanced activity of MMP-2, although the absolute content of MMP-2 was lower in this group. dp 4-6 matrix metallopeptidase 2 Rattus norvegicus 236-241 24988912-4 2014 The DP group also exhibited hyperglycaemia and hypotestosteronemia, higher cell proliferation and AR expression, a reduction in alpha-actin (possibly interfering with the reproductive function of the prostate), and enhanced activity of MMP-2, although the absolute content of MMP-2 was lower in this group. dp 4-6 matrix metallopeptidase 2 Rattus norvegicus 276-281 25272092-2 2014 SMTL-B contains a calponin-homology domain and is structurally similar to cardiac troponin T. As calponin-1 and troponin T are proteolyzed by intracellular matrix metalloproteinase (MMP)-2 in oxidative stress injury, we hypothesized that SMTL-B is also cleaved by MMP-2 and contributes to lipopolysaccharide (LPS)-induced vascular hypocontractility. smtl-b 0-6 matrix metallopeptidase 2 Rattus norvegicus 156-188 25272092-2 2014 SMTL-B contains a calponin-homology domain and is structurally similar to cardiac troponin T. As calponin-1 and troponin T are proteolyzed by intracellular matrix metalloproteinase (MMP)-2 in oxidative stress injury, we hypothesized that SMTL-B is also cleaved by MMP-2 and contributes to lipopolysaccharide (LPS)-induced vascular hypocontractility. smtl-b 0-6 matrix metallopeptidase 2 Rattus norvegicus 264-269 25077715-8 2014 In the rat muscle DEX induced atrophy model, Titin-MMP2 fragment was decreased in the beginning of DEX treatment, and then significantly increased later on during DEX administration. Dexamethasone 18-21 matrix metallopeptidase 2 Rattus norvegicus 51-55 25077715-8 2014 In the rat muscle DEX induced atrophy model, Titin-MMP2 fragment was decreased in the beginning of DEX treatment, and then significantly increased later on during DEX administration. Dexamethasone 99-102 matrix metallopeptidase 2 Rattus norvegicus 51-55 25077715-8 2014 In the rat muscle DEX induced atrophy model, Titin-MMP2 fragment was decreased in the beginning of DEX treatment, and then significantly increased later on during DEX administration. Dexamethasone 99-102 matrix metallopeptidase 2 Rattus norvegicus 51-55 24011462-11 2014 CONCLUSIONS: Controlled release of ascorbic acid using gelatin hydrogel sheet-attenuated AAA formation through antioxidant and anti-inflammatory effect, regulation of MMP-2, TIMP-1, and TIMP-2, and preserving elastin and collagen in this animal model. Ascorbic Acid 35-48 matrix metallopeptidase 2 Rattus norvegicus 167-172 27122821-6 2014 Curcumin-treated cardiac fibroblasts had increased matrix metalloproteinase (MMP)-2 activity in the presence of Ang II treatment. Curcumin 0-8 matrix metallopeptidase 2 Rattus norvegicus 51-83 24802761-7 2014 PD98059 or NF-kappaB signal pathway selective inhibitor Bay 11-7082 effectively blocked TNF-alpha-induced expression of MMP-2 in rat MCs, as determined by gene and protein expression. 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 0-7 matrix metallopeptidase 2 Rattus norvegicus 120-125 24802761-7 2014 PD98059 or NF-kappaB signal pathway selective inhibitor Bay 11-7082 effectively blocked TNF-alpha-induced expression of MMP-2 in rat MCs, as determined by gene and protein expression. 3-(4-methylphenylsulfonyl)-2-propenenitrile 56-67 matrix metallopeptidase 2 Rattus norvegicus 120-125 24929859-8 2014 Furthermore, in MCT-treated rats, oral administration of MAG-DPA decreased NF-kappaB and p38 MAPK activation, leading to a reduction in MMP-2, MMP-9, and VEGF expression levels in lung tissue homogenates. 1-O-docosapentaenoylglycerol 57-64 matrix metallopeptidase 2 Rattus norvegicus 136-141 25276370-8 2014 In addition, the protein expression of collagen I as well as collagen III and the ratio of mRNA levels of MMP2/TIMP2 were the highest in CIH group but the lowest in NC group, with CIH + Ad group in between. cih 137-140 matrix metallopeptidase 2 Rattus norvegicus 106-110 25276370-8 2014 In addition, the protein expression of collagen I as well as collagen III and the ratio of mRNA levels of MMP2/TIMP2 were the highest in CIH group but the lowest in NC group, with CIH + Ad group in between. cih 180-183 matrix metallopeptidase 2 Rattus norvegicus 106-110 25143788-0 2014 Ramipril inhibits AGE-RAGE-induced matrix metalloproteinase-2 activation in experimental diabetic nephropathy. Ramipril 0-8 matrix metallopeptidase 2 Rattus norvegicus 35-61 25122164-10 2014 The improvement of QSYQ was accompanied with a restoration of angiotensin II-NADPHoxidase-ROS-MMPs pathways. ros 90-93 matrix metallopeptidase 2 Rattus norvegicus 94-98 25143788-4 2014 We examined here the involvement of AGE and RAS in MMP-2 activation in streptozotocin (STZ)-induced diabetic rats and in AGE-exposed rat renal proximal tubular cells (RPTCs). Streptozocin 71-85 matrix metallopeptidase 2 Rattus norvegicus 51-56 25143788-4 2014 We examined here the involvement of AGE and RAS in MMP-2 activation in streptozotocin (STZ)-induced diabetic rats and in AGE-exposed rat renal proximal tubular cells (RPTCs). Streptozocin 87-90 matrix metallopeptidase 2 Rattus norvegicus 51-56 25143788-9 2014 RESULTS: AGE and RAGE expression levels and MMP-2 activity in the tubules of diabetic rats was significantly increased in association with increased albuminuria, all of which were blocked by ramipril. Ramipril 191-199 matrix metallopeptidase 2 Rattus norvegicus 44-49 25143788-11 2014 Ramiprilat or BAY11-7082 inhibited the AGE-induced MMP-2 activation or reactive oxygen species generation in RPTCs. ramiprilat 0-10 matrix metallopeptidase 2 Rattus norvegicus 51-56 25143788-11 2014 Ramiprilat or BAY11-7082 inhibited the AGE-induced MMP-2 activation or reactive oxygen species generation in RPTCs. 3-(4-methylphenylsulfonyl)-2-propenenitrile 14-24 matrix metallopeptidase 2 Rattus norvegicus 51-56 25143788-12 2014 Angiotensin II increased MMP-2 gene expression in RPTCs, which was blocked by BAY11-7082. 3-(4-methylphenylsulfonyl)-2-propenenitrile 78-88 matrix metallopeptidase 2 Rattus norvegicus 25-30 25143788-14 2014 Blockade of AGE-RAGE axis by ramipril may protect against DN partly via suppression of MMP-2. Ramipril 29-37 matrix metallopeptidase 2 Rattus norvegicus 87-92 24972653-4 2014 Downregulation of NF-kappaB, cyclin D1, cyclin E1, matrix metalloproteinases (MMP)-2, MMP-9, and proliferating cell nuclear antigen (PCNA) were noted in EA-treated experimental rats and controlled inflammation mediated liver cancer when compared to the diethylnitrosamine (DEN)-induced group. Ellagic Acid 153-155 matrix metallopeptidase 2 Rattus norvegicus 51-84 24930357-12 2014 CONCLUSION: CG could protect BBB integrity in experimental cerebral ischemia-reperfusion injury via regulating NO/cav-1/MMPs pathway. calycosin-7-O-beta-D-glucoside 12-14 matrix metallopeptidase 2 Rattus norvegicus 120-124 24482159-10 2014 The physical and chemical properties of sAB allow increased autocrine expression of VEGF, MMP-2 and MMP-9, favoring bone formation/remodeling with very good healing of cranial defects when compared to natural repair in the CSD-control. sab 40-43 matrix metallopeptidase 2 Rattus norvegicus 90-95 24685074-0 2014 Erythropoietin modulates imbalance of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in doxorubicin-induced cardiotoxicity. Doxorubicin 112-123 matrix metallopeptidase 2 Rattus norvegicus 38-64 24685074-8 2014 Compared to the control group, the expression of MMP-2 was up-regulated whereas that of TIMP-2 was down-regulated in the DOX group. Doxorubicin 121-124 matrix metallopeptidase 2 Rattus norvegicus 49-54 24685074-10 2014 CONCLUSIONS: The present study suggests that EPO can exert a cardioprotective effect on DOX-induced cardiotoxicity which may be associated with improving MMP-2/TIMP-2 imbalance. Doxorubicin 88-91 matrix metallopeptidase 2 Rattus norvegicus 154-159 24769130-6 2014 Treatment with daidzein reduced the expression of Matrix metalloproteinase 2 (MMP-2) and increased the expression of Tissue inhibitor of matrixmetalloproteinases 1 (TIMP 1). daidzein 15-23 matrix metallopeptidase 2 Rattus norvegicus 50-76 24769130-6 2014 Treatment with daidzein reduced the expression of Matrix metalloproteinase 2 (MMP-2) and increased the expression of Tissue inhibitor of matrixmetalloproteinases 1 (TIMP 1). daidzein 15-23 matrix metallopeptidase 2 Rattus norvegicus 78-83 24787389-9 2014 CONCLUSION: Hcy can increase intestinal permeability and aggravate inflammatory damage in rats with TNBS-induced colitis, the underlying mechanisms of which may be attributed to its effects of promoting the expression of MMP-2 and MMP-9, leading to injury of the intestinal barrier. Homocysteine 12-15 matrix metallopeptidase 2 Rattus norvegicus 221-226 24929536-11 2014 At 6 wk, the doxycycline-treated MFI group showed a significant decrease in MMP-2, an increase in MMP-3, and no change in MMP-9. Doxycycline 13-24 matrix metallopeptidase 2 Rattus norvegicus 76-81 24929536-12 2014 At 12 wk, MMP-9 showed a remarkable reduction, whereas MMP-2 and -3 protein levels increased in the doxycycline-treated MFI group. Doxycycline 100-111 matrix metallopeptidase 2 Rattus norvegicus 55-67 24618002-11 2014 Importantly, sophocarpine (20 and 40 mg/kg) decreased pro-inflammatory cytokine levels (IL-6, 14.6% and 18.5%; IL-1beta, 23.1% and 32.6%), collagen content (27.7% and 50.1%), as well as matrix metalloproteinases-2, 9 (MMP-2, 9) expression (MMP-2, 11.8% and 18.5%; MMP-9, 16.2% and 21.1%). sophocarpine 13-25 matrix metallopeptidase 2 Rattus norvegicus 218-226 24859152-0 2014 Tanshinone IIA reduces the risk of Alzheimer"s disease by inhibiting iNOS, MMP-2 and NF-kappaBp65 transcription and translation in the temporal lobes of rat models of Alzheimer"s disease. tanshinone 0-14 matrix metallopeptidase 2 Rattus norvegicus 75-80 24792035-4 2014 Treatment with either the Rho-associated protein kinase (ROCK) inhibitor Y-27632 or suppression of ROCK-1/2 by small interfering RNA technology significantly reduced the MMP-2 expression, thus suggesting that ROCK regulates such expression. Y 27632 73-80 matrix metallopeptidase 2 Rattus norvegicus 170-175 24792035-5 2014 Similar results were observed when VSMC were pretreated with either U0126 or SB203580, which are selective inhibitors of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase, respectively, thus suggesting that these kinases are important for the induction of MMP-2 expression by PDGF-BB. vsmc 35-39 matrix metallopeptidase 2 Rattus norvegicus 285-290 24792035-5 2014 Similar results were observed when VSMC were pretreated with either U0126 or SB203580, which are selective inhibitors of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase, respectively, thus suggesting that these kinases are important for the induction of MMP-2 expression by PDGF-BB. U 0126 68-73 matrix metallopeptidase 2 Rattus norvegicus 285-290 24792035-5 2014 Similar results were observed when VSMC were pretreated with either U0126 or SB203580, which are selective inhibitors of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase, respectively, thus suggesting that these kinases are important for the induction of MMP-2 expression by PDGF-BB. SB 203580 77-85 matrix metallopeptidase 2 Rattus norvegicus 285-290 24618002-11 2014 Importantly, sophocarpine (20 and 40 mg/kg) decreased pro-inflammatory cytokine levels (IL-6, 14.6% and 18.5%; IL-1beta, 23.1% and 32.6%), collagen content (27.7% and 50.1%), as well as matrix metalloproteinases-2, 9 (MMP-2, 9) expression (MMP-2, 11.8% and 18.5%; MMP-9, 16.2% and 21.1%). sophocarpine 13-25 matrix metallopeptidase 2 Rattus norvegicus 218-223 25024745-13 2014 In vitro treatment of CD90+ cells with Mocetinostat reversed myofibroblast phenotype as indicated by a decrease in alpha-Smooth muscle actin (alpha-SMA), Collagen III, and Matrix metalloproteinase-2 (MMP2). mocetinostat 39-51 matrix metallopeptidase 2 Rattus norvegicus 172-198 25024745-13 2014 In vitro treatment of CD90+ cells with Mocetinostat reversed myofibroblast phenotype as indicated by a decrease in alpha-Smooth muscle actin (alpha-SMA), Collagen III, and Matrix metalloproteinase-2 (MMP2). mocetinostat 39-51 matrix metallopeptidase 2 Rattus norvegicus 200-204 24976727-12 2014 Sorafenib was the only drug that also upregulated the expression of matrix metalloproteinase-2 and reduced the secretion of TGF-beta1 protein. Sorafenib 0-9 matrix metallopeptidase 2 Rattus norvegicus 68-94 24631744-8 2014 In this connection, our findings show that matrix metalloproteinases inhibitory peptide which is CLP is labeled with (99m)Tc with high yield and radiolabeled peptide might be might be utilized for the imaging of gelatinase activity due to overexpression of MMP-2 and MMP-9 in tumor tissue. Technetium 122-124 matrix metallopeptidase 2 Rattus norvegicus 257-262 24819928-0 2014 Azilsartan increases levels of IL-10, down-regulates MMP-2, MMP-9, RANKL/RANK, Cathepsin K and up-regulates OPG in an experimental periodontitis model. azilsartan 0-10 matrix metallopeptidase 2 Rattus norvegicus 53-58 24926361-0 2014 Curcumin suppresses tumor necrosis factor-alpha-induced matrix metalloproteinase-2 expression and activity in rat vascular smooth muscle cells via the NF-kappaB pathway. Curcumin 0-8 matrix metallopeptidase 2 Rattus norvegicus 56-82 24926361-3 2014 Reverse transcription-polymerase chain reaction and western blot analysis were used to determine the MMP-2 mRNA and protein expression levels in TNF-alpha-stimulated VSMCs. vsmcs 166-171 matrix metallopeptidase 2 Rattus norvegicus 101-106 24824358-0 2014 Deep sea water prevents balloon angioplasty-induced hyperplasia through MMP-2: an in vitro and in vivo study. Water 9-14 matrix metallopeptidase 2 Rattus norvegicus 72-77 24926361-7 2014 In addition, curcumin inhibited the TNF-alpha-induced induction of MMP-2 activity and expression. Curcumin 13-21 matrix metallopeptidase 2 Rattus norvegicus 67-72 24926361-9 2014 Signal transduction experiments indicated that TNF-alpha-induced MMP-2 expression in VSMCs was partly reversed with the application of an NF-kappaB inhibitor (BAY11-7082). 3-(4-methylphenylsulfonyl)-2-propenenitrile 159-169 matrix metallopeptidase 2 Rattus norvegicus 65-70 24926361-11 2014 Therefore, these observations indicated that curcumin suppressed TNF-alpha-stimulated VSMC migration and partially prevented TNF-alpha-induced MMP-2 expression and activity in VSMCs via the NF-kappaB pathway. Curcumin 45-53 matrix metallopeptidase 2 Rattus norvegicus 143-148 24819928-6 2014 RESULTS: Treatment with 5 mg/kg AZT resulted in reduced MPO (p<0.05) and IL-1beta (p<0.05), increased levels of IL-10 (p<0.05), and reduced expression of MMP-2, MMP-9, COX-2, RANK, RANKL, cathepsin K, and increased expression of OPG. azilsartan 32-35 matrix metallopeptidase 2 Rattus norvegicus 163-168 24802298-8 2014 The expression of gelatinases in rats induced by WS or CS exposure was markedly increased in whole lung tissue, and immunohistochemistry showed that MMP9, MMP2 and TIMP1 were primarily expressed in the airway epithelium. Cesium 55-57 matrix metallopeptidase 2 Rattus norvegicus 155-159 24160412-0 2014 The effects of alpha-lipoic acid on MMP-2 and MMP-9 activities in a rat renal ischemia and re-perfusion model. Thioctic Acid 15-32 matrix metallopeptidase 2 Rattus norvegicus 36-41 24360976-4 2014 At the molecular level, pretreatment with honokiol blocked TNF-alpha-induced protein expression of matrix metalloproteinase (MMP)-2 and MMP-9, nuclear factor (NF)-kappaB activation, and extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylation. honokiol 42-50 matrix metallopeptidase 2 Rattus norvegicus 99-131 24160412-2 2014 We investigated the possible preventive effect of alpha-lipoic acid (LA) in a renal I-R injury model in rats by assessing its reducing effect on the expression and activation of MMP-2 and MMP-9 induced by I-R. Thioctic Acid 50-67 matrix metallopeptidase 2 Rattus norvegicus 178-183 24855831-5 2014 After drugs treatment, irbesartan and the drug combination remarkably decreased SBP, LVMI, contents of angiotensinII (AngII), hydroxyproline and collagen, the mRNA and protein expression levels of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) (P < or = 0.05). Irbesartan 23-33 matrix metallopeptidase 2 Rattus norvegicus 197-223 24308702-4 2014 In CMECs, extracellular Ub increased protein levels of VEGF-A and MMP-2, known angiogenesis regulators. BM 24-26 matrix metallopeptidase 2 Rattus norvegicus 66-71 24855831-5 2014 After drugs treatment, irbesartan and the drug combination remarkably decreased SBP, LVMI, contents of angiotensinII (AngII), hydroxyproline and collagen, the mRNA and protein expression levels of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) (P < or = 0.05). Irbesartan 23-33 matrix metallopeptidase 2 Rattus norvegicus 225-230 24855831-7 2014 Therefore, emodin, irbesartan or two drugs together can potentially inhibit the ventricular fibrosis in Goldblatt hypertensive rats by reducing MMP-2 and TIMP-2 expression. Irbesartan 19-29 matrix metallopeptidase 2 Rattus norvegicus 144-149 24722316-6 2014 Our results revealed that MMP-2 and MMP-9 were obviously increased in both mRNA and protein level after H2S exposure, and they could be inhibited by MMP inhibitor doxycycline (DOX) in rat model. Hydrogen Sulfide 104-107 matrix metallopeptidase 2 Rattus norvegicus 26-31 24743169-9 2014 By immunofluorescence we observed an increase in MMP-2 and TIMP-1 staining in aortas of oxygen-exposed rats whereas TIMP-2 staining was reduced, indicating a shift in the balance towards degradation of the extra-cellular matrix and increased deposition of collagen. Oxygen 88-94 matrix metallopeptidase 2 Rattus norvegicus 49-54 24966898-6 2014 These results suggest that MMP-2 and MMP-9 may play a significant role in blood-brain barrier disruption after alcohol abuse. Alcohols 111-118 matrix metallopeptidase 2 Rattus norvegicus 27-32 24722316-0 2014 Dexamethasone ameliorates H2S-induced acute lung injury by alleviating matrix metalloproteinase-2 and -9 expression. Dexamethasone 0-13 matrix metallopeptidase 2 Rattus norvegicus 71-104 24722316-0 2014 Dexamethasone ameliorates H2S-induced acute lung injury by alleviating matrix metalloproteinase-2 and -9 expression. Hydrogen Sulfide 26-29 matrix metallopeptidase 2 Rattus norvegicus 71-104 24861934-0 2014 Cypermethrin induces astrocyte damage: role of aberrant Ca(2+), ROS, JNK, P38, matrix metalloproteinase 2 and migration related reelin protein. cypermethrin 0-12 matrix metallopeptidase 2 Rattus norvegicus 79-105 24560960-10 2014 These effects on MMP/TIMP balance were inhibited by L-NAME administration (an eNOS inhibitor, 10mg/kg). NG-Nitroarginine Methyl Ester 52-58 matrix metallopeptidase 2 Rattus norvegicus 17-20 24722316-6 2014 Our results revealed that MMP-2 and MMP-9 were obviously increased in both mRNA and protein level after H2S exposure, and they could be inhibited by MMP inhibitor doxycycline (DOX) in rat model. Doxycycline 163-174 matrix metallopeptidase 2 Rattus norvegicus 26-31 24722316-1 2014 Acute lung injury (ALI) is one of the fatal outcomes after exposure to high levels of hydrogen sulfide (H2S), and the matrix metalloproteinases (MMPs) especially MMP-2 and MMP-9 are believed to be involved in the development of ALI by degrading the extracellular matrix (ECM) of blood-air barrier. Hydrogen Sulfide 86-102 matrix metallopeptidase 2 Rattus norvegicus 145-149 24722316-1 2014 Acute lung injury (ALI) is one of the fatal outcomes after exposure to high levels of hydrogen sulfide (H2S), and the matrix metalloproteinases (MMPs) especially MMP-2 and MMP-9 are believed to be involved in the development of ALI by degrading the extracellular matrix (ECM) of blood-air barrier. Hydrogen Sulfide 86-102 matrix metallopeptidase 2 Rattus norvegicus 162-167 24722316-6 2014 Our results revealed that MMP-2 and MMP-9 were obviously increased in both mRNA and protein level after H2S exposure, and they could be inhibited by MMP inhibitor doxycycline (DOX) in rat model. Doxycycline 176-179 matrix metallopeptidase 2 Rattus norvegicus 26-31 24722316-1 2014 Acute lung injury (ALI) is one of the fatal outcomes after exposure to high levels of hydrogen sulfide (H2S), and the matrix metalloproteinases (MMPs) especially MMP-2 and MMP-9 are believed to be involved in the development of ALI by degrading the extracellular matrix (ECM) of blood-air barrier. Hydrogen Sulfide 104-107 matrix metallopeptidase 2 Rattus norvegicus 162-167 24722316-3 2014 The present work was aimed to investigate the roles of MMP-2 and MMP-9 in H2S-induced ALI and the protective effects of DXM. Hydrogen Sulfide 74-77 matrix metallopeptidase 2 Rattus norvegicus 55-60 24722316-7 2014 Moreover, DXM significantly ameliorated the symptoms of H2S-induced ALI including alveolar edema, infiltration of inflammatory cells and the protein leakage in BAFL via up-regulating glucocorticoid receptor(GR) to mediate the suppression of MMP-2 and MMP-9. Dexamethasone 10-13 matrix metallopeptidase 2 Rattus norvegicus 241-246 24722316-7 2014 Moreover, DXM significantly ameliorated the symptoms of H2S-induced ALI including alveolar edema, infiltration of inflammatory cells and the protein leakage in BAFL via up-regulating glucocorticoid receptor(GR) to mediate the suppression of MMP-2 and MMP-9. Hydrogen Sulfide 56-59 matrix metallopeptidase 2 Rattus norvegicus 241-246 24722316-9 2014 Our results, taken together, demonstrated that MMP-2 and MMP-9 were involved in the development of H2S-induced ALI and DXM exerted protective effects by alleviating the expression of MMP-2 and MMP-9. Hydrogen Sulfide 99-102 matrix metallopeptidase 2 Rattus norvegicus 47-52 24722316-9 2014 Our results, taken together, demonstrated that MMP-2 and MMP-9 were involved in the development of H2S-induced ALI and DXM exerted protective effects by alleviating the expression of MMP-2 and MMP-9. Hydrogen Sulfide 99-102 matrix metallopeptidase 2 Rattus norvegicus 183-188 24722316-9 2014 Our results, taken together, demonstrated that MMP-2 and MMP-9 were involved in the development of H2S-induced ALI and DXM exerted protective effects by alleviating the expression of MMP-2 and MMP-9. Dexamethasone 119-122 matrix metallopeptidase 2 Rattus norvegicus 183-188 24722316-10 2014 Therefore, MMP-2 and MMP-9 might represent novel pharmacological targets for the treatment of H2S and other hazard gases induced ALI. Hydrogen Sulfide 94-97 matrix metallopeptidase 2 Rattus norvegicus 11-16 24440777-9 2014 Surgery induced occludin protein expression decreases and MMP-2,9 proteins increase and these influences can be enhanced by high concentration of sevoflurane inhalation. Sevoflurane 146-157 matrix metallopeptidase 2 Rattus norvegicus 58-63 24606818-14 2014 Treatment with a combination of minocycline and aspirin decreased percentage infarct volume, arrhythmias, mortality and collagen level when compared with vehicle-treated diabetic controls and showed reduced levels of MMP-2 and MMP-9. Minocycline 32-43 matrix metallopeptidase 2 Rattus norvegicus 217-222 24606818-14 2014 Treatment with a combination of minocycline and aspirin decreased percentage infarct volume, arrhythmias, mortality and collagen level when compared with vehicle-treated diabetic controls and showed reduced levels of MMP-2 and MMP-9. Aspirin 48-55 matrix metallopeptidase 2 Rattus norvegicus 217-222 24595240-5 2014 The AChE inhibitor physostigmine ameliorated the MK801-induced reduction of BDNF mRNA and protein levels, reduced MK801-triggered MMP-2 activity and prevented decreased TIMP-2 mRNA expression. Physostigmine 19-32 matrix metallopeptidase 2 Rattus norvegicus 130-135 24595240-5 2014 The AChE inhibitor physostigmine ameliorated the MK801-induced reduction of BDNF mRNA and protein levels, reduced MK801-triggered MMP-2 activity and prevented decreased TIMP-2 mRNA expression. Dizocilpine Maleate 49-54 matrix metallopeptidase 2 Rattus norvegicus 130-135 24595240-5 2014 The AChE inhibitor physostigmine ameliorated the MK801-induced reduction of BDNF mRNA and protein levels, reduced MK801-triggered MMP-2 activity and prevented decreased TIMP-2 mRNA expression. Dizocilpine Maleate 114-119 matrix metallopeptidase 2 Rattus norvegicus 130-135 24418386-4 2014 Our aim was to determine whether sucrose induced IR modifies MMP-2 and MMP-9 behavior in expanded visceral adipose tissue and the contribution of this tissue to circulating activity of these gelatinases. Sucrose 33-40 matrix metallopeptidase 2 Rattus norvegicus 61-66 25187675-9 2014 In skeletal muscles, low-intensity exercise training, but not high intensity exercise, reduced the levels of COX-2, iNOS, and MMP-2, which were otherwise markedly elevated in the presence of STZ. Streptozocin 191-194 matrix metallopeptidase 2 Rattus norvegicus 126-131 24322055-6 2014 CFs harvested from the hearts of noninjected DS rats demonstrated a significantly increased messenger RNA (mRNA) expression of matrix metalloproteinase (MMP)-2, MMP-9, and both collagen I and III. ds 45-47 matrix metallopeptidase 2 Rattus norvegicus 127-159 24242015-5 2014 The present study was formulated to assess the efficacy of T11TS in the modulations of MMP-2 and -9 and their endogenous inhibitors (TIMP-1 and TIMP-2) as well as modulations of integrin alphav and TGF-beta1 in glioma-induced rats and also on the phenotypic markers of endothelial cells (CD31 and CD34). t11ts 59-64 matrix metallopeptidase 2 Rattus norvegicus 87-99 24242015-7 2014 It was observed that T11TS administration significantly downregulates the expression of matrix metalloproteinase-2 and -9 along with its ligand integrin alphav and upregulates TIMP-1 and TIMP-2. t11ts 21-26 matrix metallopeptidase 2 Rattus norvegicus 88-121 24281858-6 2014 Colon of the rats treated with DMH exhibited higher glycoconjugates and proliferation index such as elevated expressions of argyrophilic nucleolar organizing regions (AgNORs), proliferating cell nuclear antigen (PCNA), cyclin D1, matrix metalloproteins (MMP-2 and -9), and mast cells. 1,2-Dimethylhydrazine 31-34 matrix metallopeptidase 2 Rattus norvegicus 254-266 24309158-9 2014 Further, GA treatment effectively prevented the AGEs mediated up-regulation of pro-fibrotic genes and ECM proteins such as TNF-alpha, TGF-beta, MMP-2 and -9 expression. Gallic Acid 9-11 matrix metallopeptidase 2 Rattus norvegicus 144-156 24440697-5 2014 Our results indicate that polyphenols bind to monomeric tropoelastin and enhance coacervation, aid in crosslinking of elastin by increasing lysyl oxidase (LOX) synthesis, and by blocking MMP-2 activity. Polyphenols 26-37 matrix metallopeptidase 2 Rattus norvegicus 187-192 24334444-17 2014 Systemic estradiol administration further increased the mean (SD) MMP-2 mRNA (0.83 [0.10]) and protein (0.69 [0.12]) expression (P < 0.05), while systemic testosterone administration decreased the mean (SD) MMP-2 mRNA (0.12 [0.04]) and protein (0.27 [0.07]) expression (P < 0.01). Estradiol 9-18 matrix metallopeptidase 2 Rattus norvegicus 66-71 24334444-17 2014 Systemic estradiol administration further increased the mean (SD) MMP-2 mRNA (0.83 [0.10]) and protein (0.69 [0.12]) expression (P < 0.05), while systemic testosterone administration decreased the mean (SD) MMP-2 mRNA (0.12 [0.04]) and protein (0.27 [0.07]) expression (P < 0.01). Estradiol 9-18 matrix metallopeptidase 2 Rattus norvegicus 210-215 24721310-12 2014 CONCLUSIONS: Hydrogen which may contribute to reduce rCklf1 expression prevents infiltration of inflammation and expression of MMP2 thus decreasing destruction and degradation of elastic fibers, therefore ameliorates development of AAA. Hydrogen 13-21 matrix metallopeptidase 2 Rattus norvegicus 127-131 24380772-0 2014 Moderate inhibition of myocardial matrix metalloproteinase-2 by ilomastat is cardioprotective. ilomastat 64-73 matrix metallopeptidase 2 Rattus norvegicus 34-60 24380772-2 2014 Therefore, here we investigated if the MMP inhibitor ilomastat administered either before ischemia or before reperfusion is able to reduce infarct size via inhibition of MMP-2, the most abundant MMP in the rat heart. ilomastat 53-62 matrix metallopeptidase 2 Rattus norvegicus 170-175 24380772-10 2014 The cytoprotective concentration of ilomastat (500nM) showed a moderate (approximately 25%) inhibition of intracellular MMP-2 in ischemic/reperfused cardiomyocytes. ilomastat 36-45 matrix metallopeptidase 2 Rattus norvegicus 120-125 24291173-10 2014 Furthermore, olmesartan down-regulated matrix metalloproteinase-2 and angiotensin II type I receptor expression in the kidney. olmesartan 13-23 matrix metallopeptidase 2 Rattus norvegicus 39-65 24337018-9 2014 PCPA markedly attenuated MCT-induced pulmonary vascular remodeling and lung inflammation, inhibited the expression of Tph-1 and SERT and suppressed the expression of MMP-2/-9, TIMP-1/-2, interleukin-1beta (IL-1beta), tumor necrosis factor-alpha (TNF-alpha) and intercellular adhesion molecule-1 (ICAM-1). Fenclonine 0-4 matrix metallopeptidase 2 Rattus norvegicus 166-174 24337018-10 2014 These findings suggest that the amelioration of MCT-induced pulmonary vascular remodeling and lung inflammation by PCPA is associated with the downregulation of Tph-1, SERT, MMP/TIMP and inflammatory cytokine expression in rats. Fenclonine 115-119 matrix metallopeptidase 2 Rattus norvegicus 174-177 25136580-8 2014 ANP and BNP increased and that of MMP-2 increased in isoproterenol twice treated group compared to control group, without CTGF. Isoproterenol 53-66 matrix metallopeptidase 2 Rattus norvegicus 34-39 25358632-8 2014 Treatment with MGO significantly augmented the proliferation of mesenchymal-like mesothelial cells, accumulation of AGE, de novo expression of alphaSMA and RAGE and gene expression of type I collagen, TGF-beta1, Snail and MMP-2, whereas both MGO and RF alone had, at most, marginal effects on the changes in these biological parameters. Pyruvaldehyde 15-18 matrix metallopeptidase 2 Rattus norvegicus 222-227 25605162-4 2014 Our results showed that both IV and oral dosages of DOX-MTX NP caused significant decrease in mRNA levels of MMP-2 compared to the untreated group (p<0.003). dox-mtx 52-59 matrix metallopeptidase 2 Rattus norvegicus 109-114 25605162-6 2014 Our results indicated that IV dosage of MTX-DOX is more effective than free DOX (12 fold) in inhibiting the activity of MMP-2 in OSCCs (P<0.001). mtx-dox 40-47 matrix metallopeptidase 2 Rattus norvegicus 120-125 25605162-6 2014 Our results indicated that IV dosage of MTX-DOX is more effective than free DOX (12 fold) in inhibiting the activity of MMP-2 in OSCCs (P<0.001). Doxorubicin 44-47 matrix metallopeptidase 2 Rattus norvegicus 120-125 25605162-7 2014 Furthermore, MMP-2 mRNA expression in the DOX-MTX treated group showed a significant relation with histopathological changes (P=0.011). dox-mtx 42-49 matrix metallopeptidase 2 Rattus norvegicus 13-18 24169002-3 2014 Therefore, we conjugated a thiolated MMP2 antibody to the PEG chains on the CMB surface, which was verified by fluorescent microscopy. Polyethylene Glycols 58-61 matrix metallopeptidase 2 Rattus norvegicus 37-41 24169002-3 2014 Therefore, we conjugated a thiolated MMP2 antibody to the PEG chains on the CMB surface, which was verified by fluorescent microscopy. cmb 76-79 matrix metallopeptidase 2 Rattus norvegicus 37-41 24795889-9 2014 Furthermore, naringenin and its beta-CD complex significantly inhibited the mRNA and protein expression of VEGF, COX-2, PI3K, p38MAPK, MMP-2, and MMP-9 in retina and choroid tissues. naringenin 13-23 matrix metallopeptidase 2 Rattus norvegicus 135-140 24795889-9 2014 Furthermore, naringenin and its beta-CD complex significantly inhibited the mRNA and protein expression of VEGF, COX-2, PI3K, p38MAPK, MMP-2, and MMP-9 in retina and choroid tissues. betadex 32-39 matrix metallopeptidase 2 Rattus norvegicus 135-140 23481598-8 2014 MMP-2 activity of SHR RAECs was increased significantly and doxycycline (50 muM) effectively reduced the level of MMP-2 and hyper-permeability in SHR RAECs. Doxycycline 60-71 matrix metallopeptidase 2 Rattus norvegicus 114-119 23481598-10 2014 Doxycycline (50 muM) attenuated hyper-permeability via decreased MMP-2 by protecting VEGFR2, VE-cadherin, Beta-catenin from cleavage and inhibited the reduction of mitochondrial transmembrane potential (MTP), thus prevented mitochondria-mediated apoptotic signaling and capillary rarefaction in the SHR. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 65-70 23433350-8 2014 In first and the second moments, latent MMP-2 was significantly elevated in the eyes treated with NAC and CS (P < 0.001). Acetylcysteine 98-101 matrix metallopeptidase 2 Rattus norvegicus 40-45 25036062-10 2014 The MMP2 enzyme activity was evaluated in different concentrations of genistein. Genistein 70-79 matrix metallopeptidase 2 Rattus norvegicus 4-8 24649712-9 2014 In the CaCl2 group, the MMP-2 and MMP-9 levels were significantly higher than those in the NaCl group (p < 0.05). Calcium Chloride 7-12 matrix metallopeptidase 2 Rattus norvegicus 24-29 24114660-10 2014 SHR showed increased aortic MMP-2 levels which co-localized with higher aortic MMP activity and ROS levels, and all those biochemical alterations associated with hypertension were blunted by treatment with doxycycline. Reactive Oxygen Species 96-99 matrix metallopeptidase 2 Rattus norvegicus 28-33 24114660-10 2014 SHR showed increased aortic MMP-2 levels which co-localized with higher aortic MMP activity and ROS levels, and all those biochemical alterations associated with hypertension were blunted by treatment with doxycycline. Doxycycline 206-217 matrix metallopeptidase 2 Rattus norvegicus 28-33 23433350-8 2014 In first and the second moments, latent MMP-2 was significantly elevated in the eyes treated with NAC and CS (P < 0.001). Chondroitin Sulfates 106-108 matrix metallopeptidase 2 Rattus norvegicus 40-45 23433350-9 2014 Active MMP-2 did not change significantly among treatment groups in the first moment (P > 0.05); significantly higher activity was observed in the second moment in the eyes treated with CS (P <0.001). Chondroitin Sulfates 189-191 matrix metallopeptidase 2 Rattus norvegicus 7-12 23433350-13 2014 Significant higher levels of active form of MMP-2 in 3% chondroitin sulfate-treated group may indicate that the agent acts as substrate for such enzyme. Chondroitin Sulfates 56-75 matrix metallopeptidase 2 Rattus norvegicus 44-49 23806385-0 2013 Nebivolol attenuates prooxidant and profibrotic mechanisms involving TGF-beta and MMPs, and decreases vascular remodeling in renovascular hypertension. Nebivolol 0-9 matrix metallopeptidase 2 Rattus norvegicus 82-86 24436993-0 2013 Effects of hyperbaric oxygen on MMP-2 and MMP-9 expression and spinal cord edema after spinal cord injury. Oxygen 22-28 matrix metallopeptidase 2 Rattus norvegicus 32-37 24436993-1 2013 AIMS: To evaluate the effects of hyperbaric oxygen (HBO) therapy on MMP-2 and MMP-9 expression and spinal cord edema after acute spinal cord injury (SCI). Oxygen 44-50 matrix metallopeptidase 2 Rattus norvegicus 68-73 24436993-10 2013 MMP-2 (P < 0.05) and MMP-9 (P < 0.01) levels were positively correlated with spinal cord water content. Water 95-100 matrix metallopeptidase 2 Rattus norvegicus 0-5 24741986-6 2014 CONCLUSION: Protective effect of IPIC on myocardium may be due to reduce free radical, lower expression of MMP-2 and protect myocardial interstitium. ipic 33-37 matrix metallopeptidase 2 Rattus norvegicus 107-112 23806385-13 2013 Moreover, nebivolol, but not metoprolol, attenuated hypertension-induced increases in aortic NAD(P)H oxidase activity, superoxide production, TBARS concentrations, nitrotyrosine levels, TGF-beta upregulation, and MMP-2 and -9 expression/activity. Nebivolol 10-19 matrix metallopeptidase 2 Rattus norvegicus 213-225 23806385-15 2013 These results show for the first time that nebivolol, but not metoprolol, attenuates prooxidant and profibrotic mechanisms involving TGF-beta and MMP-2 and MMP-9, which promote vascular remodeling in hypertension. Nebivolol 43-52 matrix metallopeptidase 2 Rattus norvegicus 146-151 23949118-8 2013 Tempol treatment significantly corrected the changes in the cardiac extracellular matrix, TGF-beta, ROS or serum LDH, CK-MB levels, and normalized MMP-2 activity along with preservation of cardiac tissues integrity of diabetic rats against damaging responses. tempol 0-6 matrix metallopeptidase 2 Rattus norvegicus 147-152 23872719-4 2013 Our study demonstrated that atorvastatin attenuates neuropathic pain through inhibition of cytokines, MMP-2, and NGF in sciatic nerve and spinal cord suggesting that atorvastatin could be an additional therapeutic strategy in management of neuropathic pain. Atorvastatin 28-40 matrix metallopeptidase 2 Rattus norvegicus 102-107 24118063-0 2013 Effect of telmisartan on levels of IL-1, TNF-alpha, down-regulated COX-2, MMP-2, MMP-9 and RANKL/RANK in an experimental periodontitis model. Telmisartan 10-21 matrix metallopeptidase 2 Rattus norvegicus 74-79 24369253-3 2013 RESULTS: Compared with the cells in normal glucose, the cells cultured in the presence of high glucose for 24 and 48 h showed significantly increased TGFbeta 1 and FN protein expression and lowered MMP-2 protein expression (P<0.01). Glucose 95-102 matrix metallopeptidase 2 Rattus norvegicus 198-203 24369253-4 2013 Compared with the cells cultured in high glucose, BPS exposure at the concentration of 1, 2, and 5 micromol/L for 24 and 48 h significantly lowered TGFbeta 1 protein expression (P<0.01), and at 2 and 5 micromol/L, BPS significantly decreased FN protein expression and increased MMP-2 protein expression in high glucose-induced cells (P<0.05). beraprost 50-53 matrix metallopeptidase 2 Rattus norvegicus 281-286 23937199-10 2013 In conclusion, we suggest that nitric oxide (NO) contributes to OA-induced MMP activation, BBB disruption and the development of transient brain edema. Nitric Oxide 31-43 matrix metallopeptidase 2 Rattus norvegicus 75-78 23564480-7 2013 The decreased expression of Bcl-2, MMP-2 and MMP-9 alone with cytochrome c release from mitochondria into the cytosol was also observed in the TMZ/PYR combination group. Temozolomide 143-146 matrix metallopeptidase 2 Rattus norvegicus 35-40 23990224-8 2013 The expression of AQP-1, AQP-4, MMP-2, and MMP-9 at 24 h and of HIF-1alpha at 8 h following ischemia/reperfusion was significantly suppressed in the propofol post-treatment group (P < 0.05). Propofol 149-157 matrix metallopeptidase 2 Rattus norvegicus 32-37 23990224-9 2013 Propofol post-treatment attenuated cerebral edema after transient cerebral ischemia, in association with reduced expression of AQP-1, AQP-4, MMP-2, and MMP-9. Propofol 0-8 matrix metallopeptidase 2 Rattus norvegicus 141-146 23990224-10 2013 The decreased expression of AQPs and MMPs after propofol post-treatment might result from suppression of HIF-1alpha expression. Propofol 48-56 matrix metallopeptidase 2 Rattus norvegicus 37-41 23564480-7 2013 The decreased expression of Bcl-2, MMP-2 and MMP-9 alone with cytochrome c release from mitochondria into the cytosol was also observed in the TMZ/PYR combination group. Pyrimethamine 147-150 matrix metallopeptidase 2 Rattus norvegicus 35-40 23783073-8 2013 These results suggest that relaxin crosses the BBB and activates MMP-2 in brain cortex, which may interact with PAs to increase distensibility. Aminosalicylic Acid 112-115 matrix metallopeptidase 2 Rattus norvegicus 65-70 24130702-8 2013 Furthermore, MMP-2, MMP-9, RANKL/RANK, and COX-2 were all downregulated by Atorvastatin treatment, while OPG expression was increased. Atorvastatin 75-87 matrix metallopeptidase 2 Rattus norvegicus 13-18 23900029-9 2013 The levels of MMP-2 and MMP-9 were both significantly increased after the ulceration, but these responses were suppressed by the repeated indomethacin treatment. Indomethacin 138-150 matrix metallopeptidase 2 Rattus norvegicus 14-19 23900029-10 2013 The healing of these ulcers was significantly delayed by the repeated administration of MMP inhibitors such as ARP-101 and SB-3CT. SB 3CT compound 123-129 matrix metallopeptidase 2 Rattus norvegicus 88-91 23900029-11 2013 SIGNIFICANCE: The results confirm the importance of the balance between pro-angiogenic and anti-angiogenic activities in the healing of indomethacin-induced small intestinal damage and further suggest that the increased expression of MMP-2 and MMP-9 is another important factor for ulcer healing in the small intestine. Indomethacin 136-148 matrix metallopeptidase 2 Rattus norvegicus 234-239 23986225-8 2013 Wound tissue from NTX-treated T1D rats had comparable numbers of MMP-2+ fibroblasts to control specimens, as well as accelerated maturation of granulation tissue. Naltrexone 18-21 matrix metallopeptidase 2 Rattus norvegicus 65-70 23582053-3 2013 In the present study, we determined whether administering differing concentrations of EtOH alter the expressions of BBB integral proteins, including aquaporins-4 and -9 (AQP-4, AQP-9), matrix metallopeptidases-2 and -9 (MMP-2, MMP-9), zonula occludens-1 (ZO-1), and basal lamina (laminin). Ethanol 86-90 matrix metallopeptidase 2 Rattus norvegicus 185-218 24142718-5 2013 When LDL-induced cells were treated with curcumin in the concentration of 12.5 or 25.0 mumol/L, LDL-induced proliferation of mesangial cells was suppressed, the expression of MMP-2 mRNA and protein increased, the expression of COX-2 mRNA and protein downregulated, the production of ROS inhibited and p38 MAPK inactivated (P<0.05). Curcumin 41-49 matrix metallopeptidase 2 Rattus norvegicus 175-180 24142718-6 2013 In conclusion, curcumin can inhibit the LDL-induced proliferation of mesangial cells and up-regulate the expression of MMP-2, which may be related with the inhibitory effect of curcumin on COX-2 expression, ROS production and p38 MAPK. Curcumin 15-23 matrix metallopeptidase 2 Rattus norvegicus 119-124 24142718-6 2013 In conclusion, curcumin can inhibit the LDL-induced proliferation of mesangial cells and up-regulate the expression of MMP-2, which may be related with the inhibitory effect of curcumin on COX-2 expression, ROS production and p38 MAPK. Curcumin 177-185 matrix metallopeptidase 2 Rattus norvegicus 119-124 24142718-6 2013 In conclusion, curcumin can inhibit the LDL-induced proliferation of mesangial cells and up-regulate the expression of MMP-2, which may be related with the inhibitory effect of curcumin on COX-2 expression, ROS production and p38 MAPK. Reactive Oxygen Species 207-210 matrix metallopeptidase 2 Rattus norvegicus 119-124 23775504-0 2013 Olmesartan decreases IL-1beta and TNF-alpha levels; downregulates MMP-2, MMP-9, COX-2, and RANKL; and upregulates OPG in experimental periodontitis. olmesartan 0-10 matrix metallopeptidase 2 Rattus norvegicus 66-71 23775504-7 2013 Furthermore, treatment with 6 mg/kg olmesartan led to downregulation of the expression of COX-2, MMP-2, MMP-9, RANKL, and RANK and to upregulation of the expression of OPG. olmesartan 36-46 matrix metallopeptidase 2 Rattus norvegicus 97-102 23775504-8 2013 These findings suggest that 6 mg/kg olmesartan reduces the inflammatory process and bone loss by downregulating MMPs and RANKL in osteoblasts and by upregulating OPG. olmesartan 36-46 matrix metallopeptidase 2 Rattus norvegicus 112-116 23582053-3 2013 In the present study, we determined whether administering differing concentrations of EtOH alter the expressions of BBB integral proteins, including aquaporins-4 and -9 (AQP-4, AQP-9), matrix metallopeptidases-2 and -9 (MMP-2, MMP-9), zonula occludens-1 (ZO-1), and basal lamina (laminin). Ethanol 86-90 matrix metallopeptidase 2 Rattus norvegicus 220-225 23582053-7 2013 Compared to control, OGD/R without EtOH significantly increased AQP-4, AQP-9, MMP-2, and MMP-9 levels, while decreasing ZO-1 and laminin levels. Ethanol 35-39 matrix metallopeptidase 2 Rattus norvegicus 78-83 23582053-8 2013 All EtOH concentration treatments (groups 3 through 5) significantly reduced the expressions of AQP-4, AQP-9, MMP-2, and MMP-9, compared to the OGD/R, non-alcohol treated slices. Ethanol 4-8 matrix metallopeptidase 2 Rattus norvegicus 110-115 23582053-11 2013 In conclusion, at an optimal dose of 30 mM, EtOH improves the expressions of MMP-2, MMP-9, AQP-4, AQP-9, ZO-1, and basal laminin, previously altered by OGD/R. Ethanol 44-48 matrix metallopeptidase 2 Rattus norvegicus 77-82 24086601-0 2013 Pipoxolan ameliorates cerebral ischemia via inhibition of neuronal apoptosis and intimal hyperplasia through attenuation of VSMC migration and modulation of matrix metalloproteinase-2/9 and Ras/MEK/ERK signaling pathways. pipoxolan 0-9 matrix metallopeptidase 2 Rattus norvegicus 157-185 24086601-9 2013 Moreover, PIPO decreased levels of matrix metalloproteinases -2 and -9 in PDGF-BB-stimulated A7r5 cells. pipoxolan 10-14 matrix metallopeptidase 2 Rattus norvegicus 35-70 24009745-8 2013 Markers of leukocyte invasiveness like matrix metalloprotease (MMP)-2, or common pro-inflammatory molecules like the CXCR4 receptor or the chemokine (C-C motif) ligand (CCL)-2 were downregulated by prednisolone. Prednisolone 198-210 matrix metallopeptidase 2 Rattus norvegicus 39-69 23856290-9 2013 Prolonged treatment of uterus or aorta of virgin rats with 17beta-estradiol and progesterone increased the amount of EMMPRIN, MMP-2 and -9, and the sex hormone-induced increases in MMPs were prevented by EMMPRIN neutralizing antibody. Estradiol 59-75 matrix metallopeptidase 2 Rattus norvegicus 126-138 23856290-9 2013 Prolonged treatment of uterus or aorta of virgin rats with 17beta-estradiol and progesterone increased the amount of EMMPRIN, MMP-2 and -9, and the sex hormone-induced increases in MMPs were prevented by EMMPRIN neutralizing antibody. Progesterone 80-92 matrix metallopeptidase 2 Rattus norvegicus 126-138 23891690-4 2013 Time course of activation of cytosolic MMP-9 and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage. Glucose 123-130 matrix metallopeptidase 2 Rattus norvegicus 49-54 23891690-7 2013 Increased mitochondrial MMPs dysfunction them and begin to damage their DNA, which initiates a vicious cycle of reactive oxygen species. Reactive Oxygen Species 112-135 matrix metallopeptidase 2 Rattus norvegicus 24-28 23830364-3 2013 Doxycycline, a nonspecific inhibitor of MMPs, has been shown to beneficially reduce MMP levels in both cancer and aneurysm models. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 40-44 23830364-9 2013 RESULTS: There were no differences in control and experimental groups 1 and 2 wk following hernia repair; 4 wk following hernia repair, doxycycline treated animals demonstrated reduced serum MMP-2 and MMP-9 levels, reduced tissue levels of MMP-2, MMP-3, and MMP-9, and increased collagen 1 to 3 ratios. Doxycycline 136-147 matrix metallopeptidase 2 Rattus norvegicus 191-196 23830364-9 2013 RESULTS: There were no differences in control and experimental groups 1 and 2 wk following hernia repair; 4 wk following hernia repair, doxycycline treated animals demonstrated reduced serum MMP-2 and MMP-9 levels, reduced tissue levels of MMP-2, MMP-3, and MMP-9, and increased collagen 1 to 3 ratios. Doxycycline 136-147 matrix metallopeptidase 2 Rattus norvegicus 240-245 23343143-7 2013 Increased MMP-2 levels in RLX-treated rats demonstrated that the hormone was administered and active in this model. Relaxin 26-29 matrix metallopeptidase 2 Rattus norvegicus 10-15 23665313-2 2013 Reactive oxygen species activate MMP-2 at both transcriptional and post-translational levels, thus MMP-2 activation is considered an early event in oxidative stress injury. Reactive Oxygen Species 0-23 matrix metallopeptidase 2 Rattus norvegicus 33-38 23665313-4 2013 We carefully investigated the mode of cell death in neonatal rat cardiomyocytes induced by different concentrations (50-500 muM) of hydrogen peroxide at various time intervals after exposure and determined whether MMP-2 is implicated in hydrogen peroxide-induced cardiomyocyte death. Hydrogen Peroxide 237-254 matrix metallopeptidase 2 Rattus norvegicus 214-219 23665313-5 2013 Treating cardiomyocytes with hydrogen peroxide led to elevated MMP-2 level/activity with maximal effects seen at 200 muM. Hydrogen Peroxide 29-46 matrix metallopeptidase 2 Rattus norvegicus 63-68 23665313-9 2013 In conclusion hydrogen peroxide increases MMP-2 level/activity in cardiomyocytes and induces necrotic cell death, however, the later effect is MMP-2 independent. Hydrogen Peroxide 14-31 matrix metallopeptidase 2 Rattus norvegicus 42-47 23665313-9 2013 In conclusion hydrogen peroxide increases MMP-2 level/activity in cardiomyocytes and induces necrotic cell death, however, the later effect is MMP-2 independent. Hydrogen Peroxide 14-31 matrix metallopeptidase 2 Rattus norvegicus 143-148 24159376-10 2013 Inhibition of MMPs by GM6001 resulted in a significant improvement in all the parameters including renal function. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 22-28 matrix metallopeptidase 2 Rattus norvegicus 14-18 23172681-4 2013 In this study, we examined the molecular mechanisms by which naringenin inhibited NDEA-induced hepatocellular carcinoma in rats by analysing the expression patterns of proliferating cell nuclear antigen, Bcl-2, NF-kappaB, VEGF and MMP-2/9. naringenin 61-71 matrix metallopeptidase 2 Rattus norvegicus 231-238 23172681-8 2013 Downregulation of NF-kappaB, VEGF and MMPs by naringenin seen in the present study were correlated with the inhibition of liver tumour induced by NDEA. naringenin 46-56 matrix metallopeptidase 2 Rattus norvegicus 38-42 23897788-0 2013 Effects of rosuvastatin on the production and activation of matrix metalloproteinase-2 and migration of cultured rat vascular smooth muscle cells induced by homocysteine. Rosuvastatin Calcium 11-23 matrix metallopeptidase 2 Rattus norvegicus 60-86 23897788-0 2013 Effects of rosuvastatin on the production and activation of matrix metalloproteinase-2 and migration of cultured rat vascular smooth muscle cells induced by homocysteine. Homocysteine 157-169 matrix metallopeptidase 2 Rattus norvegicus 60-86 23897788-1 2013 OBJECTIVE: To test the influence of homocysteine on the production and activation of matrix metalloproteinase-2 (MMP-2) and tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and on cell migration of cultured rat vascular smooth muscle cells (VSMCs). Homocysteine 36-48 matrix metallopeptidase 2 Rattus norvegicus 85-111 23897788-1 2013 OBJECTIVE: To test the influence of homocysteine on the production and activation of matrix metalloproteinase-2 (MMP-2) and tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and on cell migration of cultured rat vascular smooth muscle cells (VSMCs). Homocysteine 36-48 matrix metallopeptidase 2 Rattus norvegicus 113-118 23897788-2 2013 Also, to explore whether rosuvastatin can alter the abnormal secretion and activation of MMP-2 and TIMP-2 and migration of VSMCs induced by homocysteine. Rosuvastatin Calcium 25-37 matrix metallopeptidase 2 Rattus norvegicus 89-94 23897788-4 2013 Western blotting and gelatin zymography were used to investigate the expressions and activities of MMP-2 and TIMP-2 in VSMCs in culture medium when induced with homocysteine for 24, 48, and 72 h. Transwell chambers were employed to test the migratory ability of VSMCs when incubated with homocysteine for 48 h. Different concentrations of rosuvastatin (10(-9)-10(-5) mol/L) were added when VSMCs were induced with 1000 mumol/L homocysteine. Homocysteine 161-173 matrix metallopeptidase 2 Rattus norvegicus 99-104 23897788-4 2013 Western blotting and gelatin zymography were used to investigate the expressions and activities of MMP-2 and TIMP-2 in VSMCs in culture medium when induced with homocysteine for 24, 48, and 72 h. Transwell chambers were employed to test the migratory ability of VSMCs when incubated with homocysteine for 48 h. Different concentrations of rosuvastatin (10(-9)-10(-5) mol/L) were added when VSMCs were induced with 1000 mumol/L homocysteine. vsmcs 119-124 matrix metallopeptidase 2 Rattus norvegicus 99-104 22483258-2 2013 We hypothesized that the AT1R antagonist losartan or the renin inhibitor aliskiren, given at doses allowing similar antihypertensive effects, could prevent in vivo vascular MMPs upregulation and remodeling, and collagen/elastin deposition found in 2K1C hypertension by preventing the activation of extracellular signal-regulated kinase 1/2 (ERK 1/2) and transforming growth factor-beta1 (TGF-beta1). Losartan 41-49 matrix metallopeptidase 2 Rattus norvegicus 173-177 22483258-2 2013 We hypothesized that the AT1R antagonist losartan or the renin inhibitor aliskiren, given at doses allowing similar antihypertensive effects, could prevent in vivo vascular MMPs upregulation and remodeling, and collagen/elastin deposition found in 2K1C hypertension by preventing the activation of extracellular signal-regulated kinase 1/2 (ERK 1/2) and transforming growth factor-beta1 (TGF-beta1). aliskiren 73-82 matrix metallopeptidase 2 Rattus norvegicus 173-177 22483258-7 2013 Losartan alone or combined with aliskiren, but not aliskiren alone, abolished 2K1C-induced aortic hypertrophy and hyperplasia, and prevented the increases in aortic collagen/elastin content, MMP-2 levels, gelatinolytic activity, and expression of phospho-ERK 1/2 and TGF-beta1. Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 191-196 22483258-7 2013 Losartan alone or combined with aliskiren, but not aliskiren alone, abolished 2K1C-induced aortic hypertrophy and hyperplasia, and prevented the increases in aortic collagen/elastin content, MMP-2 levels, gelatinolytic activity, and expression of phospho-ERK 1/2 and TGF-beta1. aliskiren 32-41 matrix metallopeptidase 2 Rattus norvegicus 191-196 22483258-9 2013 CONCLUSIONS: These findings show that although losartan and aliskiren exerted similar antihypertensive effects, only losartan prevented the activation of vascular profibrotic mechanisms and MMP upregulation associated with vascular remodeling in 2K1C hypertension. Losartan 117-125 matrix metallopeptidase 2 Rattus norvegicus 190-193 23646930-6 2013 The inhibition of MMPs activity achieved by either doxycycline (a non-competitive inhibitor of collagenases), TIMP-1 (tissue inhibitor of metalloproteinases 1) or neutralising anti-MMP-9 antibody affects nuclear localisation of this gelatinase, and impacts at myoblasts proliferation. Doxycycline 51-62 matrix metallopeptidase 2 Rattus norvegicus 18-22 23897788-6 2013 However, when incubated with 5000 mumol/L homocysteine, the expression of MMP-2 was up-regulated, but its activity was down-regulated. Homocysteine 42-54 matrix metallopeptidase 2 Rattus norvegicus 74-79 23897788-7 2013 Increased homocysteine-induced production and activation of MMP-2 were reduced by rosuvastatin in a dose-dependent manner whereas secretion of TIMP-2 was not significantly altered by rosuvastatin. Homocysteine 10-22 matrix metallopeptidase 2 Rattus norvegicus 60-65 23897788-7 2013 Increased homocysteine-induced production and activation of MMP-2 were reduced by rosuvastatin in a dose-dependent manner whereas secretion of TIMP-2 was not significantly altered by rosuvastatin. Rosuvastatin Calcium 82-94 matrix metallopeptidase 2 Rattus norvegicus 60-65 23897788-9 2013 CONCLUSIONS: Homocysteine (50-1000 mumol/L) significantly increased the production and activation of MMP-2, the expression of TIMP-2, and the migration of VSMCs in a dose-dependent manner. Homocysteine 13-25 matrix metallopeptidase 2 Rattus norvegicus 101-106 23897788-10 2013 Additional extracellular rosuvastatin can decrease the excessive expression and activation of MMP-2 and abnormal migration of VSMCs induced by homocysteine. Rosuvastatin Calcium 25-37 matrix metallopeptidase 2 Rattus norvegicus 94-99 24159376-12 2013 Administration of GM6001 reduced the activity of MMPs and increased the levels of TIMP-1, -2 and -3. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 18-24 matrix metallopeptidase 2 Rattus norvegicus 49-53 23889761-5 2013 RESULTS: Behavioral tests performed on male Sprague-Dawley rats at 1, 3, 7 and 14 days after intra-plantar MMP-2/9 inhibitor administration demonstrated that acute and chronic injections of the MMP-2/9 inhibitor induced sensitization, in a dose dependent manner, to mechanical, hot and cold stimuli as measured by von Frey filaments, Hargreaves and acetone tests, respectively. Acetone 349-356 matrix metallopeptidase 2 Rattus norvegicus 194-201 23796971-4 2013 Ccl2, Gfap, and Mmp 9 mRNA levels, and MMP-2 and -9 enzymatic activities were increased after TBI regardless of brain DHA level. Thioacetazone 94-97 matrix metallopeptidase 2 Rattus norvegicus 39-51 23536977-10 2013 Elevation of HIF-1alpha, upregulation of CXCR4/CCR2 and higher activity of MMP-2/MMP-9 in DFO-treated MSCs were reversed by 2-methoxyestradiol (2-ME; 5 mumol), a HIF-1alpha inhibitor. Deferoxamine 90-93 matrix metallopeptidase 2 Rattus norvegicus 75-80 23843954-9 2013 Immunohistochemical analysis demonstrated reduced expression of MMP-2, MMP-9, RANK, RANKL, COX-2, and OPG in rats treated with 10 mg/kg Carvedilol. Carvedilol 136-146 matrix metallopeptidase 2 Rattus norvegicus 64-69 23843954-0 2013 Carvedilol decrease IL-1beta and TNF-alpha, inhibits MMP-2, MMP-9, COX-2, and RANKL expression, and up-regulates OPG in a rat model of periodontitis. Carvedilol 0-10 matrix metallopeptidase 2 Rattus norvegicus 53-58 23536977-10 2013 Elevation of HIF-1alpha, upregulation of CXCR4/CCR2 and higher activity of MMP-2/MMP-9 in DFO-treated MSCs were reversed by 2-methoxyestradiol (2-ME; 5 mumol), a HIF-1alpha inhibitor. 2-Methoxyestradiol 124-142 matrix metallopeptidase 2 Rattus norvegicus 75-80 23536977-10 2013 Elevation of HIF-1alpha, upregulation of CXCR4/CCR2 and higher activity of MMP-2/MMP-9 in DFO-treated MSCs were reversed by 2-methoxyestradiol (2-ME; 5 mumol), a HIF-1alpha inhibitor. 2-Methoxyestradiol 144-148 matrix metallopeptidase 2 Rattus norvegicus 75-80 23805912-8 2013 STZ also reduced renal MMP-2 and MMP-9 protein expression in both kidneys from male and female rats, but additional decreases were only observed in GH-treated diabetic male rats. Streptozocin 0-3 matrix metallopeptidase 2 Rattus norvegicus 23-28 23571276-9 2013 The GM6001, which reduced tissue loss at 3 to 4 weeks, significantly increased new vessel formation with expression of TJPs and MMPs. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 4-10 matrix metallopeptidase 2 Rattus norvegicus 128-132 23606560-4 2013 Here, we determined whether inhibition of matrix metalloproteinases-2 and -9 (MMPs) mediates this minocycline action. Minocycline 98-109 matrix metallopeptidase 2 Rattus norvegicus 78-82 23606560-10 2013 Minocycline administered 2 hr before the lesion significantly inhibited both MMP-9 and MMP-2 levels by ~40%. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 87-92 22981741-5 2013 In the present study, we aimed to investigate the effects of pioglitazone, a synthetic peroxisome proliferator-activated receptor-gamma agonist, on MMPs and oxidative stress in a renal IR injury model in rats. Pioglitazone 61-73 matrix metallopeptidase 2 Rattus norvegicus 148-152 23738715-13 2013 Upregulation of the expression of MMP-2 and MMP-9 could explain the beneficial effects of ginsenoside Rg1 in CTEPH. Ginsenosides 90-101 matrix metallopeptidase 2 Rattus norvegicus 34-39 23738715-13 2013 Upregulation of the expression of MMP-2 and MMP-9 could explain the beneficial effects of ginsenoside Rg1 in CTEPH. cteph 109-114 matrix metallopeptidase 2 Rattus norvegicus 34-39 23411180-7 2013 Fibrotic status and the activation of hepatic stellate cells were improved upon pterostilbene supplementation as evidenced by histopathological examination as well as the expression of alpha-smooth muscle actin (alpha-SMA), transforming growth factor-beta1 (TGF-beta1), and matrix metalloproteinase 2 (MMP2). pterostilbene 80-93 matrix metallopeptidase 2 Rattus norvegicus 274-300 23411180-7 2013 Fibrotic status and the activation of hepatic stellate cells were improved upon pterostilbene supplementation as evidenced by histopathological examination as well as the expression of alpha-smooth muscle actin (alpha-SMA), transforming growth factor-beta1 (TGF-beta1), and matrix metalloproteinase 2 (MMP2). pterostilbene 80-93 matrix metallopeptidase 2 Rattus norvegicus 302-306 23676944-5 2013 RESULTS: Compared with the air and SB203580-treated groups, levels of P38 MAPK and MMP-2 mRNA significantly increased in the hyperoxia group (P<0.01). SB 203580 35-43 matrix metallopeptidase 2 Rattus norvegicus 83-88 23499793-5 2013 Here we show that in vitro administration of rolipram and MP significantly increased neuron survival and promoted neurite outgrowth of neurons on the inhibitory substrate CSPGs by upregulation of MMP-2 expression; in vivo administration of rolipram and MP inhibited CSPG expression and increase CSPG digestion after rat SCI. Rolipram 45-53 matrix metallopeptidase 2 Rattus norvegicus 196-201 23499793-5 2013 Here we show that in vitro administration of rolipram and MP significantly increased neuron survival and promoted neurite outgrowth of neurons on the inhibitory substrate CSPGs by upregulation of MMP-2 expression; in vivo administration of rolipram and MP inhibited CSPG expression and increase CSPG digestion after rat SCI. Rolipram 240-248 matrix metallopeptidase 2 Rattus norvegicus 196-201 23523510-8 2013 Using a pull down assay in rat brain tissue homogenate with gelatine-agarose beads, we showed increased activities for both the pro and mature forms of MMP-2 and MMP-9. Sepharose 69-76 matrix metallopeptidase 2 Rattus norvegicus 152-157 23704825-11 2013 The ZnPP group also showed inhibited TGF-beta1 expression and regulated TIMP-1/MMP-2 expression, as well as obviously attenuated liver fibrosis. zinc protoporphyrin 4-8 matrix metallopeptidase 2 Rattus norvegicus 79-84 22213124-12 2013 5-LOX plays an important role in DMBA-induced inflammation associated carcinogenesis via activation of MMP-2 and VEGF. 6,11-dimethylbenzo(b)naphtho(2,3-d)thiophene 33-37 matrix metallopeptidase 2 Rattus norvegicus 103-108 23415681-12 2013 Hydralazine pretreatment reversed DE-induced TF, tPA, TNF-alpha, and MMP-2 expression but not eNOS, RAGE, and HMGB-1. Hydralazine 0-11 matrix metallopeptidase 2 Rattus norvegicus 69-74 21917342-0 2013 Tempol inhibits TGF-beta and MMPs upregulation and prevents cardiac hypertensive changes. tempol 0-6 matrix metallopeptidase 2 Rattus norvegicus 29-33 23958168-9 2013 CONCLUSIONS: Saturated hydrogen saline prevents the degradation of elastin in vessel wall and ameliorates the formation and development of AAA, which may be associated with its anti-inflammatory effects, thereby reduces the MMP-2 and 9 mRNA and protein expression. hydrogen saline 23-38 matrix metallopeptidase 2 Rattus norvegicus 224-235 25157203-2 2013 The primary candidates involved in controlling this process are a family of endopeptidases called matrix metalloproteinases (MMPs); however, the potential role of MMPs in nicotine addiction-related memories has not been adequately tested. Nicotine 171-179 matrix metallopeptidase 2 Rattus norvegicus 163-167 23417767-3 2013 Treatment of fibroblasts with 25 mM glucose increased the number of cells and the mRNA levels of collagen III, matrix metalloproteinase 2 (MMP2), and MMP9. Glucose 36-43 matrix metallopeptidase 2 Rattus norvegicus 111-137 23417767-3 2013 Treatment of fibroblasts with 25 mM glucose increased the number of cells and the mRNA levels of collagen III, matrix metalloproteinase 2 (MMP2), and MMP9. Glucose 36-43 matrix metallopeptidase 2 Rattus norvegicus 139-143 25157203-3 2013 Present results indicate transient changes in hippocampal MMP-2, -3, and -9 expression following context dependent learning of nicotine-induced conditioned place preference (CPP). Nicotine 127-135 matrix metallopeptidase 2 Rattus norvegicus 58-75 25157203-6 2013 Inhibition of MMPs using a broad spectrum MMP inhibitor (FN439) during nicotine-induced CPP training blocked the acquisition of CPP. 4-aminobenzoyl-glycyl-prolyl-leucyl-alanine hydroxamic acid 57-62 matrix metallopeptidase 2 Rattus norvegicus 14-18 25157203-6 2013 Inhibition of MMPs using a broad spectrum MMP inhibitor (FN439) during nicotine-induced CPP training blocked the acquisition of CPP. Nicotine 71-79 matrix metallopeptidase 2 Rattus norvegicus 14-18 22947212-0 2013 Isoproterenol modulates matrix metalloproteinase-2 (MMP-2) and its tissue inhibitor-2 (TIMP-2) in rat parotid gland. Isoproterenol 0-13 matrix metallopeptidase 2 Rattus norvegicus 24-50 23088810-13 2013 MMP-2 and -9 levels were subsequently increased by each type of hormone therapy compared with placebo, with a significant increase in MMP-9 in response to estrogen with and without progesterone (P < 0.05). Progesterone 181-193 matrix metallopeptidase 2 Rattus norvegicus 0-12 22947212-0 2013 Isoproterenol modulates matrix metalloproteinase-2 (MMP-2) and its tissue inhibitor-2 (TIMP-2) in rat parotid gland. Isoproterenol 0-13 matrix metallopeptidase 2 Rattus norvegicus 52-57 22947212-3 2013 The present study was undertaken to investigate the expression of MMP-2 and the tissue inhibitor metalloproteinase (TIMP)-2 in rat parotid gland following isoproterenol treatment. Isoproterenol 155-168 matrix metallopeptidase 2 Rattus norvegicus 66-71 22947212-6 2013 RESULTS: Our results suggest that isoproterenol modulates expression of MMP-2 and TIMP-2 mRNAs, as well as their protein expression levels in a time dependent-manner. Isoproterenol 34-47 matrix metallopeptidase 2 Rattus norvegicus 72-77 23290263-9 2013 CONCLUSION: Lercanidipine and labedipinedilol-A can exert their anti-inflammatory effects through suppression of NO, ROS and TNF-alpha through down-regulation of iNOS, MMP-2/MMP-9, and HMGB1, with inhibition of signaling transduction of MAPKs, Akt/IkB-alpha and NF-kappaB pathways. lercanidipine 12-25 matrix metallopeptidase 2 Rattus norvegicus 168-173 23756390-9 2013 Combination of reduced dose of indomethacin and GS-HCl significantly reduced the expressions of ICAM-1, VCAM-1, IL-8, IL-1beta, MMP-2, MMP-7, MMP-9, and MMP-11 mRNA as well as NF-kappaB activation better than high dose indomethacin alone. Indomethacin 31-43 matrix metallopeptidase 2 Rattus norvegicus 128-133 23756390-9 2013 Combination of reduced dose of indomethacin and GS-HCl significantly reduced the expressions of ICAM-1, VCAM-1, IL-8, IL-1beta, MMP-2, MMP-7, MMP-9, and MMP-11 mRNA as well as NF-kappaB activation better than high dose indomethacin alone. gs-hcl 48-54 matrix metallopeptidase 2 Rattus norvegicus 128-133 23274713-6 2013 Mechanistically, studies showed that genistein markedly reduced lipid peroxidation, recruited the anti-oxidative defense system, inhibited CYP2El activity, promoted extracellular matrix degradation by modulating the levels of tissue inhibitor of matrix metalloproteinase-1 and matrix metalloproteinase-2, induced HSC apoptosis by down-regulating B-cell lymphoma 2 mRNA, and inhibited the expression of alpha-smooth muscle actin and transforming growth factor beta(1) proteins. Genistein 37-46 matrix metallopeptidase 2 Rattus norvegicus 226-303 23290263-0 2013 Lercanidipine and labedipinedilol--A attenuate lipopolysaccharide/interferon-gamma-induced inflammation in rat vascular smooth muscle cells through inhibition of HMGB1 release and MMP-2, 9 activities. lercanidipine 0-13 matrix metallopeptidase 2 Rattus norvegicus 180-185 23290263-0 2013 Lercanidipine and labedipinedilol--A attenuate lipopolysaccharide/interferon-gamma-induced inflammation in rat vascular smooth muscle cells through inhibition of HMGB1 release and MMP-2, 9 activities. labedipinedilol 18-33 matrix metallopeptidase 2 Rattus norvegicus 180-185 23290263-9 2013 CONCLUSION: Lercanidipine and labedipinedilol-A can exert their anti-inflammatory effects through suppression of NO, ROS and TNF-alpha through down-regulation of iNOS, MMP-2/MMP-9, and HMGB1, with inhibition of signaling transduction of MAPKs, Akt/IkB-alpha and NF-kappaB pathways. labedipinedilol A 30-47 matrix metallopeptidase 2 Rattus norvegicus 168-173 23769575-0 2013 Atorvastatin reduces myocardial fibrosis in a rat model with post-myocardial infarction heart failure by increasing the matrix metalloproteinase-2/tissue matrix metalloproteinase inhibitor-2 ratio. Atorvastatin 0-12 matrix metallopeptidase 2 Rattus norvegicus 120-190 23195595-1 2013 Normobaric hyperoxia (NBO), which maintains penumbral oxygenation, reduces brain injury during cerebral ischemia, and minocycline, a tetracycline derivative, reduces reperfusion injury, including inflammation, apoptosis and matrix metalloproteinases (MMPs) activation. Minocycline 118-129 matrix metallopeptidase 2 Rattus norvegicus 251-255 23073243-12 2013 Our findings show that increased MMP-2 activity is associated with concomitant development of LV hypertrophy and increased TGF-beta and ROS levels. Reactive Oxygen Species 136-139 matrix metallopeptidase 2 Rattus norvegicus 33-38 23769575-10 2013 Compared with the MI group, the atorvastatin group showed significantly reduced expression of type I and III collagen, unchanged expression of MMP-2, significantly reduced expression of TIMP-2, and an increased MMP-2/TIMP-2 ratio. Atorvastatin 32-44 matrix metallopeptidase 2 Rattus norvegicus 143-148 23769575-10 2013 Compared with the MI group, the atorvastatin group showed significantly reduced expression of type I and III collagen, unchanged expression of MMP-2, significantly reduced expression of TIMP-2, and an increased MMP-2/TIMP-2 ratio. Atorvastatin 32-44 matrix metallopeptidase 2 Rattus norvegicus 211-216 23769575-11 2013 We further found that atorvastatin significantly inhibited the Ang II-induced fibroblast proliferation and the expression of type I and type III collagen in cardiac fibroblasts while increasing the MMP-2/TIMP-2 ratio. Atorvastatin 22-34 matrix metallopeptidase 2 Rattus norvegicus 198-203 23769575-12 2013 CONCLUSIONS: These data suggest that atorvastatin can inhibit cardiac fibroblast proliferation and enhance collagen degradation by increasing the MMP-2/TIMP-2 ratio, thereby inhibiting the formation of myocardial fibrosis in rats with heart failure after myocardial infarction. Atorvastatin 37-49 matrix metallopeptidase 2 Rattus norvegicus 146-151 23127783-3 2013 In in vitro experiments performed in neonatal rat cardiac fibroblasts, leonurine (10-20 muM) pretreatment attenuated Ang II-induced activation of extracellular signal-regulated kinase 1/2, production of intracellular reactive oxygen species (ROS), expression and activity of matrix metalloproteinase (MMP)-2/9, and expression of alpha-smooth muscle actin and types I and III collagen. leonurine 71-80 matrix metallopeptidase 2 Rattus norvegicus 275-309 23861715-7 2013 Administration of QSYQ could attenuate LAD-induced HF, and AngII-NOX2-ROS-MMPs pathway seemed to be the critical potential targets for QSYQ to reduce the remodeling. ros 70-73 matrix metallopeptidase 2 Rattus norvegicus 74-78 23861715-7 2013 Administration of QSYQ could attenuate LAD-induced HF, and AngII-NOX2-ROS-MMPs pathway seemed to be the critical potential targets for QSYQ to reduce the remodeling. qsyq 135-139 matrix metallopeptidase 2 Rattus norvegicus 74-78 23127783-5 2013 In vivo studies using a post-MI model in rats indicated that administration of leonurine inhibited myocardial fibrosis while reducing cardiac Nox4 expression, ROS production, NF-kappaB activation, and plasma MMP-2 activity. leonurine 79-88 matrix metallopeptidase 2 Rattus norvegicus 208-213 23124168-0 2013 Effect of antisense TIMP-1 cDNA on the expression of TIMP-1 and MMP-2 in lung tissue with pulmonary fibrosis induced by bleomycin. Bleomycin 120-129 matrix metallopeptidase 2 Rattus norvegicus 64-69 22475348-12 2013 MMPs correlated with -LV dP/dt(max) (% of baseline) both in plasma and in myocardial tissue. dp 25-27 matrix metallopeptidase 2 Rattus norvegicus 0-4 22475348-12 2013 MMPs correlated with -LV dP/dt(max) (% of baseline) both in plasma and in myocardial tissue. Thymidine 28-30 matrix metallopeptidase 2 Rattus norvegicus 0-4 22960133-7 2012 Also, Schisandrin B treated animal treatment abrogated protein expression of TNF-alpha and IL-1beta and degradation of MMP-2 and MMP-9 in ischemic hemispheres. schizandrin B 6-19 matrix metallopeptidase 2 Rattus norvegicus 119-124 23378729-12 2013 MMP-2 gene expression showed a tendency to decrease in the azithromycin group (p=0.063). Azithromycin 59-71 matrix metallopeptidase 2 Rattus norvegicus 0-5 23344254-6 2013 RESULTS: Cariporide significantly suppressed AGE-induced neointimal hyperplasia, vascular smooth muscle cell (VSMC) proliferation, COX-2, MMP-2 and MMP-9 expression. cariporide 9-19 matrix metallopeptidase 2 Rattus norvegicus 138-143 23344254-9 2013 CONCLUSIONS: The results indicated that cariporide inhibited AGE-induced neointimal formation by suppressing the VSMC proliferation and the up-regulation of COX-2, MMP-2, MMP-9 via inhibiting ROS and NF-kB activation. cariporide 40-50 matrix metallopeptidase 2 Rattus norvegicus 164-169 23409069-4 2013 Alcohol-induced upregulation of DDR2 was associated with the expression of matrix metalloproteinase 2, the transforming growth factor beta1 signaling pathway and tissue inhibitor of metalloproteinase 1; collagen deposition; and extracellular matrix remodeling. Alcohols 0-7 matrix metallopeptidase 2 Rattus norvegicus 75-101 23249435-2 2012 The aim of the present study was to develop a model of liver fibrosis combining ex vivo tissue culture of livers from CCl(4) treated animals with an ELISA detecting a fragment of type III collagen generated in vitro by MMP-9 (C3M), known to be associated with liver fibrosis and to investigate cAMP modulation of MMP activity and liver tissue turnover in this model. Cyclic AMP 294-298 matrix metallopeptidase 2 Rattus norvegicus 219-222 21474293-2 2012 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin (through its COX and tPA inhibitory action) and this combination can reduce cardiovascular dysfunction of diabetes. Minocycline 21-32 matrix metallopeptidase 2 Rattus norvegicus 41-46 21474293-2 2012 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin (through its COX and tPA inhibitory action) and this combination can reduce cardiovascular dysfunction of diabetes. Aspirin 87-94 matrix metallopeptidase 2 Rattus norvegicus 41-46 22989100-13 2012 Quercetin also induced activation of matrix metalloproteinases MMP2 and MMP9 contributing to decreased index of fibrosis. Quercetin 0-9 matrix metallopeptidase 2 Rattus norvegicus 63-67 22989100-14 2012 CONCLUSIONS: Treatment with quercetin reduces oxidation and inflammation and also prevents liver fibrosis, through induction of HSC apoptosis and activation of MMPs. Quercetin 28-37 matrix metallopeptidase 2 Rattus norvegicus 160-164 23052352-11 2012 In 2K-1C rats, ASE prevented vascular remodeling and the increased expression/levels of MMP-2. ase 15-18 matrix metallopeptidase 2 Rattus norvegicus 88-93 22914642-6 2012 Simultaneous treatment with the FAK inhibitor PF573228 abolished exogenous MMP-2-enhanced FAK (Tyr397) phosphorylation and collagen-I expression. 6-(4-(3-(methylsulfonyl)benzylamino)-5-(trifluoromethyl)pyrimidin-2-ylamino)-3,4-dihydroquinolin-2(1H)-one 46-54 matrix metallopeptidase 2 Rattus norvegicus 75-80 22914642-8 2012 NE-stimulated endogenous MMP-2 activation in conditioned medium was significantly attenuated by simultaneous treatment with the MMP inhibitor PD166793. (R)-2-(4'-bromo-biphenyl-4-sulfonyl-amino)-3-methyl-butyric acid 142-150 matrix metallopeptidase 2 Rattus norvegicus 25-30 21474293-2 2012 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin (through its COX and tPA inhibitory action) and this combination can reduce cardiovascular dysfunction of diabetes. Tetradecanoylphorbol Acetate 116-119 matrix metallopeptidase 2 Rattus norvegicus 41-46 21474293-16 2012 Present study revealed that aspirin potentate minocycline induced MMP-2 and MMP-9 inhibition to ameliorate cardiovascular dysfunction of diabetes and this combination can be an approach for the treatment. Aspirin 28-35 matrix metallopeptidase 2 Rattus norvegicus 66-71 21474293-16 2012 Present study revealed that aspirin potentate minocycline induced MMP-2 and MMP-9 inhibition to ameliorate cardiovascular dysfunction of diabetes and this combination can be an approach for the treatment. Minocycline 46-57 matrix metallopeptidase 2 Rattus norvegicus 66-71 22261714-12 2012 Pioglitazone can ameliorate cardiac remodeling by suppressing the gene expression of TGF-beta1 and regulating the MMP-2/TIMP-2 system. Pioglitazone 0-12 matrix metallopeptidase 2 Rattus norvegicus 114-119 22895819-0 2012 Effect of Etiasa on the expression of matrix metalloproteinase-2 and tumor necrosis factor-alpha in a rat model of ulcerative colitis. etiasa 10-16 matrix metallopeptidase 2 Rattus norvegicus 38-108 23040778-11 2012 UFH could exert protective effects by inhibiting expression of MMP-2 and MMP-9 in serum and lung tissue, in both mRNA and protein expression. Heparin 0-3 matrix metallopeptidase 2 Rattus norvegicus 63-68 22842067-6 2012 Hexarelin treatment also increased matrix metalloproteinase (MMP)-2 and MMP-9 activities and decreased myocardial mRNA expression of tissue inhibitor of metalloproteinase (TIMP)-1 in SHRs. hexarelin 0-9 matrix metallopeptidase 2 Rattus norvegicus 35-67 22842067-9 2012 In summary, our data demonstrate that hexarelin reduces cardiac fibrosis in SHRs, perhaps by decreasing collagen synthesis and accelerating collagen degradation via regulation of MMPs/TIMP. hexarelin 38-47 matrix metallopeptidase 2 Rattus norvegicus 179-183 22618526-7 2012 Here we reported the involvement of cyclic-GMP-dependent protein kinase (PKG) (an important mediator of NO and cGMP signaling pathway in VSMC) on MMP-2 expression in rat aortic SMC. Cyclic GMP 111-115 matrix metallopeptidase 2 Rattus norvegicus 146-151 22659584-0 2012 Chlorogenic acid ameliorates brain damage and edema by inhibiting matrix metalloproteinase-2 and 9 in a rat model of focal cerebral ischemia. Chlorogenic Acid 0-16 matrix metallopeptidase 2 Rattus norvegicus 66-98 22775217-5 2012 Activation of AQP4, p66Shc, ATF-6, NADPH oxidase subunits p22phox, gp91phox and matrix metalloproteinase 2 (P < 0.01) was significant and was suppressed by arginine, rhein and indometacin but not by l-arginine. Arginine 159-167 matrix metallopeptidase 2 Rattus norvegicus 80-106 22871104-10 2012 RESULTS: As compared to untreated MI rats, sildenafil improved LVEF, reduced collagen, myofibroblasts, and circulating MMPs, and increased cardiac troponin T. MDSC replicated most of these effects and stimulated cardiac angiogenesis. Sildenafil Citrate 43-53 matrix metallopeptidase 2 Rattus norvegicus 119-123 22441658-7 2012 (3) The expression of CD44v6, ICAM-1, MMP-2 and VEGF of tissue in CO(2) and N(2) group after 1, 2 and 4 weeks of pneumoperitoneum were lower than air group, TIMP-2 and ENS were higher than air group. Carbon Dioxide 66-71 matrix metallopeptidase 2 Rattus norvegicus 38-43 22441658-7 2012 (3) The expression of CD44v6, ICAM-1, MMP-2 and VEGF of tissue in CO(2) and N(2) group after 1, 2 and 4 weeks of pneumoperitoneum were lower than air group, TIMP-2 and ENS were higher than air group. Nitrogen 76-80 matrix metallopeptidase 2 Rattus norvegicus 38-43 22775217-5 2012 Activation of AQP4, p66Shc, ATF-6, NADPH oxidase subunits p22phox, gp91phox and matrix metalloproteinase 2 (P < 0.01) was significant and was suppressed by arginine, rhein and indometacin but not by l-arginine. Indomethacin 179-190 matrix metallopeptidase 2 Rattus norvegicus 80-106 22775217-5 2012 Activation of AQP4, p66Shc, ATF-6, NADPH oxidase subunits p22phox, gp91phox and matrix metalloproteinase 2 (P < 0.01) was significant and was suppressed by arginine, rhein and indometacin but not by l-arginine. Arginine 202-212 matrix metallopeptidase 2 Rattus norvegicus 80-106 22676642-6 2012 Inhibition of MMP-9/MMP-2 suppressed CCI-induced mechanical allodynia and concomitant TNF-alpha and IL-17A expression in nerves. CCI 37-40 matrix metallopeptidase 2 Rattus norvegicus 20-25 22430123-12 2012 Lung VEGF and eNOS increased in the L-citrulline-treated rats, though this treatment did not change MMP2 gene expression but regulated the MMP2 active protein, which rose in BALF (p = 0.003). Citrulline 36-48 matrix metallopeptidase 2 Rattus norvegicus 139-143 21247645-4 2012 The aim of the present study was to evaluate the effect of Rosiglitazone on lipopolysaccharide (LPS)-induced MMP-2 activation as well as its possible mechanism. Rosiglitazone 59-72 matrix metallopeptidase 2 Rattus norvegicus 109-114 21247645-9 2012 RESULTS: LPS-induced MMP-2 activity was inhibited by Rosiglitazone (PPARgamma agonist) in the rat aortic endothelial cells (RAEC). Rosiglitazone 53-66 matrix metallopeptidase 2 Rattus norvegicus 21-26 21247645-10 2012 LPS-induced MMP-2 activation was diminished due to exposure to NF-kappaB Activation Inhibitor II (JSH-23) or Ras inhibitor, farnesylthiosalicylic acid (FTS). 4-methyl-N1-(3-phenylpropyl)benzene-1,2-diamine 98-104 matrix metallopeptidase 2 Rattus norvegicus 12-17 21247645-10 2012 LPS-induced MMP-2 activation was diminished due to exposure to NF-kappaB Activation Inhibitor II (JSH-23) or Ras inhibitor, farnesylthiosalicylic acid (FTS). farnesylthiosalicylic acid 124-150 matrix metallopeptidase 2 Rattus norvegicus 12-17 21247645-10 2012 LPS-induced MMP-2 activation was diminished due to exposure to NF-kappaB Activation Inhibitor II (JSH-23) or Ras inhibitor, farnesylthiosalicylic acid (FTS). farnesylthiosalicylic acid 152-155 matrix metallopeptidase 2 Rattus norvegicus 12-17 21247645-14 2012 CONCLUSIONS: Our data shows that PPARgamma agonist, Rosiglitazone suppresses LPS-activated MMP-2 secretion via Ras-MEK1/2 signaling pathways and NF-kappaB activation. Rosiglitazone 52-65 matrix metallopeptidase 2 Rattus norvegicus 91-96 22496348-5 2012 Pretreatment with the MMP inhibitors SB-3CT (MMP-2/MMP-9 Inhibitor IV), BB-94 (batimastat), or Ro-28-2653 (cipemastat) enhanced contraction in myometrium of pregnant rats. SB 3CT compound 37-43 matrix metallopeptidase 2 Rattus norvegicus 45-50 25206993-8 2012 An increase of immunhistochemical reactions of iNOS and MMP2, but a decrease of eNOS activity, were observed in rat hippocampus and peripheral tissues during the PTZ induced seizures. Pentylenetetrazole 162-165 matrix metallopeptidase 2 Rattus norvegicus 56-60 22154988-8 2012 The inhibitory effects of FA and GA on MMP-2 were very comparable. Gallic Acid 33-35 matrix metallopeptidase 2 Rattus norvegicus 39-44 22154988-9 2012 GA suppressed MMP-2 more effectively than FA in DRCKD rats. Gallic Acid 0-2 matrix metallopeptidase 2 Rattus norvegicus 14-19 22426603-7 2012 Treatment of RASMCs with emodin significantly and dose-dependently attenuated TNF-alpha-induced proliferation, migration, mRNA and protein expression of MMP-2 and MMP-9, and NF-kappaB activation. rasmcs 13-19 matrix metallopeptidase 2 Rattus norvegicus 177-182 22249316-8 2012 In addition, MGO-injected retinas demonstrated increases of both activity and expression of MMP-2 and MMP-9, and the degradation of occludin was found in the MGO-injected retinas. Pyruvaldehyde 13-16 matrix metallopeptidase 2 Rattus norvegicus 92-97 22528580-10 2012 Although the CG group had higher tissue MMP-2 levels than the control group, the tissue MMP-2 levels were not significantly different from the other groups. chlorhexidine gluconate 13-15 matrix metallopeptidase 2 Rattus norvegicus 40-45 22249316-4 2012 Herein, we hypothesize that increased levels of MGO disrupt the tight junction protein known as occludin protein by matrix metalloproteinases (MMPs), leading to breakage of the BRB. Pyruvaldehyde 48-51 matrix metallopeptidase 2 Rattus norvegicus 143-147 22249316-9 2012 CONCLUSIONS: The results suggest that the activation of MMPs by elevated levels of MGO in the retina may facilitate an increase in vascular permeability by a mechanism involving proteolytic degradation of occludin. Pyruvaldehyde 83-86 matrix metallopeptidase 2 Rattus norvegicus 56-60 22180326-8 2012 MMP-2 and MMP-9 activities were increased in embryos and decidua from diabetic rats and decreased with safflower oil and folic acid supplementations. Folic Acid 121-131 matrix metallopeptidase 2 Rattus norvegicus 0-5 22173873-7 2012 The results of real-time PCR, western blot, and gelatin zymography analyses revealed that the gene and protein expression and activities of matrix metalloproteinases (MMPs) MMP-2 and MMP-9 were significantly elevated in a different time-dependent manner after ischemia-reperfusion but significantly inhibited by doxycycline treatment. Doxycycline 312-323 matrix metallopeptidase 2 Rattus norvegicus 167-171 22173873-7 2012 The results of real-time PCR, western blot, and gelatin zymography analyses revealed that the gene and protein expression and activities of matrix metalloproteinases (MMPs) MMP-2 and MMP-9 were significantly elevated in a different time-dependent manner after ischemia-reperfusion but significantly inhibited by doxycycline treatment. Doxycycline 312-323 matrix metallopeptidase 2 Rattus norvegicus 173-178 22173873-9 2012 These results suggested that the protective effects of doxycycline against BBB damage induced by reperfusion might be related to the up-regulation of tight junction proteins and inhibition of MMP-2, MMP-9, and PKCdelta. Doxycycline 55-66 matrix metallopeptidase 2 Rattus norvegicus 192-197 22447222-1 2012 AIM: To investigate the role of matrix metalloproteinases (MMPs) in the responses of rats to a prolonged doxorubicin (DOX) treatment. Doxorubicin 105-116 matrix metallopeptidase 2 Rattus norvegicus 59-63 22804981-1 2012 OBJECTIVE: To observe the expression of the matrix metalloproteinase 2 (MMP-2) and membrane-type 1 metalloproteinase (MT1-MMP) in lung of rats exposed to paraquat (PQ) and the effects of Salvia miltiorrhiza monomer IH764-3 on above expression. Paraquat 154-162 matrix metallopeptidase 2 Rattus norvegicus 44-70 22804981-1 2012 OBJECTIVE: To observe the expression of the matrix metalloproteinase 2 (MMP-2) and membrane-type 1 metalloproteinase (MT1-MMP) in lung of rats exposed to paraquat (PQ) and the effects of Salvia miltiorrhiza monomer IH764-3 on above expression. Paraquat 154-162 matrix metallopeptidase 2 Rattus norvegicus 72-77 22804981-1 2012 OBJECTIVE: To observe the expression of the matrix metalloproteinase 2 (MMP-2) and membrane-type 1 metalloproteinase (MT1-MMP) in lung of rats exposed to paraquat (PQ) and the effects of Salvia miltiorrhiza monomer IH764-3 on above expression. Paraquat 164-166 matrix metallopeptidase 2 Rattus norvegicus 44-70 22804981-1 2012 OBJECTIVE: To observe the expression of the matrix metalloproteinase 2 (MMP-2) and membrane-type 1 metalloproteinase (MT1-MMP) in lung of rats exposed to paraquat (PQ) and the effects of Salvia miltiorrhiza monomer IH764-3 on above expression. Paraquat 164-166 matrix metallopeptidase 2 Rattus norvegicus 72-77 22804981-12 2012 CONCLUSION: The expression changes of MMP-2 and MT1-MMP genes of lungs in rats intragastrically exposed to PQ could result in the unbalance the synthesis and degradation of ECM, which may be a cause of lung fibrosis. Paraquat 107-109 matrix metallopeptidase 2 Rattus norvegicus 38-43 22447222-1 2012 AIM: To investigate the role of matrix metalloproteinases (MMPs) in the responses of rats to a prolonged doxorubicin (DOX) treatment. Doxorubicin 118-121 matrix metallopeptidase 2 Rattus norvegicus 59-63 22447222-12 2012 The effects of DOX were linked to a stimulation of plasma MMP-2 and MMP-9 activities that had already increased by 4 weeks after the end of the treatment. Doxorubicin 15-18 matrix metallopeptidase 2 Rattus norvegicus 58-63 22447222-13 2012 In the left ventricle, however, DOX only led to increased MMP-2 activation at 8 weeks after the end of treatment. Doxorubicin 32-35 matrix metallopeptidase 2 Rattus norvegicus 58-63 22447222-14 2012 These changes in tissue MMP-2 were connected with stimulation of Akt kinase activation, inhibition of SOD, an increase in superoxide levels, induction of iNOS protein expression and caspase-3 activation. Superoxides 122-132 matrix metallopeptidase 2 Rattus norvegicus 24-29 22447222-15 2012 CONCLUSION: Our results show that MMPs are involved in the chronic cardiotoxicity of DOX in rats. Doxorubicin 85-88 matrix metallopeptidase 2 Rattus norvegicus 34-38 22199370-5 2012 Some rats were given the MMP inhibitors ONO-4817 or doxycycline. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 40-48 matrix metallopeptidase 2 Rattus norvegicus 25-28 22998827-7 2012 BBB permeability became progressively more severe, and recovered at 6 h. The gene and protein expression of occludin and ZO-1 were significantly decreased, while MMP-2 and MMP-9 expression were significantly increased after exposure to PEMF. pemf 236-240 matrix metallopeptidase 2 Rattus norvegicus 162-167 22260250-4 2012 Concurrently, ammonia increased the activity of extracellular matrix metalloproteinases (MMP-2/MMP-9), increased cell permeability to fluorescein isothiocyanate-dextran (40 kDa), and increased the expression of y+LAT2, a transporter that mediates the uptake to the cells of the nitric oxide precursor, arginine. Ammonia 14-21 matrix metallopeptidase 2 Rattus norvegicus 89-94 22260250-5 2012 The increase of cell permeability was ameliorated upon co-treatment with a MMP inhibitor, SB-3CT and with an antioxidant, glutathione diethyl ester, which also reduced F2-isoprostanes. SB 3CT compound 90-96 matrix metallopeptidase 2 Rattus norvegicus 75-78 22260250-5 2012 The increase of cell permeability was ameliorated upon co-treatment with a MMP inhibitor, SB-3CT and with an antioxidant, glutathione diethyl ester, which also reduced F2-isoprostanes. glutathione diethyl ester 122-147 matrix metallopeptidase 2 Rattus norvegicus 75-78 22260250-5 2012 The increase of cell permeability was ameliorated upon co-treatment with a MMP inhibitor, SB-3CT and with an antioxidant, glutathione diethyl ester, which also reduced F2-isoprostanes. F2-Isoprostanes 168-183 matrix metallopeptidase 2 Rattus norvegicus 75-78 22260250-7 2012 The results support the concept that ONS and ONS-related activation of MMPs in cerebral capillary endothelial cells contribute to the alterations in BBB permeability and to the vasogenic component of cerebral edema associated with acute liver failure. (2S)-(4-{3-[(4,5-dichloro-1-methyl-1H-indole-2-carbonyl)amino]oxetan-3-yl}phenyl)(pyridin-3-yl)acetic acid 37-40 matrix metallopeptidase 2 Rattus norvegicus 71-75 22260250-7 2012 The results support the concept that ONS and ONS-related activation of MMPs in cerebral capillary endothelial cells contribute to the alterations in BBB permeability and to the vasogenic component of cerebral edema associated with acute liver failure. (2S)-(4-{3-[(4,5-dichloro-1-methyl-1H-indole-2-carbonyl)amino]oxetan-3-yl}phenyl)(pyridin-3-yl)acetic acid 45-48 matrix metallopeptidase 2 Rattus norvegicus 71-75 22397940-10 2012 The immunoprecipitation of heart homogenates using anti-phosphoserine antibody showed that MMP-2 is phosphorylated. Phosphoserine 56-69 matrix metallopeptidase 2 Rattus norvegicus 91-96 22290321-0 2012 Nandrolone inhibits MMP-2 in the left ventricle of rats. Nandrolone 0-10 matrix metallopeptidase 2 Rattus norvegicus 20-25 22290321-2 2012 The main objective of the present study was to investigate the effects of nandrolone decanoate on matrix metalloprotease (MMP-2) activity and protein level in the left ventricle (LV) of rats after 7 weeks of mechanical load exercise. Nandrolone Decanoate 74-94 matrix metallopeptidase 2 Rattus norvegicus 122-127 22378877-6 2012 Using selective MMP-2/9 inhibitor SB-3CT (2-[[(4-phenoxyphenyl)sulfonyl]methyl]-thiirane) or their neutralizing antibodies or Cav-1 siRNA, we found that MMP-2 was the major enzyme mediating OGD-induced occludin degradation, while Cav-1 was responsible for claudin-5 redistribution. 2-((4-phenoxyphenyl)sulfonylmethyl)thiirane 42-88 matrix metallopeptidase 2 Rattus norvegicus 16-40 22142686-5 2012 Oral administration of MOE400 and MOE800 for 14 days significantly inhibited intimal area, intimal/medial ratio (I/M), stenosis rate, expression of proliferating cell nuclear antigen (PCNA), MMP-2, and -9 in denudated rat carotid artery. moe400 23-29 matrix metallopeptidase 2 Rattus norvegicus 191-204 22142686-5 2012 Oral administration of MOE400 and MOE800 for 14 days significantly inhibited intimal area, intimal/medial ratio (I/M), stenosis rate, expression of proliferating cell nuclear antigen (PCNA), MMP-2, and -9 in denudated rat carotid artery. moe800 34-40 matrix metallopeptidase 2 Rattus norvegicus 191-204 22083546-6 2012 Manipulating CaSR function in these cells by NPS2390 (an antagonist of CaSR) or GdCl(3) (an agonist of CaSR) affected the oxLDL-induced MMP-2 production. gdcl 80-84 matrix metallopeptidase 2 Rattus norvegicus 136-141 22083546-8 2012 Phosphorylation of Akt and MMP-2 production stimulated by oxLDL were attenuated by LY294002 (a specific inhibitor of PI3K). 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 83-91 matrix metallopeptidase 2 Rattus norvegicus 27-32 22045867-4 2012 We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. Minocycline 54-65 matrix metallopeptidase 2 Rattus norvegicus 35-40 22225921-7 2012 The upregulation of MMP-2 and MMP-9, as well as AQP-4 and AQP-9, following ischemia/reperfusion, was significantly reduced in ethanol-treated groups (P<0.05). Ethanol 126-133 matrix metallopeptidase 2 Rattus norvegicus 20-25 22225921-8 2012 CONCLUSIONS: Ethanol ameliorates brain edema and BBB disruption after stroke, in association with a reduction in the expression of MMPs and AQPs. Ethanol 13-20 matrix metallopeptidase 2 Rattus norvegicus 131-135 21740410-5 2012 KEY RESULTS: Treatment of FHRs with the MMP inhibitor doxycycline, preserved endothelial function as well as prevented the development of hypertension, suggesting that MMPs impair endothelial function. Doxycycline 54-65 matrix metallopeptidase 2 Rattus norvegicus 168-172 22273146-8 2012 BBB-P correlated positively with MMP-2 and MMP-9 in controls, whereas hyperoxia led to an inverse association, most pronounced for HBO/MMP-9 (r = -0.606; P < 0.05). bbb-p 0-5 matrix metallopeptidase 2 Rattus norvegicus 33-38 22063920-5 2012 We detected a strong antagonistic action of new triazine derivative (IMT) on ethanol-induced rat liver stellate cells activation, observed as a significant decrease in alpha-SMA, collagen synthesis, reactive oxygen species production, TGF-beta, TNF-alpha, MMP-2 and TIMP-1 production as well as JNK, p38MAPK, NFkappaB, IkappaB, Smad3 phosphorylation. Triazines 48-56 matrix metallopeptidase 2 Rattus norvegicus 256-261 22353423-13 2012 Importantly, intrathecal administration of NOV siRNA specifically led to an up-regulation of MMP-9 in the DRG and MMP-2 in the DHSC concomitant with increased mechanical allodynia. dhsc 127-131 matrix metallopeptidase 2 Rattus norvegicus 114-119 21792602-7 2012 IL-1beta or TNF-alpha increased expression of MMP-9 and MMP-2 in rheumatoid synoviocytes; EGF stimulated expression of MMP-9 but not of MMP-2; genistein suppressed production of MMP-9 more than MMP-2 induced by IL-1beta or TNF-alpha; rMMP-9, rMMP-2, or their inhibitors had no effect on the (3)H-TdR incorporation of synovial cells. Genistein 143-152 matrix metallopeptidase 2 Rattus norvegicus 242-248 22248199-14 2012 Tissue MMP-2 levels were significantly higher in the CG group compared other groups (P < 0.05). cysteinylglycine 53-55 matrix metallopeptidase 2 Rattus norvegicus 7-12 22063920-5 2012 We detected a strong antagonistic action of new triazine derivative (IMT) on ethanol-induced rat liver stellate cells activation, observed as a significant decrease in alpha-SMA, collagen synthesis, reactive oxygen species production, TGF-beta, TNF-alpha, MMP-2 and TIMP-1 production as well as JNK, p38MAPK, NFkappaB, IkappaB, Smad3 phosphorylation. Ethanol 77-84 matrix metallopeptidase 2 Rattus norvegicus 256-261 21944319-8 2012 Relative to medium, VSMCs delivered at either time point significantly reduced cardiac expression and activity of MMP-2 and -9, reduced expression of TNF-alpha, and increased expression of TIMP-3. vsmcs 20-25 matrix metallopeptidase 2 Rattus norvegicus 114-126 22045867-4 2012 We hypothesised that inhibition of MMP-2 and MMP-9 by minocycline can be potentiated by aspirin through inhibition of cyclooxygenase-2 and tissue plasminogen activator, resulting in amelioration of clinical cerebral ischaemia in diabetes. Aspirin 88-95 matrix metallopeptidase 2 Rattus norvegicus 35-40 22045867-9 2012 Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. Aspirin 38-45 matrix metallopeptidase 2 Rattus norvegicus 189-194 22045867-9 2012 Our data indicate that combination of aspirin and minocycline therapy protects from the consequences of cerebral ischaemia in animal models of diabetes and is associated with inhibition of MMP-2 and MMP-9. Minocycline 50-61 matrix metallopeptidase 2 Rattus norvegicus 189-194 22186621-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. Polyphenols 0-11 matrix metallopeptidase 2 Rattus norvegicus 82-86 21360558-8 2012 ASA and IBP prevented translocation of NFkappaB to the nucleus and, interestingly, ASA induced MMP-2 and MMP-13 whereas IBP induced MMP-2, MMP-9 and MMP-13. Aspirin 0-3 matrix metallopeptidase 2 Rattus norvegicus 132-137 21360558-8 2012 ASA and IBP prevented translocation of NFkappaB to the nucleus and, interestingly, ASA induced MMP-2 and MMP-13 whereas IBP induced MMP-2, MMP-9 and MMP-13. Ibuprofen 8-11 matrix metallopeptidase 2 Rattus norvegicus 95-100 21360558-8 2012 ASA and IBP prevented translocation of NFkappaB to the nucleus and, interestingly, ASA induced MMP-2 and MMP-13 whereas IBP induced MMP-2, MMP-9 and MMP-13. Ibuprofen 8-11 matrix metallopeptidase 2 Rattus norvegicus 132-137 21360558-8 2012 ASA and IBP prevented translocation of NFkappaB to the nucleus and, interestingly, ASA induced MMP-2 and MMP-13 whereas IBP induced MMP-2, MMP-9 and MMP-13. Aspirin 83-86 matrix metallopeptidase 2 Rattus norvegicus 95-100 21360558-8 2012 ASA and IBP prevented translocation of NFkappaB to the nucleus and, interestingly, ASA induced MMP-2 and MMP-13 whereas IBP induced MMP-2, MMP-9 and MMP-13. Ibuprofen 120-123 matrix metallopeptidase 2 Rattus norvegicus 132-137 22150674-11 2012 Kidneys from ethanol-treated rats showed increased activity of MMP-2. Ethanol 13-20 matrix metallopeptidase 2 Rattus norvegicus 63-68 22150674-15 2012 Since iNOS-derived NO and MMPs contribute to progressive renal injury, the increased levels of NO and MMPs observed in ethanol-treated rats might contribute to progressive renal damage. Ethanol 119-126 matrix metallopeptidase 2 Rattus norvegicus 102-106 22792126-5 2012 Moreover, significant decreases of MMP-9/MMP-2 ratio, uPA, phosphorylated ERK (p-ERK) and NF-kappaB (p-P65) were detected in livers of CCl(4)-administrated rats that were treated with OGAE or sylimarin as compared to those rats that were treated with saline or CCl(4). Cefaclor 135-138 matrix metallopeptidase 2 Rattus norvegicus 41-46 22577570-9 2012 After treatment with quercetin, we observed an improvement in liver complications, decreased fibrosis, as analyzed by picrosirius for the quantification of collagen, and decreased levels of matrix metalloproteinase 2 (MMP-2) compared with the CCl(4) group. Quercetin 21-30 matrix metallopeptidase 2 Rattus norvegicus 190-216 22577570-9 2012 After treatment with quercetin, we observed an improvement in liver complications, decreased fibrosis, as analyzed by picrosirius for the quantification of collagen, and decreased levels of matrix metalloproteinase 2 (MMP-2) compared with the CCl(4) group. Quercetin 21-30 matrix metallopeptidase 2 Rattus norvegicus 218-223 22906269-0 2012 The therapeutic effect of (DL)-3-n-butylphthalide in rats with chronic cerebral hypoperfusion through downregulation of amyloid precursor protein and matrix metalloproteinase-2. 3-n-butylphthalide 26-49 matrix metallopeptidase 2 Rattus norvegicus 150-176 22906269-6 2012 Western blot analysis indicated that, in comparison with the sham-operated control group, protein levels of Abeta40 and MMP-2 were significantly increased in the cerebral cortex of hypoperfused rats, and treatment with DL-NBP prevented this hypoperfusion-induced increase in Abeta40 and MMP-2. 3-n-butylphthalide 220-226 matrix metallopeptidase 2 Rattus norvegicus 120-125 22906269-6 2012 Western blot analysis indicated that, in comparison with the sham-operated control group, protein levels of Abeta40 and MMP-2 were significantly increased in the cerebral cortex of hypoperfused rats, and treatment with DL-NBP prevented this hypoperfusion-induced increase in Abeta40 and MMP-2. 3-n-butylphthalide 220-226 matrix metallopeptidase 2 Rattus norvegicus 288-293 22186621-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. epigallocatechin gallate 39-65 matrix metallopeptidase 2 Rattus norvegicus 82-86 22186621-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. epigallocatechin gallate 67-71 matrix metallopeptidase 2 Rattus norvegicus 82-86 22186621-8 2012 MMP-2 and MMP-9 activities were lower in TFDG- and EGCG-treated rat osteoclast precursor cells than in control cultures. theaflavin-3,3'-digallate 41-45 matrix metallopeptidase 2 Rattus norvegicus 0-5 32092838-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. Polyphenols 0-11 matrix metallopeptidase 2 Rattus norvegicus 82-86 32092838-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. epigallocatechin gallate 39-65 matrix metallopeptidase 2 Rattus norvegicus 82-86 22186621-8 2012 MMP-2 and MMP-9 activities were lower in TFDG- and EGCG-treated rat osteoclast precursor cells than in control cultures. epigallocatechin gallate 51-55 matrix metallopeptidase 2 Rattus norvegicus 0-5 22186621-10 2012 TFDG and EGCG inhibited the formation and differentiation of osteoclasts via inhibition of MMPs. theaflavin-3,3'-digallate 0-4 matrix metallopeptidase 2 Rattus norvegicus 91-95 22186621-10 2012 TFDG and EGCG inhibited the formation and differentiation of osteoclasts via inhibition of MMPs. epigallocatechin gallate 9-13 matrix metallopeptidase 2 Rattus norvegicus 91-95 22814007-0 2012 Baclofen influences acquisition and MMP-2, MMP-9 levels in the hippocampus of rats after hypoxia. Baclofen 0-8 matrix metallopeptidase 2 Rattus norvegicus 36-41 32092838-3 2012 Polyphenols in green tea, particularly epigallocatechin-3-gallate (EGCG), inhibit MMPs expression and activity. epigallocatechin gallate 67-71 matrix metallopeptidase 2 Rattus norvegicus 82-86 32092838-4 2012 However, the effects of the black tea polyphenol, theaflavin-3,3"-digallate (TFDG), on osteoclast and MMP activity are unknown. theaflavin-3,3'-digallate 77-81 matrix metallopeptidase 2 Rattus norvegicus 102-105 32092838-8 2012 MMP-2 and MMP-9 activities were lower in TFDG- and EGCG-treated rat osteoclast precursor cells than in control cultures. theaflavin-3,3'-digallate 41-45 matrix metallopeptidase 2 Rattus norvegicus 0-5 32092838-8 2012 MMP-2 and MMP-9 activities were lower in TFDG- and EGCG-treated rat osteoclast precursor cells than in control cultures. epigallocatechin gallate 51-55 matrix metallopeptidase 2 Rattus norvegicus 0-5 32092838-10 2012 TFDG and EGCG inhibited the formation and differentiation of osteoclasts via inhibition of MMPs. theaflavin-3,3'-digallate 0-4 matrix metallopeptidase 2 Rattus norvegicus 91-95 32092838-10 2012 TFDG and EGCG inhibited the formation and differentiation of osteoclasts via inhibition of MMPs. epigallocatechin gallate 9-13 matrix metallopeptidase 2 Rattus norvegicus 91-95 22814007-6 2012 Baclofen used before the deprivation of oxygen, decreased the level of the active form of MMP-2 and pro-MMP-9. Baclofen 0-8 matrix metallopeptidase 2 Rattus norvegicus 90-95 22814007-4 2012 There was a significant decrease in the level of the active form of MMP-2 as well as an increase in the level of pro-MMP-9 in the hippocampus of rats without hypoxia 30 min after the administration of baclofen. Baclofen 201-209 matrix metallopeptidase 2 Rattus norvegicus 68-73 22814007-7 2012 CONCLUSIONS: These results show that MMP-2 and MMP-9 activities in the hippocampus can be regulated by baclofen in non-pathological conditions and very shortly after hypoxia induction. Baclofen 103-111 matrix metallopeptidase 2 Rattus norvegicus 37-42 22814007-8 2012 We suggest that the changes in MMP-2 and MMP-9 levels are the mechanism activities of baclofen in the acquisition process. Baclofen 86-94 matrix metallopeptidase 2 Rattus norvegicus 31-36 22136281-0 2012 Pioglitazone reduces peritoneal fibrosis via inhibition of TGF-beta, MMP-2, and MMP-9 in a model of encapsulating peritoneal sclerosis. Pioglitazone 0-12 matrix metallopeptidase 2 Rattus norvegicus 69-74 23056375-9 2012 Furthermore, corticosterone treated endothelial cells in both 3-dimensional and monolayer cultures had decreased MMP-2 production and activation resulting in decreased proteolysis by endothelial cells, limiting their angiogenic potential. Corticosterone 13-27 matrix metallopeptidase 2 Rattus norvegicus 113-118 23056375-10 2012 Promoter assays revealed that corticosterone treatment transcriptionally repressed MMP-2, which may map to a predicted GRE between -1510 and -1386 bp of the MMP-2 promoter. Corticosterone 30-44 matrix metallopeptidase 2 Rattus norvegicus 83-88 23056375-10 2012 Promoter assays revealed that corticosterone treatment transcriptionally repressed MMP-2, which may map to a predicted GRE between -1510 and -1386 bp of the MMP-2 promoter. Corticosterone 30-44 matrix metallopeptidase 2 Rattus norvegicus 157-162 23056375-11 2012 Additionally, Sp1, a known transcriptional activator of MMP-2 was decreased following corticosterone treatment. Corticosterone 86-100 matrix metallopeptidase 2 Rattus norvegicus 56-61 22136281-1 2012 OBJECTIVE: Matrix metalloproteinases (MMPs) and transforming growth factor beta (TGF-beta) were increased in peritoneal dialysis patients with encapsulating peritoneal sclerosis (EPS) and in chlorhexidine gluconate (CG)-induced peritoneal sclerosing animal models. chlorhexidine gluconate 191-214 matrix metallopeptidase 2 Rattus norvegicus 38-42 22136281-1 2012 OBJECTIVE: Matrix metalloproteinases (MMPs) and transforming growth factor beta (TGF-beta) were increased in peritoneal dialysis patients with encapsulating peritoneal sclerosis (EPS) and in chlorhexidine gluconate (CG)-induced peritoneal sclerosing animal models. chlorhexidine gluconate 216-218 matrix metallopeptidase 2 Rattus norvegicus 38-42 22295524-1 2011 OBJECTIVE: To investigate the inhibitor of matrix metalloproteinase-2 (MMP-2) (2R)-2-[5-[4-[ ethyl-methylamino] phenyl [thiophene-2-sulfonylamino]-3-methylbutyric acid (TISAM) therapeutic effect on experimental autoimmune myocarditis (EAM) in Lewis rats. 2-[5-[4-[ ethyl-methylamino] phenyl [thiophene-2-sulfonylamino]-3-methylbutyric acid 83-167 matrix metallopeptidase 2 Rattus norvegicus 43-69 21971830-5 2011 Thus, after hours or days of relaxin treatment, respectively, arterial MMP-9 or MMP-2 hydrolyze "big" endothelin (ET) at a gly-leu bond to form ET(1-32), which in turn activates the endothelial ET(B) receptor/nitric oxide vasodilatory pathway. Glycine 123-126 matrix metallopeptidase 2 Rattus norvegicus 80-85 21971830-5 2011 Thus, after hours or days of relaxin treatment, respectively, arterial MMP-9 or MMP-2 hydrolyze "big" endothelin (ET) at a gly-leu bond to form ET(1-32), which in turn activates the endothelial ET(B) receptor/nitric oxide vasodilatory pathway. Leucine 127-130 matrix metallopeptidase 2 Rattus norvegicus 80-85 21971830-5 2011 Thus, after hours or days of relaxin treatment, respectively, arterial MMP-9 or MMP-2 hydrolyze "big" endothelin (ET) at a gly-leu bond to form ET(1-32), which in turn activates the endothelial ET(B) receptor/nitric oxide vasodilatory pathway. Nitric Oxide 209-221 matrix metallopeptidase 2 Rattus norvegicus 80-85 22045122-0 2011 Matrix metalloproteinase 2 induces epithelial-mesenchymal transition in proximal tubules from the luminal side and progresses fibrosis in mineralocorticoid/salt-induced hypertensive rats. Salts 156-160 matrix metallopeptidase 2 Rattus norvegicus 0-26 22045122-5 2011 RESULTS: At week 4, the DOCA-treated group exhibited hypertension, tubulointerstitial fibrosis, increased MMP2 activity in the kidney and urine, and overexpression of MMP2 in proximal tubule cells and MMP14 in apical membranes; these results were more pronounced at week 8. Desoxycorticosterone Acetate 24-28 matrix metallopeptidase 2 Rattus norvegicus 106-110 22045122-5 2011 RESULTS: At week 4, the DOCA-treated group exhibited hypertension, tubulointerstitial fibrosis, increased MMP2 activity in the kidney and urine, and overexpression of MMP2 in proximal tubule cells and MMP14 in apical membranes; these results were more pronounced at week 8. Desoxycorticosterone Acetate 24-28 matrix metallopeptidase 2 Rattus norvegicus 167-171 22045122-7 2011 These DOCA/salt-induced changes (except for hypertension) and fibrosis progression observed at week 8 were reversed by TISAM (a selective MMP2 inhibitor), which was administered from week 4 to week 8. Desoxycorticosterone Acetate 6-10 matrix metallopeptidase 2 Rattus norvegicus 138-142 22045122-7 2011 These DOCA/salt-induced changes (except for hypertension) and fibrosis progression observed at week 8 were reversed by TISAM (a selective MMP2 inhibitor), which was administered from week 4 to week 8. Salts 11-15 matrix metallopeptidase 2 Rattus norvegicus 138-142 22045122-7 2011 These DOCA/salt-induced changes (except for hypertension) and fibrosis progression observed at week 8 were reversed by TISAM (a selective MMP2 inhibitor), which was administered from week 4 to week 8. tisam 119-124 matrix metallopeptidase 2 Rattus norvegicus 138-142 22045122-9 2011 CONCLUSION: Eight weeks of treatment with DOCA/salt activated MMP2, primarily on the apical surface of proximal tubule cells, which induced epithelial-mesenchymal transition from the luminal side and promoted tubulointerstitial fibrosis progression. Desoxycorticosterone Acetate 42-46 matrix metallopeptidase 2 Rattus norvegicus 62-66 22045122-9 2011 CONCLUSION: Eight weeks of treatment with DOCA/salt activated MMP2, primarily on the apical surface of proximal tubule cells, which induced epithelial-mesenchymal transition from the luminal side and promoted tubulointerstitial fibrosis progression. Salts 47-51 matrix metallopeptidase 2 Rattus norvegicus 62-66 22039247-10 2011 With DTSH treatment, doxycycline inhibited the activity and expression of MMPs, the expression of VEGF and of phosphorylated VEGFR1 and VEGFR2, and the production of iNOS and IL-1beta in local cornea. dtsh 5-9 matrix metallopeptidase 2 Rattus norvegicus 74-78 22039247-10 2011 With DTSH treatment, doxycycline inhibited the activity and expression of MMPs, the expression of VEGF and of phosphorylated VEGFR1 and VEGFR2, and the production of iNOS and IL-1beta in local cornea. Doxycycline 21-32 matrix metallopeptidase 2 Rattus norvegicus 74-78 22039247-11 2011 CONCLUSIONS: Doxycycline enhances the inhibitory effects of bevacizumab on CNV and prevents its side effects on CWH, possibly by inhibiting the expression and activity of MMPs, the expression of VEGF and of phosphorylated VEGFR1 and VEGFR2, and the production of iNOS and IL-1beta. Doxycycline 13-24 matrix metallopeptidase 2 Rattus norvegicus 171-175 22741467-17 2012 CONCLUSION: The anti-fibrosis effects of A&A might be associated with modulating the imbalance of PAs/PAIs system as well as MMPs/TIMPs system, thereby alleviate ECM accumulation and interstitial fibrosis. a& 41-46 matrix metallopeptidase 2 Rattus norvegicus 129-133 21832167-1 2011 Our previous studies showed that the prototypical testicular toxic phthalate monoester, mono-(2-ethylhexyl) phthalate (MEHP), suppresses Sertoli cell TIMP2 levels and allows for the activation of MMP2 in seminiferous epithelium. phthalic acid 67-76 matrix metallopeptidase 2 Rattus norvegicus 196-200 21832167-1 2011 Our previous studies showed that the prototypical testicular toxic phthalate monoester, mono-(2-ethylhexyl) phthalate (MEHP), suppresses Sertoli cell TIMP2 levels and allows for the activation of MMP2 in seminiferous epithelium. mono-(2-ethylhexyl)phthalate 88-117 matrix metallopeptidase 2 Rattus norvegicus 196-200 21832167-1 2011 Our previous studies showed that the prototypical testicular toxic phthalate monoester, mono-(2-ethylhexyl) phthalate (MEHP), suppresses Sertoli cell TIMP2 levels and allows for the activation of MMP2 in seminiferous epithelium. mono-(2-ethylhexyl)phthalate 119-123 matrix metallopeptidase 2 Rattus norvegicus 196-200 21884701-11 2011 This was blocked by MMP 2 and 9 inhibition, which also abolished RI-induced CCG. cationic colloidal gold 76-79 matrix metallopeptidase 2 Rattus norvegicus 20-25 21884701-13 2011 In conclusion, MMP 2 and 9 activation is essential for CCG and is mediated, in part, by p38 MAPK. cationic colloidal gold 55-58 matrix metallopeptidase 2 Rattus norvegicus 15-26 21843641-1 2011 INTRODUCTION: Beyond their decades of long use as broad-spectrum antibiotics, tetracyclines and their derivatives have been shown to exhibit non-antimicrobial properties including their ability to interact with matrix metalloproteinases (MMP), tissue inhibitors of MMPs, growth factors and cytokines. Tetracyclines 78-91 matrix metallopeptidase 2 Rattus norvegicus 238-241 21843641-1 2011 INTRODUCTION: Beyond their decades of long use as broad-spectrum antibiotics, tetracyclines and their derivatives have been shown to exhibit non-antimicrobial properties including their ability to interact with matrix metalloproteinases (MMP), tissue inhibitors of MMPs, growth factors and cytokines. Tetracyclines 78-91 matrix metallopeptidase 2 Rattus norvegicus 265-269 21843641-9 2011 CMTs suppress cataractogenesis in a diabetic rat model, possibly by affecting MMPs. cmts 0-4 matrix metallopeptidase 2 Rattus norvegicus 78-82 22295524-1 2011 OBJECTIVE: To investigate the inhibitor of matrix metalloproteinase-2 (MMP-2) (2R)-2-[5-[4-[ ethyl-methylamino] phenyl [thiophene-2-sulfonylamino]-3-methylbutyric acid (TISAM) therapeutic effect on experimental autoimmune myocarditis (EAM) in Lewis rats. 2-[5-[4-[ ethyl-methylamino] phenyl [thiophene-2-sulfonylamino]-3-methylbutyric acid 83-167 matrix metallopeptidase 2 Rattus norvegicus 71-76 21856919-11 2011 Both MMP-2 and tissue inhibitors of metalloproteinase-2 as assessed by immunofluorescence were lower in the endothelium (reduction of 60%) and adventitia (reduction of 50%) of LPLN compared with LP mUA. lpln 176-180 matrix metallopeptidase 2 Rattus norvegicus 5-10 21856919-11 2011 Both MMP-2 and tissue inhibitors of metalloproteinase-2 as assessed by immunofluorescence were lower in the endothelium (reduction of 60%) and adventitia (reduction of 50%) of LPLN compared with LP mUA. leucylproline 176-178 matrix metallopeptidase 2 Rattus norvegicus 5-10 21414971-10 2011 In situ enzymatic activity of MMP in the mesangial areas was also detected in 50-week-old MCT-injected OLETF rats. oletf 103-108 matrix metallopeptidase 2 Rattus norvegicus 30-33 21353475-5 2011 The hepatic matrix metalloproteinase-2 concentration in the ethanol group was significantly higher than in the control and ethanol/vitamin groups. Ethanol 60-67 matrix metallopeptidase 2 Rattus norvegicus 12-38 21353475-5 2011 The hepatic matrix metalloproteinase-2 concentration in the ethanol group was significantly higher than in the control and ethanol/vitamin groups. Ethanol 123-130 matrix metallopeptidase 2 Rattus norvegicus 12-38 21353475-6 2011 Furthermore, the plasma homocysteine concentration at the 16th week and the hepatic matrix metalloproteinase-2 concentration showed a significant positive correlation in rats of each group. Homocysteine 24-36 matrix metallopeptidase 2 Rattus norvegicus 84-110 21434884-2 2011 We tested the hypothesis that treatment with pyrrolidine dithiocarbamate (PDTC), which interferes with NF-kappaB-induced MMPs gene transcription, could exert antihypertensive effects, prevent MMP-2 and MMP-9 up-regulation, and protect against the functional alterations and vascular remodelling of two-kidney, one clip (2K1C) hypertension. pyrrolidine dithiocarbamic acid 45-72 matrix metallopeptidase 2 Rattus norvegicus 121-125 21745137-9 2011 Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) zymography detected only the MMP-2 expression/activity for the untreated-control group (group I). Sodium Dodecyl Sulfate 0-23 matrix metallopeptidase 2 Rattus norvegicus 99-104 21745137-9 2011 Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) zymography detected only the MMP-2 expression/activity for the untreated-control group (group I). polyacrylamide 24-38 matrix metallopeptidase 2 Rattus norvegicus 99-104 21745137-9 2011 Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) zymography detected only the MMP-2 expression/activity for the untreated-control group (group I). Sodium Dodecyl Sulfate 60-63 matrix metallopeptidase 2 Rattus norvegicus 99-104 22097212-7 2011 The MMP-2 expression was determined by immunohistochemical assay (SP method). TFF2 protein, human 66-68 matrix metallopeptidase 2 Rattus norvegicus 4-9 20598359-8 2011 By double immunostaining, Ets-1-positive cells were frequently found to co-express matrix metalloproteinase-2 (MMP-2) in STZ-treated rat kidneys. Streptozocin 121-124 matrix metallopeptidase 2 Rattus norvegicus 83-109 20598359-8 2011 By double immunostaining, Ets-1-positive cells were frequently found to co-express matrix metalloproteinase-2 (MMP-2) in STZ-treated rat kidneys. Streptozocin 121-124 matrix metallopeptidase 2 Rattus norvegicus 111-116 20598359-10 2011 A positive relationship was observed between the expression of Ets-1 in glomeruli or tubulointerstitium and the expression of MMP-2 (P<0.01; P<0.01, respectively) in STZ-treated rat kidneys. Streptozocin 172-175 matrix metallopeptidase 2 Rattus norvegicus 126-131 21434884-2 2011 We tested the hypothesis that treatment with pyrrolidine dithiocarbamate (PDTC), which interferes with NF-kappaB-induced MMPs gene transcription, could exert antihypertensive effects, prevent MMP-2 and MMP-9 up-regulation, and protect against the functional alterations and vascular remodelling of two-kidney, one clip (2K1C) hypertension. pyrrolidine dithiocarbamic acid 45-72 matrix metallopeptidase 2 Rattus norvegicus 192-197 21434884-2 2011 We tested the hypothesis that treatment with pyrrolidine dithiocarbamate (PDTC), which interferes with NF-kappaB-induced MMPs gene transcription, could exert antihypertensive effects, prevent MMP-2 and MMP-9 up-regulation, and protect against the functional alterations and vascular remodelling of two-kidney, one clip (2K1C) hypertension. pyrrolidine dithiocarbamic acid 74-78 matrix metallopeptidase 2 Rattus norvegicus 121-125 21434884-2 2011 We tested the hypothesis that treatment with pyrrolidine dithiocarbamate (PDTC), which interferes with NF-kappaB-induced MMPs gene transcription, could exert antihypertensive effects, prevent MMP-2 and MMP-9 up-regulation, and protect against the functional alterations and vascular remodelling of two-kidney, one clip (2K1C) hypertension. pyrrolidine dithiocarbamic acid 74-78 matrix metallopeptidase 2 Rattus norvegicus 192-197 20371087-7 2011 VSMC released increasing levels of active MMP-2 in a dose-response fashion at IL-1beta 1-10 ng/mL (P < 0.05) while significantly increased levels of latent MMP-2 (pro-MMP-2) were attained more gradually (10 ng/mL, P < 0.05). vsmc 0-4 matrix metallopeptidase 2 Rattus norvegicus 42-47 22003940-7 2011 MMP-2 activity, usually elevated during myelination and repair, was also found to be up-regulated following LEV, while LEV exhibited no negative effects on myelination. Levetiracetam 108-111 matrix metallopeptidase 2 Rattus norvegicus 0-5 21273387-13 2011 ATRA reduced both MMP-2 and TIMP-1 activity in BAL fluid of emphysematous lungs. Tretinoin 0-4 matrix metallopeptidase 2 Rattus norvegicus 18-23 21342246-8 2011 MMP-2 activities exhibited a ~50% downregulation during gastric ulceration which were rescued by melatonin. Melatonin 97-106 matrix metallopeptidase 2 Rattus norvegicus 0-5 20371087-7 2011 VSMC released increasing levels of active MMP-2 in a dose-response fashion at IL-1beta 1-10 ng/mL (P < 0.05) while significantly increased levels of latent MMP-2 (pro-MMP-2) were attained more gradually (10 ng/mL, P < 0.05). vsmc 0-4 matrix metallopeptidase 2 Rattus norvegicus 159-164 20371087-7 2011 VSMC released increasing levels of active MMP-2 in a dose-response fashion at IL-1beta 1-10 ng/mL (P < 0.05) while significantly increased levels of latent MMP-2 (pro-MMP-2) were attained more gradually (10 ng/mL, P < 0.05). vsmc 0-4 matrix metallopeptidase 2 Rattus norvegicus 166-175 20371087-10 2011 IL-lbeta-stimulated VSMC migration was significantly attenuated by both the pan-selective MMP inhibitor GM6001 and cis-9-octadecenoyl-N-hydroxylamide, a MMP-2-selective inhibitor. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 104-110 matrix metallopeptidase 2 Rattus norvegicus 153-158 20371087-10 2011 IL-lbeta-stimulated VSMC migration was significantly attenuated by both the pan-selective MMP inhibitor GM6001 and cis-9-octadecenoyl-N-hydroxylamide, a MMP-2-selective inhibitor. cis-9-octadecenoyl-n-hydroxylamide 115-149 matrix metallopeptidase 2 Rattus norvegicus 153-158 20371087-12 2011 VSMC migration induced by IL-lbeta requires active MMP-2. vsmc 0-4 matrix metallopeptidase 2 Rattus norvegicus 51-56 21175737-3 2011 We studied here the role of matrix metalloproteinases (MMPs)-2 and -9, also called gelatinases A and B, in the degradation of the BBB in the striatal lesions induced by the systemic administration of 3-NPA to Sprague-Dawley rats. 3-nitropropionic acid 200-205 matrix metallopeptidase 2 Rattus norvegicus 83-102 21418086-12 2011 At 10 mg/kg, fluoxetine significantly inhibited MCT-induced increases in the expression of serotonin transporter (SERT) and phosphorylated extracellular signal-regulated kinase 1/2 and downregulated the expression of OPN, macrophage inflammatory protein-1beta and matrix metalloproteinase 2/tissue inhibitor of metalloproteinase 2. Fluoxetine 13-23 matrix metallopeptidase 2 Rattus norvegicus 264-330 21551278-11 2011 Active MMP-2 expression was reduced in aorta from SHRSP + DOX (0.21 +- 0.06 vs. 0.49 +- 0.13 arbitrary units; P < 0.05). Doxycycline 58-61 matrix metallopeptidase 2 Rattus norvegicus 7-12 21689423-11 2011 MMP2 activity before ischaemia was significantly reduced in the Chol+RPO group when compared to the Chol group. chol 64-68 matrix metallopeptidase 2 Rattus norvegicus 0-4 21689423-11 2011 MMP2 activity before ischaemia was significantly reduced in the Chol+RPO group when compared to the Chol group. chol 100-104 matrix metallopeptidase 2 Rattus norvegicus 0-4 21876619-0 2011 Doxycycline blocks gastric ulcer by regulating matrix metalloproteinase-2 activity and oxidative stress. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 47-73 21876619-1 2011 AIM: To examine the effect of doxycycline on the activity of matrix metalloproteinases (MMPs) and oxidative stress in gastric tissues of rats following gastric injury. Doxycycline 30-41 matrix metallopeptidase 2 Rattus norvegicus 88-92 21876619-9 2011 In contrast, the reduced MMP-2 activity in ulcerated tissues was increased by doxycycline during ulcer prevention. Doxycycline 78-89 matrix metallopeptidase 2 Rattus norvegicus 25-30 21876619-12 2011 Our results suggest a novel regulatory role of doxycycline on MMP-2 activity in addition to inhibitory action on MMP-9 and MMP-3 during prevention of gastric ulcers. Doxycycline 47-58 matrix metallopeptidase 2 Rattus norvegicus 62-67 21876619-13 2011 CONCLUSION: This is the first demonstration of dual action of doxycycline, that is, regulation of MMP activity and reduction of oxidative stress in arresting gastric injury. Doxycycline 62-73 matrix metallopeptidase 2 Rattus norvegicus 98-101 21460197-3 2011 Therefore, we hypothesize that prolonged exposure to norepinephrine (NE) and ANG II induces arteriolar inward remodeling dependent on the activation of MMPs and the production of ROS. Norepinephrine 53-67 matrix metallopeptidase 2 Rattus norvegicus 152-156 21460197-7 2011 Inhibition of ROS production prevented the activation of MMPs and the remodeling process, whereas inhibition of MMP activation did not affect ROS production. Reactive Oxygen Species 14-17 matrix metallopeptidase 2 Rattus norvegicus 57-61 21460197-8 2011 These results indicate that prolonged stimulation of resistance arterioles with NE + ANG II induces a ROS-dependent activation of MMPs necessary for the development of arteriolar inward remodeling. Reactive Oxygen Species 102-105 matrix metallopeptidase 2 Rattus norvegicus 130-134 21360312-6 2011 Moreover, diabetes-induced another type of oxidative stress markers in rats, matrix metalloproteinases, MMP-2, and MMP-9 were also normalized with doxycycline treatment in blood. Doxycycline 147-158 matrix metallopeptidase 2 Rattus norvegicus 104-109 21345984-6 2011 RESULTS: High glucose increased MMP2 and decreased connexin 43 in the mitochondria of retinal endothelial cells. Glucose 14-21 matrix metallopeptidase 2 Rattus norvegicus 32-36 21484106-5 2011 RESULTS: Gelatin zymography and Western blot showed that matrix metalloproteinase-2 expressions were inhibited by LY52 in a dose-dependent manner, and inhibitory rates of LY52 on HepG2 cells were higher than on HepG2.2.15 cells. ly52 114-118 matrix metallopeptidase 2 Rattus norvegicus 57-83 21484106-7 2011 CONCLUSIONS: These results suggested that LY52 might inhibit the invasion of hepatocellular carcinoma cells by suppressing matrix metalloproteinase-2, although the inhibitory effects of LY52 on HBV-negative cells were more obvious than that of HBV-infected cells. ly52 42-46 matrix metallopeptidase 2 Rattus norvegicus 123-149 21480801-7 2011 Moreover, CH uptake significantly decreased both proenzyme and active forms of MMP2 compared with casein and control groups (P < .05). ch 10-12 matrix metallopeptidase 2 Rattus norvegicus 79-83 21443925-6 2011 At 4h, hyperthermia increased the expression of MMP-2 and -9 and subsequent degradation of laminin and collagen IV at the level that was comparable to normothermic stroke after 24h and significantly higher than 4h of normothermic stroke (p<0.001). 4h 3-5 matrix metallopeptidase 2 Rattus norvegicus 48-60 21349324-1 2011 (2S,4R)-methyl 1-acetyl-4-(N-(4-bromophenyl)sulfamoyloxy)pyrrolidine-2-carboxylate (CIP-A5) is the N1-acetyl substituted pyrrolidine derivative which was designed against the structure of matrix metalloproteinase (MMP-2) and MMP-9. (2S,4R)-methyl-1-acetyl-4-(N-(4-bromophenyl)sulfamoyloxy)pyrrolidine-2-carboxylate 0-82 matrix metallopeptidase 2 Rattus norvegicus 214-219 21349324-1 2011 (2S,4R)-methyl 1-acetyl-4-(N-(4-bromophenyl)sulfamoyloxy)pyrrolidine-2-carboxylate (CIP-A5) is the N1-acetyl substituted pyrrolidine derivative which was designed against the structure of matrix metalloproteinase (MMP-2) and MMP-9. cip-a5 84-90 matrix metallopeptidase 2 Rattus norvegicus 214-219 21349324-1 2011 (2S,4R)-methyl 1-acetyl-4-(N-(4-bromophenyl)sulfamoyloxy)pyrrolidine-2-carboxylate (CIP-A5) is the N1-acetyl substituted pyrrolidine derivative which was designed against the structure of matrix metalloproteinase (MMP-2) and MMP-9. n1-acetyl substituted pyrrolidine 99-132 matrix metallopeptidase 2 Rattus norvegicus 214-219 21507637-3 2011 We identify a hydroxamate tetrazole 4e that spares MMP-1 and -14, shows >400-fold selectivity versus MMP-8 and >600-fold selectivity versus MMP-2, and has a 4.8 h half-life in rats. hydroxamate tetrazole 14-35 matrix metallopeptidase 2 Rattus norvegicus 146-151 21447487-4 2011 We investigated whether propofol affected the expression of MMPs and subsequent cell migration and invasion and the signalling pathways involved in primary rat cardiac fibroblasts undergoing hypoxia and reoxygenation. Propofol 24-32 matrix metallopeptidase 2 Rattus norvegicus 60-64 21392796-10 2011 The expression of both MMP-2 and MMP-9 and the destruction of elastic fibers in aortic tissues were significantly decreased by cilostazol treatment (P < 0.05), probably through the suppression of NF-kappaB activation (P < 0.01). Cilostazol 127-137 matrix metallopeptidase 2 Rattus norvegicus 23-28 21354273-0 2011 Matrix metalloproteinases 2 and 9 in the cochlea: expression and activity after aminoglycoside exposition. Aminoglycosides 80-94 matrix metallopeptidase 2 Rattus norvegicus 0-33 21354273-6 2011 We focused on the localization and function of MMP-2 and MMP-9 in the cochlea, by determining their expression and activity under normal conditions and after cochlear damage via aminoglycoside exposition. Aminoglycosides 178-192 matrix metallopeptidase 2 Rattus norvegicus 47-52 21354273-13 2011 Organs of Corti treated with gentamicin for 24 h showed an upregulation of MMP-2 and MMP-9 proteins, but did not show a significant upregulation of mRNA expression 3, 6, 12, 24, and 36 h after gentamicin exposure. Gentamicins 29-39 matrix metallopeptidase 2 Rattus norvegicus 75-80 20847042-8 2011 CMC significantly protected the antioxidant activity in both the pulmonary and systemic levels, reduced pathologic apoptosis, and inhibited MMP-2 and MMP-9 activities in the lungs of rats with CSE-induced emphysema. cmc 0-3 matrix metallopeptidase 2 Rattus norvegicus 140-145 21176109-0 2011 Doxycycline dose-dependently inhibits MMP-2-mediated vascular changes in 2K1C hypertension. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 38-43 21176109-2 2011 While these alterations may be blunted by doxycycline, a non-selective MMPs inhibitor, no previous study has examined the effects of different doses of doxycycline on these alterations. Doxycycline 42-53 matrix metallopeptidase 2 Rattus norvegicus 71-75 21176109-10 2011 In conclusion, our results suggest that relatively lower doses of doxycycline do not attenuate the vascular alterations found in the 2K1C hypertension model, and only the highest dose of doxycycline affects MMPs and vascular structure. Doxycycline 187-198 matrix metallopeptidase 2 Rattus norvegicus 207-211 21176109-11 2011 Our results support the idea that the effects of doxycycline on MMP-2 and vascular structure are pressure independent. Doxycycline 49-60 matrix metallopeptidase 2 Rattus norvegicus 64-69 21447487-9 2011 Subsequent activation of MMPs resulted in increased cell migration, invasion, and wound-healing activity under hypoxia-reoxygenation, which was decreased by LY294002 (AKT inhibitor) and U0126 (ERK inhibitor) in rat cardiac fibroblasts. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 157-165 matrix metallopeptidase 2 Rattus norvegicus 25-29 21447487-9 2011 Subsequent activation of MMPs resulted in increased cell migration, invasion, and wound-healing activity under hypoxia-reoxygenation, which was decreased by LY294002 (AKT inhibitor) and U0126 (ERK inhibitor) in rat cardiac fibroblasts. U 0126 186-191 matrix metallopeptidase 2 Rattus norvegicus 25-29 21447487-11 2011 CONCLUSIONS: Propofol affected the expression of MMPs and TIMPs and subsequently induced cell migration and invasive ability, through activation of the ERK and AKT signalling pathway in hypoxia-reoxygenated rat cardiac fibroblasts. Propofol 13-21 matrix metallopeptidase 2 Rattus norvegicus 49-53 20661683-2 2011 The aim of the present study was to investigate potential involvement of selected MMPs in the pathogenesis of neuronal apoptosis induced by the NMDA antagonist MK-801 (dizocilpine) or the GABA(A) agonist phenobarbital in infant rats, transgenic rats overexpressing MMP-9 and MMP-9 knockout mice. gamma-Aminobutyric Acid 188-192 matrix metallopeptidase 2 Rattus norvegicus 82-86 20080260-15 2011 CONCLUSION: Doxycycline had protective effects on I/R injury by decreasing apoptosis via reducing the level of pro-inflammatory cytokines, increasing the level of TIMP-1, and inhibiting the activity of MMP-2. Doxycycline 12-23 matrix metallopeptidase 2 Rattus norvegicus 202-207 20661683-2 2011 The aim of the present study was to investigate potential involvement of selected MMPs in the pathogenesis of neuronal apoptosis induced by the NMDA antagonist MK-801 (dizocilpine) or the GABA(A) agonist phenobarbital in infant rats, transgenic rats overexpressing MMP-9 and MMP-9 knockout mice. Phenobarbital 204-217 matrix metallopeptidase 2 Rattus norvegicus 82-86 20661683-2 2011 The aim of the present study was to investigate potential involvement of selected MMPs in the pathogenesis of neuronal apoptosis induced by the NMDA antagonist MK-801 (dizocilpine) or the GABA(A) agonist phenobarbital in infant rats, transgenic rats overexpressing MMP-9 and MMP-9 knockout mice. N-Methylaspartate 144-148 matrix metallopeptidase 2 Rattus norvegicus 82-86 21505995-0 2011 Retinoic acid diminished the expression of MMP-2 in hyperoxia-exposed premature rat lung fibroblasts through regulating mitogen-activated protein kinases. Tretinoin 0-13 matrix metallopeptidase 2 Rattus norvegicus 43-48 20661683-2 2011 The aim of the present study was to investigate potential involvement of selected MMPs in the pathogenesis of neuronal apoptosis induced by the NMDA antagonist MK-801 (dizocilpine) or the GABA(A) agonist phenobarbital in infant rats, transgenic rats overexpressing MMP-9 and MMP-9 knockout mice. Dizocilpine Maleate 160-166 matrix metallopeptidase 2 Rattus norvegicus 82-86 20661683-2 2011 The aim of the present study was to investigate potential involvement of selected MMPs in the pathogenesis of neuronal apoptosis induced by the NMDA antagonist MK-801 (dizocilpine) or the GABA(A) agonist phenobarbital in infant rats, transgenic rats overexpressing MMP-9 and MMP-9 knockout mice. Dizocilpine Maleate 168-179 matrix metallopeptidase 2 Rattus norvegicus 82-86 21518085-5 2011 Moreover, an increased MMP-2 level was observed in a rat model with pulmonary inflammation and fibrosis induced by bleomycin-A5. bleomycetin 115-127 matrix metallopeptidase 2 Rattus norvegicus 23-28 21382440-9 2011 Expression of VEGF, iNOS, MMP-2, and MMP-9 in aneurysmal walls was also increased by methionine treatment. Methionine 85-95 matrix metallopeptidase 2 Rattus norvegicus 26-31 21229381-5 2011 Utilizing immuno-spin trapping in protein fractions that were rich in iron, we tentatively indentified protein carrier(s) of ferrous iron by MALDI-TOF MS. One of the identified proteins was the metalloproteinase (MMP) inhibitor, TIMP-2. Iron 133-137 matrix metallopeptidase 2 Rattus norvegicus 213-216 19876598-6 2011 DMH-induced rats exhibited elevated expressions of Nuclear factor kappa B-p65 (NF-kappaB-p65), Cyclooxygenase-2 (COX-2), Matrixmetallo proteinases (MMP) 2/9, Proliferating cell nuclear antigen (PCNA), and Extracellular signal-regulated kinase-2 (ERK-2) as confirmed by immunofluorescence. Dimethylhydrazines 0-3 matrix metallopeptidase 2 Rattus norvegicus 121-156 19876598-7 2011 Further, Westernblot analysis of MMPs-2/9, ERK-2 and Protein kinase B (Akt) revealed increased expressions of these proteins in DMH-induced groups of rats. Dimethylhydrazines 128-131 matrix metallopeptidase 2 Rattus norvegicus 33-41 19876598-10 2011 In conclusion, astaxanthin exhibits anti-inflammatory and anti-cancer effects by inducing apoptosis in DMH-induced rat colon carcinogenesis by modulating the expressions of NFkB, COX-2, MMPs-2/9, Akt and ERK-2. astaxanthine 15-26 matrix metallopeptidase 2 Rattus norvegicus 186-194 21505995-1 2011 This study examined the effects of retinoic acid (RA), PD98059, SP600125 and SB203580 on the hyperoxia-induced expression and regulation of matrix metalloproteinase-2 (MMP-2) and metalloproteinase-2 (TIMP-2) in premature rat lung fibroblasts (LFs). Tretinoin 35-48 matrix metallopeptidase 2 Rattus norvegicus 140-166 21401606-12 2011 CONCLUSIONS: Icariin ameliorates left ventricular dysfunction and cardiac remodelling through down-regulating matrix metalloproteinase-2 and 9 activity and myocardial apoptosis in rats with congestive heart failure. icariin 13-20 matrix metallopeptidase 2 Rattus norvegicus 110-136 21505995-1 2011 This study examined the effects of retinoic acid (RA), PD98059, SP600125 and SB203580 on the hyperoxia-induced expression and regulation of matrix metalloproteinase-2 (MMP-2) and metalloproteinase-2 (TIMP-2) in premature rat lung fibroblasts (LFs). 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 55-62 matrix metallopeptidase 2 Rattus norvegicus 140-166 21505995-1 2011 This study examined the effects of retinoic acid (RA), PD98059, SP600125 and SB203580 on the hyperoxia-induced expression and regulation of matrix metalloproteinase-2 (MMP-2) and metalloproteinase-2 (TIMP-2) in premature rat lung fibroblasts (LFs). pyrazolanthrone 64-72 matrix metallopeptidase 2 Rattus norvegicus 140-166 21505995-1 2011 This study examined the effects of retinoic acid (RA), PD98059, SP600125 and SB203580 on the hyperoxia-induced expression and regulation of matrix metalloproteinase-2 (MMP-2) and metalloproteinase-2 (TIMP-2) in premature rat lung fibroblasts (LFs). SB 203580 77-85 matrix metallopeptidase 2 Rattus norvegicus 140-166 21505995-1 2011 This study examined the effects of retinoic acid (RA), PD98059, SP600125 and SB203580 on the hyperoxia-induced expression and regulation of matrix metalloproteinase-2 (MMP-2) and metalloproteinase-2 (TIMP-2) in premature rat lung fibroblasts (LFs). SB 203580 77-85 matrix metallopeptidase 2 Rattus norvegicus 168-173 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 29-36 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). pyrazolanthrone 38-46 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). SB 203580 51-59 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). pyrazolanthrone 234-242 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). SB 203580 247-255 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-6 2011 The results showed that: (1) PD98059, SP600125 and SB203580 significantly inhibited p-ERK1/2, p-JNK1/2 and p-p38 respectively in LFs; (2) The expression of MMP-2 mRNA in LFs exposed to hyperoxia was decreased after treatment with RA, SP600125 and SB203580 respectively (P<0.01 or 0.05), but did not change after treatment with PD98059 (P>0.05). 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 330-337 matrix metallopeptidase 2 Rattus norvegicus 156-161 21505995-8 2011 SB203580 inhibited the expression of pro- and active MMP-2 either in room air or under hyperoxia (P<0.01). SB 203580 0-8 matrix metallopeptidase 2 Rattus norvegicus 53-58 21362404-9 2011 Matrix metalloproteinase-2 (MMP-2) activity and vascular endothelial growth factor (VEGF) expression decreased in rats bearing W256 treated with 10 mg/kg quercetin when compared with CTR. Quercetin 154-163 matrix metallopeptidase 2 Rattus norvegicus 0-26 20544295-2 2011 PROCEDURES: We study the combination of MMP(2)-targeted microbubbles (TMB(2)) and control microbubbles with myocardium in 1 week post-I/R rats. 3,3',5,5'-tetramethylbenzidine 70-73 matrix metallopeptidase 2 Rattus norvegicus 40-46 20544295-6 2011 CONCLUSIONS: A targeted ultrasound contrast imaging approach that employs novel TMB(2) has the potential to provide a less-invasive, higher-resolution technique for in vivo localization of MMP(2) activation and tracking of MMP-mediated post-I/R remodeling. 3,3',5,5'-tetramethylbenzidine 80-83 matrix metallopeptidase 2 Rattus norvegicus 189-195 20544295-6 2011 CONCLUSIONS: A targeted ultrasound contrast imaging approach that employs novel TMB(2) has the potential to provide a less-invasive, higher-resolution technique for in vivo localization of MMP(2) activation and tracking of MMP-mediated post-I/R remodeling. 3,3',5,5'-tetramethylbenzidine 80-83 matrix metallopeptidase 2 Rattus norvegicus 189-192 21362404-9 2011 Matrix metalloproteinase-2 (MMP-2) activity and vascular endothelial growth factor (VEGF) expression decreased in rats bearing W256 treated with 10 mg/kg quercetin when compared with CTR. Quercetin 154-163 matrix metallopeptidase 2 Rattus norvegicus 28-33 21362404-10 2011 Thus, the inhibition of tumor growth, survival increase, decrease of MMP-2 and VEGF levels and reduction of cachexia in animals treated with quercetin strongly support the anticancer function of this flavonoid. Flavonoids 200-209 matrix metallopeptidase 2 Rattus norvegicus 69-74 21172400-9 2011 Betulin and betulinic acid, also decreased ethanol-induced activity of MMP-2. betulin 0-7 matrix metallopeptidase 2 Rattus norvegicus 71-76 21207142-1 2011 We investigated whether polyphenols modulate the expression and activity of the enzymes gelatinases A (MMP-2) and B (MMP-9), involved in the pathogenesis of multiple sclerosis (MS). Polyphenols 24-35 matrix metallopeptidase 2 Rattus norvegicus 103-115 21207142-3 2011 As assessed by zymography and RT-PCR, RSV and Oliplus, but not QRC and GTE, dose-dependently inhibited the LPS-induced levels and mRNA expression of MMP-2 and MMP-9. Resveratrol 38-41 matrix metallopeptidase 2 Rattus norvegicus 149-154 21207142-6 2011 Our results indicate that the flavonoids and non-flavonoids tested exert their inhibitory effect on MMPs, displaying different mechanisms of action, possibly related to their structure. Flavonoids 30-40 matrix metallopeptidase 2 Rattus norvegicus 100-104 21207142-6 2011 Our results indicate that the flavonoids and non-flavonoids tested exert their inhibitory effect on MMPs, displaying different mechanisms of action, possibly related to their structure. Flavonoids 49-59 matrix metallopeptidase 2 Rattus norvegicus 100-104 21468558-3 2011 In this study, we examined the sequential expression of MMP-2, MMP-9 and TIMP-1 in a rat model of pulmonary fibrosis induced by PQ. Paraquat 128-130 matrix metallopeptidase 2 Rattus norvegicus 56-61 21468558-9 2011 In conclusion, unbalanced MMP/TIMP-1 expression and excessive gelatinolytic activity contribute to PQ-induced pulmonary fibrosis. Paraquat 99-101 matrix metallopeptidase 2 Rattus norvegicus 26-29 21172400-9 2011 Betulin and betulinic acid, also decreased ethanol-induced activity of MMP-2. betulinic acid 12-26 matrix metallopeptidase 2 Rattus norvegicus 71-76 21172400-9 2011 Betulin and betulinic acid, also decreased ethanol-induced activity of MMP-2. Ethanol 43-50 matrix metallopeptidase 2 Rattus norvegicus 71-76 20971083-2 2011 In the present study we examined a novel MMP-inhibitor (Ro 28-2653) with high selectivity for MMP2, MMP9 and membrane type 1-MMP in an acute stroke model comparing two different treatment regimens. Ro 28-2653 56-66 matrix metallopeptidase 2 Rattus norvegicus 94-98 21220710-8 2011 Furthermore, MMP-2 and MMP-9 activities in SHR plasma were significantly reduced ( 41%) by pyrrolidine dithiocarbamate treatment. pyrrolidine dithiocarbamic acid 92-119 matrix metallopeptidase 2 Rattus norvegicus 13-18 21347430-4 2011 Exposure of VSMC isolated from 8-mo-old rats (young) to MCP-1 effects, via CCR-2 signaling, both an increase in TGF-beta1 activity, up to levels of untreated VSMC from 30-mo-old (old) rats, and a concurrent increase in MMP-2 activation. vsmc 12-16 matrix metallopeptidase 2 Rattus norvegicus 219-224 21347430-5 2011 Furthermore, exposure of young VSMC to TGF-beta1 increases levels of MCP-1, and MMP-2 activation, to levels of untreated VSMC from old rats. vsmc 31-35 matrix metallopeptidase 2 Rattus norvegicus 80-85 21347430-6 2011 This autocatalytic signaling loop that enhances collagen production and invasiveness of VSMC is effectively suppressed by si-MCP-1, a CCR2 antagonist, or MMP-2 inhibition. vsmc 88-92 matrix metallopeptidase 2 Rattus norvegicus 154-159 21430993-0 2011 Gene expressions of nitric oxide synthase and matrix metalloproteinase-2 in monocrotaline-induced pulmonary hypertension in rats after bosentan treatment. Bosentan 135-143 matrix metallopeptidase 2 Rattus norvegicus 46-72 21430993-2 2011 NO synthesis is catalyzed by endothelial nitric oxide synthase (eNOS), and NO can also produce peroxynitrite, which activates matrix metalloproteinases (MMPs). Peroxynitrous Acid 95-108 matrix metallopeptidase 2 Rattus norvegicus 153-157 21430993-3 2011 The purpose of this study was to determine the gene expression of eNOS and MMP-2 in the lungs of a rat model of pulmonary hypertension after bosentan treatment. Bosentan 141-149 matrix metallopeptidase 2 Rattus norvegicus 75-80 21430993-9 2011 Following bosentan treatment to reduce pulmonary hypertension, the expression levels of MMP-2 gene were significantly decreased on day 7 and 28. Bosentan 10-18 matrix metallopeptidase 2 Rattus norvegicus 88-93 21430993-10 2011 eNOS and tissue inhibitor of MMPs genes were also significantly decreased on day 28 after bosentan treatment. Bosentan 90-98 matrix metallopeptidase 2 Rattus norvegicus 29-33 21791917-9 2011 High phosphorus increased MMP-2 and MMP-9 expressions in VSMC from normal rats but not from CKD rats. Phosphorus 5-15 matrix metallopeptidase 2 Rattus norvegicus 26-31 22073820-13 2011 Levels of MMP-2 were negatively correlated with net ultrafiltration, effluent protein levels, and end (1-hour)-to-initial dialysate concentration ratio of glucose. Glucose 155-162 matrix metallopeptidase 2 Rattus norvegicus 10-15 20683769-3 2011 Therefore, this study aimed to investigate the regulation and function of MMP-2 and its major activator membrane type 1-matrix metalloproteinase (MT1-MMP) as well its inhibitor TIMP-1 in SN under conditions of HFES. hfes 210-214 matrix metallopeptidase 2 Rattus norvegicus 74-79 20683769-6 2011 HFES increased MMP-2 and MT1-MMP mRNA and protein expression, whereas TIMP-1 expression remained unchanged. hfes 0-4 matrix metallopeptidase 2 Rattus norvegicus 15-20 20683769-7 2011 Under conditions of HFES, we observed a shift from pro- to active-MMP-2 indicating an increase in MMP-2 enzyme activity. hfes 20-24 matrix metallopeptidase 2 Rattus norvegicus 66-71 20683769-7 2011 Under conditions of HFES, we observed a shift from pro- to active-MMP-2 indicating an increase in MMP-2 enzyme activity. hfes 20-24 matrix metallopeptidase 2 Rattus norvegicus 98-103 20683769-8 2011 Specific pharmacological MMP-2 inhibition contributed to an increase in pro-NGF amount in the cell culture supernatant and significantly reduced HFES-induced neurite outgrowth. hfes 145-149 matrix metallopeptidase 2 Rattus norvegicus 25-30 21471716-0 2011 Sesamol attenuates isoproterenol-induced acute myocardial infarction via inhibition of matrix metalloproteinase-2 and -9 expression in rats. sesamol 0-7 matrix metallopeptidase 2 Rattus norvegicus 87-120 20683769-9 2011 Losartan abolished HFES-induced nerve sprouting in a significant manner by preventing HFES-induced NGF, MMP-2, and MT1-MMP up-regulation. Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 104-109 21471716-2 2011 We tested the hypothesis that sesamol"s protection against myocardial infarction is associated with the inhibition of matrix metalloproteinase (MMP)-2 and MMP-9. sesamol 30-37 matrix metallopeptidase 2 Rattus norvegicus 118-150 20683769-9 2011 Losartan abolished HFES-induced nerve sprouting in a significant manner by preventing HFES-induced NGF, MMP-2, and MT1-MMP up-regulation. hfes 19-23 matrix metallopeptidase 2 Rattus norvegicus 104-109 21471716-8 2011 CONCLUSIONS: Sesamol effectively prevented myocardial infarction, at least in part, by controlling proteolytic activities and the expression of MMP-2 and -9 in isoproterenol-treated rats. sesamol 13-20 matrix metallopeptidase 2 Rattus norvegicus 144-156 20683769-9 2011 Losartan abolished HFES-induced nerve sprouting in a significant manner by preventing HFES-induced NGF, MMP-2, and MT1-MMP up-regulation. hfes 86-90 matrix metallopeptidase 2 Rattus norvegicus 104-109 21471716-8 2011 CONCLUSIONS: Sesamol effectively prevented myocardial infarction, at least in part, by controlling proteolytic activities and the expression of MMP-2 and -9 in isoproterenol-treated rats. Isoproterenol 160-173 matrix metallopeptidase 2 Rattus norvegicus 144-156 22553604-9 2011 The level of MMP-2 was significantly down-regulated (P=0.013) at the mRNA level in the AMT group, while the expression of EGF was significantly higher (P=0.022) compared with controls. amt 87-90 matrix metallopeptidase 2 Rattus norvegicus 13-18 21814480-2 2011 We aimed to investigate the influences of diosgenin administration upon the MMP-2 and -9 activity and expression and reproductive hormones of ovariectomized (OVX) rats, a model of menopausal status. Diosgenin 42-51 matrix metallopeptidase 2 Rattus norvegicus 76-88 21814480-11 2011 Diosgenin administration can partially reverse the effects of OVX upon MMP functions and hormone status. Diosgenin 0-9 matrix metallopeptidase 2 Rattus norvegicus 71-74 21731450-0 2011 Reactive oxygen species released from hypoxic hepatocytes regulates MMP-2 expression in hepatic stellate cells. Reactive Oxygen Species 0-23 matrix metallopeptidase 2 Rattus norvegicus 68-73 21731450-4 2011 We speculated that cell-cell interaction is involved in the regulation of MMP-2 expression and activity at low oxygen level in vivo. Oxygen 111-117 matrix metallopeptidase 2 Rattus norvegicus 74-79 21731450-7 2011 Reduced glutathione neutralized ROS released from hypoxic hepatocytes, leading to reduced MMP-2 expression in HSC-T6 cells. Glutathione 8-19 matrix metallopeptidase 2 Rattus norvegicus 90-95 21731450-9 2011 Taken together, our data suggest that ROS is an important factor released by hypoxic hepatocytes to regulate MMP-2 expression in HSCs, and NF-kappaB signaling is crucially involved in ROS-induced MMP-2 expression in HSCs. Reactive Oxygen Species 38-41 matrix metallopeptidase 2 Rattus norvegicus 109-114 21731450-9 2011 Taken together, our data suggest that ROS is an important factor released by hypoxic hepatocytes to regulate MMP-2 expression in HSCs, and NF-kappaB signaling is crucially involved in ROS-induced MMP-2 expression in HSCs. Reactive Oxygen Species 38-41 matrix metallopeptidase 2 Rattus norvegicus 196-201 21731450-9 2011 Taken together, our data suggest that ROS is an important factor released by hypoxic hepatocytes to regulate MMP-2 expression in HSCs, and NF-kappaB signaling is crucially involved in ROS-induced MMP-2 expression in HSCs. Reactive Oxygen Species 184-187 matrix metallopeptidase 2 Rattus norvegicus 109-114 21731450-9 2011 Taken together, our data suggest that ROS is an important factor released by hypoxic hepatocytes to regulate MMP-2 expression in HSCs, and NF-kappaB signaling is crucially involved in ROS-induced MMP-2 expression in HSCs. Reactive Oxygen Species 184-187 matrix metallopeptidase 2 Rattus norvegicus 196-201 21649529-8 2011 Excessive activation of MMP-2 in the heart could be partially suppressed by doxycycline. Doxycycline 76-87 matrix metallopeptidase 2 Rattus norvegicus 24-29 21649529-10 2011 Moreover, doxycycline could downregulate MMP-2 and TIMP-1 expression both at mRNA and protein levels, and TIMP-2 represented opposite expression pattern. Doxycycline 10-21 matrix metallopeptidase 2 Rattus norvegicus 41-46 21649529-12 2011 Interrupted cardiac MMP-2/TIMP-2 balance by doxycycline may play a role in this process. Doxycycline 44-55 matrix metallopeptidase 2 Rattus norvegicus 20-25 21058008-0 2011 Comparative study on antioxidant effects and vascular matrix metalloproteinase-2 downregulation by dihydropyridines in renovascular hypertension. Dihydropyridines 99-115 matrix metallopeptidase 2 Rattus norvegicus 54-80 21372438-0 2011 Investigation of gene expression of MMP-2 and TIMP-2 mRNA in rat lung in inhaled nickel oxide and titanium dioxide nanoparticles. nickel monoxide 81-93 matrix metallopeptidase 2 Rattus norvegicus 36-41 21372438-0 2011 Investigation of gene expression of MMP-2 and TIMP-2 mRNA in rat lung in inhaled nickel oxide and titanium dioxide nanoparticles. titanium dioxide 98-114 matrix metallopeptidase 2 Rattus norvegicus 36-41 20602464-0 2011 Ciprofloxacin up-regulates tendon cells to express matrix metalloproteinase-2 with degradation of type I collagen. Ciprofloxacin 0-13 matrix metallopeptidase 2 Rattus norvegicus 51-77 20602464-2 2011 This study was designed to investigate the effect of ciprofloxacin on expressions of matrix metalloproteinases (MMP)-2 and -9, tissue inhibitors of metalloproteinase (TIMP)-1 and -2 as well as type I collagen in tendon cells. Ciprofloxacin 53-66 matrix metallopeptidase 2 Rattus norvegicus 85-125 20602464-7 2011 Immunohistochemical staining for MMP-2 in ciprofloxacin-treated tendon explants was performed. Ciprofloxacin 42-55 matrix metallopeptidase 2 Rattus norvegicus 33-38 20602464-9 2011 The results revealed that ciprofloxacin up-regulated the expression of MMP-2 in tendon cells at the mRNA and protein levels. Ciprofloxacin 26-39 matrix metallopeptidase 2 Rattus norvegicus 71-76 20602464-10 2011 Immunohistochemistry also confirmed the increased expressions of MMP-2 in ciprofloxacin-treated tendon explants. Ciprofloxacin 74-87 matrix metallopeptidase 2 Rattus norvegicus 65-70 20602464-13 2011 In conclusion, ciprofloxacin up-regulates the expressions of MMP-2 in tendon cells and thus degraded type I collagen. Ciprofloxacin 15-28 matrix metallopeptidase 2 Rattus norvegicus 61-66 21058008-2 2011 While previous work showed that lercanidipine, a third-generation dihydropyridine calcium channel blocker (CCB), attenuated the oxidative stress and increased MMP-2 expression/activity in two-kidney, one-clip (2K1C) hypertension, no previous study has examined whether first- or second-generation dihydropyridines produce similar effects. lercanidipine 32-45 matrix metallopeptidase 2 Rattus norvegicus 159-164 21058008-11 2011 All dihydropyridines attenuated the increases in aortic MMP-2 levels and activity associated with 2K1C hypertension. Dihydropyridines 4-20 matrix metallopeptidase 2 Rattus norvegicus 56-61 21849805-6 2011 Furthermore, MMP-2 and MMP-9 enzymatic activity was markedly enhanced in the liver of RAdMMP-13 injected rats. radmmp-13 86-95 matrix metallopeptidase 2 Rattus norvegicus 13-18 21355315-2 2011 METHODS: After isolation and identification of MSCs, the effect of MSCs supernatant liquid (MSCs-SL) on the proliferation of RSC-364 and the expression of COX-2, MMP-2 were detected by MTT assay and RT-PCR. monooxyethylene trimethylolpropane tristearate 185-188 matrix metallopeptidase 2 Rattus norvegicus 162-167 21219209-3 2011 The objective of present study was to inhibit MMP-2 and MMP-9 by combination of minocycline and aspirin to treat diabetic nephropathy. Minocycline 80-91 matrix metallopeptidase 2 Rattus norvegicus 46-51 21219209-3 2011 The objective of present study was to inhibit MMP-2 and MMP-9 by combination of minocycline and aspirin to treat diabetic nephropathy. Aspirin 96-103 matrix metallopeptidase 2 Rattus norvegicus 46-51 22180353-12 2011 Betulin decreased the acetaldehyde-induced activity of MMP-2, but butein and betulinic acid did not. betulin 0-7 matrix metallopeptidase 2 Rattus norvegicus 55-60 22180353-12 2011 Betulin decreased the acetaldehyde-induced activity of MMP-2, but butein and betulinic acid did not. Acetaldehyde 22-34 matrix metallopeptidase 2 Rattus norvegicus 55-60 20213226-2 2010 In the present study, we have targeted MMP-2 and MMP-9 overactivation in diabetic neuropathy using a known MMP-2 and MMP-9 inhibitor, minocycline, with a non-selective COX inhibitor, aspirin. Minocycline 134-145 matrix metallopeptidase 2 Rattus norvegicus 39-44 20638255-7 2010 Val and Tsn-H exerted comparable suppressive effects on the gene expression of MMP-9 and TIMP-1, while Val decreased the MMP-2 mRNA level without affecting the transcript levels of TIMP-2. Valsartan 103-106 matrix metallopeptidase 2 Rattus norvegicus 121-126 21181362-7 2010 The results showed that ATRA inhibited HSCs proliferation and diminished the mRNA expression of collagen genes [procollagen alpha1 (I), procollagen alpha1 (III)] and profibrogenic genes (TGF-beta(1), CTGF, MMP-2, TIMP-1, TIMP-2, PAI-1), and significantly stimulated the mRNA expression of MMP-3 and MMP-13 in HSCs by suppressing the mRNA expression of JNK and AP-1. Tretinoin 24-28 matrix metallopeptidase 2 Rattus norvegicus 206-211 21181362-8 2010 These findings suggested that ATRA could inhibit proliferation and collagen production of HSCs via the suppression of active protein-1 and c-Jun N-terminal kinase signal, then decrease the mRNAs expression of profibrogenic genes (TGF-beta(1), CTGF, MMP-2, TIMP-1, TIMP-2, PAI-1), and significantly induce the mRNA expression of MMP-3 and MMP-13. Tretinoin 30-34 matrix metallopeptidase 2 Rattus norvegicus 249-254 21058936-2 2011 Based upon reports that topical fluoroquinolones (FQs) may cause perforations during corneal healing by modulating MMPs, this study evaluated the comparative effects of commercially available FQs eye drops on the expression of MMP-2 and MMP-9 in the cornea after ethanol injury. Fluoroquinolones 32-48 matrix metallopeptidase 2 Rattus norvegicus 115-119 21058936-2 2011 Based upon reports that topical fluoroquinolones (FQs) may cause perforations during corneal healing by modulating MMPs, this study evaluated the comparative effects of commercially available FQs eye drops on the expression of MMP-2 and MMP-9 in the cornea after ethanol injury. Fluoroquinolones 50-53 matrix metallopeptidase 2 Rattus norvegicus 115-119 21058936-9 2011 Among the studied FQs, ciprofloxacin was observed to exhibit maximal induction of MMP-2 and MMP-9, whereas lomefloxacin exhibited an equivocal effect on both MMP-2 and MMP-9 expression. Ciprofloxacin 23-36 matrix metallopeptidase 2 Rattus norvegicus 82-87 21058936-9 2011 Among the studied FQs, ciprofloxacin was observed to exhibit maximal induction of MMP-2 and MMP-9, whereas lomefloxacin exhibited an equivocal effect on both MMP-2 and MMP-9 expression. lomefloxacin 107-119 matrix metallopeptidase 2 Rattus norvegicus 158-163 21054405-7 2010 Furthermore, telmisartan also downregulated matrix metalloproteinase-2 expression, attenuated the increased protein expression of p22(phox), p47(phox), p67(phox), nuclear factor kappa B and Nox4 in heart tissue, and reduced oxidative-stress-induced DNA damage, which was evaluated by the expression of 8-hydroxydeoxyguanosine. Telmisartan 13-24 matrix metallopeptidase 2 Rattus norvegicus 44-70 20059586-9 2010 MMP-2 and MMP-9 immunostaining presented intense reaction in CS and TR groups, mainly in the epithelial and endothelial cells. Cesium 61-63 matrix metallopeptidase 2 Rattus norvegicus 0-5 20615646-9 2010 Ex vivo experiments showed that mRNA expressions of TNF-alpha, MMP-2, and MMP-9 in the cultured AAA tissue were decreased by exogenous TG2, whereas were increased by cystamine. Cystamine 166-175 matrix metallopeptidase 2 Rattus norvegicus 63-68 20435582-9 2010 Guggulsterone also prevented the expression of MMP-2, iNOS, and Cox-2 proteins and of IkappaB and NF-kappaB in various eye tissues. pregna-4,17-diene-3,16-dione 0-13 matrix metallopeptidase 2 Rattus norvegicus 47-52 20939987-0 2010 Effects of Chinese herbal medicine Shenlong Decoction on mRNA expressions of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-1 in lung tissue of rats with pulmonary fibrosis induced by bleomycin. Bleomycin 206-215 matrix metallopeptidase 2 Rattus norvegicus 77-103 20939987-1 2010 OBJECTIVE: To observe the expressions of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in rats with pulmonary fibrosis (PF) induced by bleomycin, and to explore the mechanisms of Shenlong Decoction in preventing and treating PF. Bleomycin 177-186 matrix metallopeptidase 2 Rattus norvegicus 41-67 20939987-1 2010 OBJECTIVE: To observe the expressions of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in rats with pulmonary fibrosis (PF) induced by bleomycin, and to explore the mechanisms of Shenlong Decoction in preventing and treating PF. Bleomycin 177-186 matrix metallopeptidase 2 Rattus norvegicus 69-74 20581100-7 2010 MMP-2 expression was examined by quantitative real-time PCR and zymography in doxycycline-treated ELT3 cells and tumor growth using angiomyolipoma-derived tumor xenografts in nude mice. Doxycycline 78-89 matrix metallopeptidase 2 Rattus norvegicus 0-5 20492444-3 2010 Herein, we investigated the effect of melatonin on MMP-2-mediated angiogenesis during gastroprotection. Melatonin 38-47 matrix metallopeptidase 2 Rattus norvegicus 51-56 19954952-2 2010 HYPOTHESIS: Matrix metalloproteinase-2 (MMP-2) is activated by ROS and contributes to the acute loss of myocardial contractile function by targeting and cleaving susceptible proteins including troponin I (TnI) and alpha-actinin. Reactive Oxygen Species 63-66 matrix metallopeptidase 2 Rattus norvegicus 12-38 19954952-2 2010 HYPOTHESIS: Matrix metalloproteinase-2 (MMP-2) is activated by ROS and contributes to the acute loss of myocardial contractile function by targeting and cleaving susceptible proteins including troponin I (TnI) and alpha-actinin. Reactive Oxygen Species 63-66 matrix metallopeptidase 2 Rattus norvegicus 40-45 20492444-5 2010 Melatonin augmented angiogenesis that was associated with amelioration of MMP-2 expression and activity and, upregulation of vascular endothelial growth factor (VEGF) in rat cornea. Melatonin 0-9 matrix metallopeptidase 2 Rattus norvegicus 74-79 20492444-6 2010 Melatonin prevented gastric lesions by promoting angiogenesis via upregulation of VEGF followed by over-expression of MMP-2. Melatonin 0-9 matrix metallopeptidase 2 Rattus norvegicus 118-123 20492444-9 2010 Our data demonstrated that melatonin exerts angiogenesis through MMP-2 and VEGF over-expression during protection and healing of gastric ulcers. Melatonin 27-36 matrix metallopeptidase 2 Rattus norvegicus 65-70 20333532-8 2010 Administration of IND alone significantly decreased MMP-2 expression at the ulcer margin; on the other hand, subsequent administration of LPZ increased the MMP-2 expression. Indomethacin 18-21 matrix metallopeptidase 2 Rattus norvegicus 52-57 20821936-5 2010 In the DM group, compared with the NC group, the gene and protein expression of MMP-2 decreased while the TIMP-2 gene and protein expression increased in heart tissues, along with a markedly cardiac collagen deposition.All the above changes were attenuated by benazepril treatment in the DB group. benazepril 260-270 matrix metallopeptidase 2 Rattus norvegicus 80-85 20821936-7 2010 Benazepril may ameliorate cardiac fibrosis partly by regulating the MMP-2/TIMP-2 system. benazepril 0-10 matrix metallopeptidase 2 Rattus norvegicus 68-73 20543091-10 2010 To verify if PC-induced inhibition of MMPs had a causative role in the reduction of infarct size, in separate experiments, we measured infarct size after the pharmacological inhibition of MMPs by ilomastat and found a significant reduction of infarct size compared with the vehicle-treated group. pc 13-15 matrix metallopeptidase 2 Rattus norvegicus 38-42 21126480-11 2010 CONCLUSION: Penehyclidine hydrochloride can decrease the level of MMP-2, HYP in lung tissues and the ET in serum and BALF, increase that of caveolin-1 and lessen the damage induced by paraquat. Penequine hydrochloride 12-39 matrix metallopeptidase 2 Rattus norvegicus 66-71 20621845-0 2010 Elevation of ADAM10, ADAM17, MMP-2 and MMP-9 expression with media degeneration features CaCl2-induced thoracic aortic aneurysm in a rat model. Calcium Chloride 89-94 matrix metallopeptidase 2 Rattus norvegicus 29-34 20621845-6 2010 MMP-2, MMP-9, ADAM-10 and ADAM-17 mRNA levels were increased in CaCl(2)-treated segments (all p<0.01), with trends of elevation in CaCl(2)-untreated segments, as compared with NaCl-treated segments. Calcium Chloride 64-71 matrix metallopeptidase 2 Rattus norvegicus 0-5 20621845-7 2010 Immunohistochemistry displayed significantly increased expressions of MMP-2, MMP-9, ADAM-10 and ADAM-17 (all p<0.01) in intima and media for CaCl(2)-treated segments. Calcium Chloride 144-151 matrix metallopeptidase 2 Rattus norvegicus 70-75 20333532-11 2010 On the other hand, LPZ administration increased MMP-2 expression, and this effect was not influenced by the inhibition of PG synthesis. Lansoprazole 19-22 matrix metallopeptidase 2 Rattus norvegicus 48-53 20333532-13 2010 Additionally, the stimulated expression of MMP-2, which is not secreted by endogenous PGs, is another important factor for ulcer healing by LPZ. Phosphatidylglycerols 86-89 matrix metallopeptidase 2 Rattus norvegicus 43-48 20189191-6 2010 At 7 days, mRNA expression and gelatinolytic activity of matrix metalloproteinase-2 and 9 in vein grafts were significantly suppressed by pioglitazone treatment. Pioglitazone 138-150 matrix metallopeptidase 2 Rattus norvegicus 57-89 20690843-7 2010 RESULTS: The inflammatory and fibrotic tissue reaction is attenuated with PDS in comparison to PG, e.g., the size of the granuloma was smaller with less cell turnover, and less remodeling as represented by, e.g., reduction of apoptosis, expression of MMP-2, or TNF-R2. 3-{1-[3-(Dimethylamino)propyl]-2-Methyl-1h-Indol-3-Yl}-4-(2-Methyl-1h-Indol-3-Yl)-1h-Pyrrole-2,5-Dione 74-77 matrix metallopeptidase 2 Rattus norvegicus 251-256 21516719-0 2010 [State of the liver antioxidant system and content of matrix metalloproteinase-2 of the large intestine under the effect of maleimide derivative in experimental colorectal carcinogenesis in rats]. maleimide 124-133 matrix metallopeptidase 2 Rattus norvegicus 54-80 20610236-10 2010 Because function and structure were restored by doxycycline, the inhibition of MMPs or their modulation may provide beneficial effects for therapeutic intervention in cardiac hypertrophy. Doxycycline 48-59 matrix metallopeptidase 2 Rattus norvegicus 79-83 20649877-10 2010 In addition pro-MMP-2 on gelatin zymography was importantly suppressed by doxycycline in ICN. Doxycycline 74-85 matrix metallopeptidase 2 Rattus norvegicus 16-21 20452391-8 2010 Furthermore, carvedilol down-regulated matrix metalloproteinase-2 expression in the heart, increased nephrin expression in the kidney, and attenuated the increased protein expression of NADPH oxidase subunits in heart and kidney. Carvedilol 13-23 matrix metallopeptidase 2 Rattus norvegicus 39-65 21516719-1 2010 The maleimide derivative--1-(4-Cl-benzyl)-3-Cl-4-(CF3-phenylamino)-1H-pyrrol-2.5-dione (MI-1) with cytostatic activity did not cause substantial changes of liver antioxidant system and level of matrix metalloproteinase-2 in intestinal mucosa after chronic treatment (for 20 weeks). maleimide 4-13 matrix metallopeptidase 2 Rattus norvegicus 194-220 20434464-5 2010 Administration of eugenol induced apoptosis via the mitochondrial pathway by modulating the Bcl-2 family proteins, Apaf-1, cytochrome C, and caspases and inhibiting invasion, and angiogenesis as evidenced by changes in the activities of MMPs and the expression of MMP-2 and -9, VEGF, VEGFR1, TIMP-2 and RECK. Eugenol 18-25 matrix metallopeptidase 2 Rattus norvegicus 237-241 20434464-5 2010 Administration of eugenol induced apoptosis via the mitochondrial pathway by modulating the Bcl-2 family proteins, Apaf-1, cytochrome C, and caspases and inhibiting invasion, and angiogenesis as evidenced by changes in the activities of MMPs and the expression of MMP-2 and -9, VEGF, VEGFR1, TIMP-2 and RECK. Eugenol 18-25 matrix metallopeptidase 2 Rattus norvegicus 264-276 20624160-9 2010 The transcription level of matrix metalloproteinase (MMP)-2 was increased in oxytocin-treated UCB-MSCs. ucb 94-97 matrix metallopeptidase 2 Rattus norvegicus 27-59 20979757-11 2010 CONCLUSIONS: These results indicate Hcy could increase the permeability of blood-brain barrier, the mechanism may be activating the transcription of MMP-2 in rats. Homocysteine 36-39 matrix metallopeptidase 2 Rattus norvegicus 149-154 19490185-9 2010 Fin + Dox treatment for 30 days promoted a decrease in gelatinolytic activity of MMP-2 and an increase in MMP-9. Doxazosin 6-9 matrix metallopeptidase 2 Rattus norvegicus 81-86 20628426-5 2010 Bosentan completely prevented the increase in M/L ratio and MMP-2 activity in diabetes but paradoxically increased M/L ratio and MMP activation in control animals. Bosentan 0-8 matrix metallopeptidase 2 Rattus norvegicus 60-65 20628426-5 2010 Bosentan completely prevented the increase in M/L ratio and MMP-2 activity in diabetes but paradoxically increased M/L ratio and MMP activation in control animals. Bosentan 0-8 matrix metallopeptidase 2 Rattus norvegicus 60-63 24683264-15 2010 CONCLUSION: Doxycycline was associated with protective effects against I/R injury through decreasing apoptosis via attenuating the response of proinflammatory cytokines and inhibiting the activity of MMP-2 in this rat model. Doxycycline 12-23 matrix metallopeptidase 2 Rattus norvegicus 200-205 20370796-1 2010 Our previous study found that Chinese yellow wine could inhibit the production of homocysteine (HCY) induced extracellular matrix metalloproteinase-2 (MMP-2) in the cultured rat vascular smooth muscle cells. Homocysteine 82-94 matrix metallopeptidase 2 Rattus norvegicus 123-149 20370796-1 2010 Our previous study found that Chinese yellow wine could inhibit the production of homocysteine (HCY) induced extracellular matrix metalloproteinase-2 (MMP-2) in the cultured rat vascular smooth muscle cells. Homocysteine 82-94 matrix metallopeptidase 2 Rattus norvegicus 151-156 20370796-1 2010 Our previous study found that Chinese yellow wine could inhibit the production of homocysteine (HCY) induced extracellular matrix metalloproteinase-2 (MMP-2) in the cultured rat vascular smooth muscle cells. Homocysteine 96-99 matrix metallopeptidase 2 Rattus norvegicus 123-149 20370796-1 2010 Our previous study found that Chinese yellow wine could inhibit the production of homocysteine (HCY) induced extracellular matrix metalloproteinase-2 (MMP-2) in the cultured rat vascular smooth muscle cells. Homocysteine 96-99 matrix metallopeptidase 2 Rattus norvegicus 151-156 19490185-10 2010 In conclusion, combined treatment with Fin and Dox interferes in the epithelial cell behaviour and in the MMPs activity, potentially via TGF-beta1-mediated and androgen pathways. Doxazosin 47-50 matrix metallopeptidase 2 Rattus norvegicus 106-110 20121733-4 2010 Rats were randomly assigned into four groups: 75% partial hepatectomy (PH); 100% LT; 25% LT and 25% LT treated with CTT peptide (MMP-2/9 inhibitor). ctt peptide 116-127 matrix metallopeptidase 2 Rattus norvegicus 129-136 20331602-0 2010 Spironolactone and hydrochlorothiazide exert antioxidant effects and reduce vascular matrix metalloproteinase-2 activity and expression in a model of renovascular hypertension. Spironolactone 0-14 matrix metallopeptidase 2 Rattus norvegicus 85-111 20331602-0 2010 Spironolactone and hydrochlorothiazide exert antioxidant effects and reduce vascular matrix metalloproteinase-2 activity and expression in a model of renovascular hypertension. Hydrochlorothiazide 19-38 matrix metallopeptidase 2 Rattus norvegicus 85-111 20331602-13 2010 CONCLUSIONS AND IMPLICATIONS: SPRL or HCTZ, alone or combined, exerted antioxidant effects, and decreased renovascular hypertension-induced MMP-2 up-regulation, thus improving the vascular dysfunction and remodelling found in this model of hypertension. Spironolactone 30-34 matrix metallopeptidase 2 Rattus norvegicus 140-145 20331602-13 2010 CONCLUSIONS AND IMPLICATIONS: SPRL or HCTZ, alone or combined, exerted antioxidant effects, and decreased renovascular hypertension-induced MMP-2 up-regulation, thus improving the vascular dysfunction and remodelling found in this model of hypertension. Hydrochlorothiazide 38-42 matrix metallopeptidase 2 Rattus norvegicus 140-145 20496196-7 2010 The overexpressions of hepatic TGF-beta1, IL-1beta, IL-10, MMP-2, and TIMP-1 were suppressed by bicyclol in BSA-treated rats. bicyclol 96-104 matrix metallopeptidase 2 Rattus norvegicus 59-64 20441599-7 2010 In contrast, Sal B and vitamin E significantly attenuated the expression of alpha-SMA, TGF-beta1, TbetaR-I, p-Smad2/3, and MMP-2 activity, but increased E-cadherin expression. salvianolic acid B 13-18 matrix metallopeptidase 2 Rattus norvegicus 123-128 20441599-7 2010 In contrast, Sal B and vitamin E significantly attenuated the expression of alpha-SMA, TGF-beta1, TbetaR-I, p-Smad2/3, and MMP-2 activity, but increased E-cadherin expression. Vitamin E 23-32 matrix metallopeptidase 2 Rattus norvegicus 123-128 20441599-9 2010 TGF-beta1 induced a typical EMT in HK-2 cells, while it was blocked by Sal B and SB-431542, as evidenced by blocking morphologic transformation, restoring E-cadherin and CK-18 expression, inhibiting alpha-SMA expression and F-actin reorganization, and down-regulating MMP-2/9 activities in TGF-beta1 mediated HK-2 cells. salvianolic acid B 71-76 matrix metallopeptidase 2 Rattus norvegicus 268-273 20441599-9 2010 TGF-beta1 induced a typical EMT in HK-2 cells, while it was blocked by Sal B and SB-431542, as evidenced by blocking morphologic transformation, restoring E-cadherin and CK-18 expression, inhibiting alpha-SMA expression and F-actin reorganization, and down-regulating MMP-2/9 activities in TGF-beta1 mediated HK-2 cells. 4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide 81-90 matrix metallopeptidase 2 Rattus norvegicus 268-273 20016929-6 2010 Biochemical data showed that sodium selenate treatment induced a significant regulation of MMP-2 activity and protein loss as well as normalization of increased levels of tissue nitrite and protein thiol oxidation. Selenic Acid 29-44 matrix metallopeptidase 2 Rattus norvegicus 91-96 20016929-8 2010 Taken together, our data demonstrate that these beneficial effects of sodium selenate treatment in diabetics are related to be not only inhibition of increased oxidative stress but also prevention of both receptor- and smooth muscle-mediated dysfunction of vasculature, in part, via regulation of MMP-2. Selenic Acid 70-85 matrix metallopeptidase 2 Rattus norvegicus 297-302 19897563-7 2010 Both BQ-123 and bosentan prevented the development of CSE-induced emphysema, blocked the expression of ET(A) receptor, inhibited pulmonary apoptosis, inactivated MMP-2 and MMP-9 activities in the lung tissues, reduced the concentrations of inflammatory cytokines TNF-alpha and IL-1beta, and improved the biological antioxidant activity in the serum. cyclo(Trp-Asp-Pro-Val-Leu) 5-11 matrix metallopeptidase 2 Rattus norvegicus 162-167 19897563-7 2010 Both BQ-123 and bosentan prevented the development of CSE-induced emphysema, blocked the expression of ET(A) receptor, inhibited pulmonary apoptosis, inactivated MMP-2 and MMP-9 activities in the lung tissues, reduced the concentrations of inflammatory cytokines TNF-alpha and IL-1beta, and improved the biological antioxidant activity in the serum. Bosentan 16-24 matrix metallopeptidase 2 Rattus norvegicus 162-167 19969080-9 2010 Doxycycline attenuated hypertension induced increases in all the 3 investigated MMPs in both the media and the intima (all P<0.05), but it did not change the amounts of TIMPs 1-4 (P>0.05). Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 80-84 20194304-7 2010 Expression of 9 collagen genes and Mmp2 was upregulated by a high-salt diet in the renal medulla of SS rats, but not in SS-13(BN) rats, an expression pattern opposite to miR-29b. Salts 66-70 matrix metallopeptidase 2 Rattus norvegicus 35-39 19482300-4 2010 We tested whether MMP-2 induced venous relaxation involves inhibition of the Ca(2+) mobilization mechanisms of VSM contraction due to generation of Arg-Gly-Asp (RGD)-containing peptides. arginyl-glycyl-aspartic acid 148-159 matrix metallopeptidase 2 Rattus norvegicus 18-23 19482300-4 2010 We tested whether MMP-2 induced venous relaxation involves inhibition of the Ca(2+) mobilization mechanisms of VSM contraction due to generation of Arg-Gly-Asp (RGD)-containing peptides. Peptides 177-185 matrix metallopeptidase 2 Rattus norvegicus 18-23 19482300-7 2010 RESULTS: In IVC incubated in normal Krebs (2.5 mM Ca(2+)), the alpha-adrenergic agonist phenylephrine (Phe, 10(-5) M) caused initial peak (133.2 +/- 17.5) followed by a maintained contraction (73.4 +/- 11.6), that was inhibited by MMP-2 (1 microg/mL) to 32.4 +/- 12.8 in 30 min. Phenylephrine 88-101 matrix metallopeptidase 2 Rattus norvegicus 231-236 19482300-8 2010 The inhibitory effects of MMP-2 were reversible by washing the tissue with Krebs or in the presence of the MMP inhibitors TIMP-1 (1 microg/mL), Ro 28-2653, and BB-94 (10(-6) M), and were not associated with changes in IVC structure, demonstrating specificity. krebs 75-80 matrix metallopeptidase 2 Rattus norvegicus 26-31 19482300-8 2010 The inhibitory effects of MMP-2 were reversible by washing the tissue with Krebs or in the presence of the MMP inhibitors TIMP-1 (1 microg/mL), Ro 28-2653, and BB-94 (10(-6) M), and were not associated with changes in IVC structure, demonstrating specificity. krebs 75-80 matrix metallopeptidase 2 Rattus norvegicus 26-29 19482300-8 2010 The inhibitory effects of MMP-2 were reversible by washing the tissue with Krebs or in the presence of the MMP inhibitors TIMP-1 (1 microg/mL), Ro 28-2653, and BB-94 (10(-6) M), and were not associated with changes in IVC structure, demonstrating specificity. batimastat 160-165 matrix metallopeptidase 2 Rattus norvegicus 26-31 19482300-8 2010 The inhibitory effects of MMP-2 were reversible by washing the tissue with Krebs or in the presence of the MMP inhibitors TIMP-1 (1 microg/mL), Ro 28-2653, and BB-94 (10(-6) M), and were not associated with changes in IVC structure, demonstrating specificity. batimastat 160-165 matrix metallopeptidase 2 Rattus norvegicus 26-29 20035854-11 2010 In our study it was showed that CCl(4)-treated group significantly increased the protein levels of uPA, MMP-2, MMP-9 and TIMP-1. Cefaclor 32-35 matrix metallopeptidase 2 Rattus norvegicus 104-109 19874802-0 2010 Effects of cisplatin on matrix metalloproteinase-2 in transformed thyroid cells. Cisplatin 11-20 matrix metallopeptidase 2 Rattus norvegicus 24-50 19874802-1 2010 We investigated the effects of cisplatin (cisPt) on matrix metalloproteinase-2 (MMP-2) gelatinolitic activity in transformed PC E1Araf rat thyroid cells. Cisplatin 42-47 matrix metallopeptidase 2 Rattus norvegicus 52-78 19874802-4 2010 The effect of cisPt on MMP-2 was dependent on PKC-zeta activation since it was potentiated by a myristoylated PKC-zeta pseudo substrate peptide or by PKC-zeta down-regulation by siRNA. Cisplatin 14-19 matrix metallopeptidase 2 Rattus norvegicus 23-28 19874802-7 2010 The inhibition of cell migration was also obtained with cisPt; in cisPt-treated cells the administration of MMP-2 active protein was able to restore cell migration capacity. Cisplatin 56-61 matrix metallopeptidase 2 Rattus norvegicus 108-113 19874802-7 2010 The inhibition of cell migration was also obtained with cisPt; in cisPt-treated cells the administration of MMP-2 active protein was able to restore cell migration capacity. Cisplatin 66-71 matrix metallopeptidase 2 Rattus norvegicus 108-113 19874802-8 2010 In conclusion, the decrease of MMP-2 secretion after cisPt was allowed by PKB/AKT and counteracted by PKC-zeta; the cisPt-provoked inhibition of MMP-2 secretion ended in reduction of cell migration. Cisplatin 53-58 matrix metallopeptidase 2 Rattus norvegicus 31-36 19874802-8 2010 In conclusion, the decrease of MMP-2 secretion after cisPt was allowed by PKB/AKT and counteracted by PKC-zeta; the cisPt-provoked inhibition of MMP-2 secretion ended in reduction of cell migration. Cisplatin 116-121 matrix metallopeptidase 2 Rattus norvegicus 31-36 20233689-9 2010 PDT with TSPP offers, in vivo , consistent results regarding ROS generation, MMP2 activation and cytotoxic capacity. sodium pyrophosphate 9-13 matrix metallopeptidase 2 Rattus norvegicus 77-81 20108352-3 2010 siRNA was employed to inhibit MMP-2 expression, and this was compared to GM6001"s (a broad-spectrum MMP inhibitor) inhibition of general MMPs. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 73-79 matrix metallopeptidase 2 Rattus norvegicus 137-141 19579000-9 2010 As RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2. Risperidone 66-77 matrix metallopeptidase 2 Rattus norvegicus 147-151 19579000-9 2010 As RT-PCR and Western blot revealed that the treatment effects of risperidone and haloperidol seemed to be mediated through activation of VEGF and MMP2. Haloperidol 82-93 matrix metallopeptidase 2 Rattus norvegicus 147-151 19579000-16 2010 The findings indicate a promoting effect of risperidone and haloperidol on survival of young neurons in the hippocampus by enhancing the expression of the anti-apoptotic protein BCL-2 and by activation of VEGF/MMP2, whereby an interference with ketamine and thus a priority role of the NMDA system was not evident. Risperidone 44-55 matrix metallopeptidase 2 Rattus norvegicus 210-214 19579000-16 2010 The findings indicate a promoting effect of risperidone and haloperidol on survival of young neurons in the hippocampus by enhancing the expression of the anti-apoptotic protein BCL-2 and by activation of VEGF/MMP2, whereby an interference with ketamine and thus a priority role of the NMDA system was not evident. Haloperidol 60-71 matrix metallopeptidase 2 Rattus norvegicus 210-214 20019701-5 2010 Furthermore, CILO almost completely inhibited a set of upregulated proinflammatory genes (ICAM-1, MCP-1, PDGF-A, osteopontin, MMP-2 and ACE), as well as NAD(P)H oxidase components (p22phox, gp91phox, p47phox) and Aldo-inducible genes (SGK-1 and NHE-1) in the aortic tissues from Aldo-rats. Cilostazol 13-17 matrix metallopeptidase 2 Rattus norvegicus 126-131 20051877-5 2010 Dox produced cardiac structural injury and significant elevation in plasma levels of cardiac enzymes, MMP-2, and cardiac iNOS mRNA expression together with significant reduction in plasma TIMP-1 level. Doxorubicin 0-3 matrix metallopeptidase 2 Rattus norvegicus 102-107 20051877-6 2010 Lisinopril significantly decreases plasma MMP-2 level and cardiac iNOS mRNA expression by 13% and 15%, respectively, in group 3 compared with 36% and 47%, respectively, in group 4 as compared with group 2. Lisinopril 0-10 matrix metallopeptidase 2 Rattus norvegicus 42-47 20127004-7 2010 Results from Western blotting showed that curcumin inhibited the protein levels of PKC, FAK, NF-kappaB p65 and Rho A leading to the inhibition of ERK1/2, MKK7, COX-2 and ROCK1, respectively, finally causing the inhibition of MMP-2 and -9 for the inhibition of migration and invasion of N18 cells. Curcumin 42-50 matrix metallopeptidase 2 Rattus norvegicus 225-237 19874802-8 2010 In conclusion, the decrease of MMP-2 secretion after cisPt was allowed by PKB/AKT and counteracted by PKC-zeta; the cisPt-provoked inhibition of MMP-2 secretion ended in reduction of cell migration. Cisplatin 116-121 matrix metallopeptidase 2 Rattus norvegicus 145-150 20084675-5 2010 Nevertheless the effect of BA on the activities and expression of MMP-2 and MMP-9 during hepatocellular carcinoma is not yet recognized. bacoside A 27-29 matrix metallopeptidase 2 Rattus norvegicus 66-71 20084675-7 2010 Results of gelatin zymography study showed that BA co-treatment significantly decreased the activities of MMP-2 and MMP-9, which is increased during hepatocellular carcinoma. bacoside A 48-50 matrix metallopeptidase 2 Rattus norvegicus 106-111 20084675-8 2010 Further immunoblot analysis showed decreased expression of MMP-2 and MMP-9 in rats co-treated with BA compared to DEN-induced hepatocellular carcinoma. bacoside A 99-101 matrix metallopeptidase 2 Rattus norvegicus 59-64 20084675-8 2010 Further immunoblot analysis showed decreased expression of MMP-2 and MMP-9 in rats co-treated with BA compared to DEN-induced hepatocellular carcinoma. Diethylnitrosamine 114-117 matrix metallopeptidase 2 Rattus norvegicus 59-64 20084675-9 2010 Our results reveal that BA exerts its anti-metastatic effect against DEN-induced hepatocellular carcinoma by inhibiting the activities and expressions of MMP-2 and MMP-9. bacoside A 24-26 matrix metallopeptidase 2 Rattus norvegicus 154-159 20084675-9 2010 Our results reveal that BA exerts its anti-metastatic effect against DEN-induced hepatocellular carcinoma by inhibiting the activities and expressions of MMP-2 and MMP-9. Diethylnitrosamine 69-72 matrix metallopeptidase 2 Rattus norvegicus 154-159 20371878-2 2010 The aims of the study were to investigate the influence of I/R on MMP-2 and to study the effects of wortmannin on modulation of MMP-2 activities after cycle of short I/R procedures (ischemic preconditioning, IP). Wortmannin 100-110 matrix metallopeptidase 2 Rattus norvegicus 128-133 20371878-13 2010 Moreover, the actions of wortmannin were linked with modulation of MMP-2 activities. Wortmannin 25-35 matrix metallopeptidase 2 Rattus norvegicus 67-72 20127004-0 2010 Curcumin blocks migration and invasion of mouse-rat hybrid retina ganglion cells (N18) through the inhibition of MMP-2, -9, FAK, Rho A and Rock-1 gene expression. Curcumin 0-8 matrix metallopeptidase 2 Rattus norvegicus 113-122 20035854-0 2010 Fraxinus rhynchophylla ethanol extract attenuates carbon tetrachloride-induced liver fibrosis in rats via down-regulating the expressions of uPA, MMP-2, MMP-9 and TIMP-1. Carbon Tetrachloride 50-70 matrix metallopeptidase 2 Rattus norvegicus 146-151 20035854-12 2010 FR(EtOH) (0.1 and 0.5 g/kg BW) could inhibit the protein levels of uPA, MMP-2, MMP-9 and TIMP-1. Ethanol 3-7 matrix metallopeptidase 2 Rattus norvegicus 72-77 20035854-15 2010 FR(EtOH) down-regulated the expressions of uPA, MMP-2 and MMP-9 in CCl(4)-induced liver fibrosis in rats. Ethanol 3-7 matrix metallopeptidase 2 Rattus norvegicus 48-53 20407607-0 2010 Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. Streptozocin 111-125 matrix metallopeptidase 2 Rattus norvegicus 62-67 20407607-2 2010 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. Minocycline 21-32 matrix metallopeptidase 2 Rattus norvegicus 41-46 20407607-0 2010 Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. Aspirin 84-91 matrix metallopeptidase 2 Rattus norvegicus 62-67 19879865-1 2010 Nicotine plays a role in smoking-associated cardiovascular diseases, and may upregulate matrix metalloproteinase (MMP)-2 and MMP-9. Nicotine 0-8 matrix metallopeptidase 2 Rattus norvegicus 88-120 19879865-8 2010 MMP-2 and MMP-9 levels increased in the supernatant of SMC cells incubated with nicotine 150 nM (P<0.05) but not with 50 nM. Nicotine 80-88 matrix metallopeptidase 2 Rattus norvegicus 0-5 19879865-12 2010 These findings suggest that nicotine produces cardiovascular effects involving MMPs. Nicotine 28-36 matrix metallopeptidase 2 Rattus norvegicus 79-83 19879865-13 2010 It is possible that MMPs inhibition may counteract the effects produced by nicotine. Nicotine 75-83 matrix metallopeptidase 2 Rattus norvegicus 20-24 20407607-0 2010 Attenuation of diabetic retinopathy by enhanced inhibition of MMP-2 and MMP-9 using aspirin and minocycline in streptozotocin-diabetic rats. Minocycline 96-107 matrix metallopeptidase 2 Rattus norvegicus 62-67 20407607-2 2010 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. Aspirin 87-94 matrix metallopeptidase 2 Rattus norvegicus 41-46 20407607-2 2010 We hypothesized that minocycline induced MMP-2 and MMP-9 inhibition can be enhanced by aspirin, a non-selective COX and tPA inhibitor and this combination can reduce progression of diabetic retinopathy. Tetradecanoylphorbol Acetate 120-123 matrix metallopeptidase 2 Rattus norvegicus 41-46 20213142-2 2010 The purpose of this study was to characterize the role of MMPs as depicted by the expression of MMP-2 and MMP-9 during 4-nitroquinoline 1-oxide-induced rat tongue carcinogenesis. 4-Nitroquinoline 119-135 matrix metallopeptidase 2 Rattus norvegicus 96-101 19508332-0 2010 Finasteride treatment alters MMP-2 and -9 gene expression and activity in the rat ventral prostate. Finasteride 0-11 matrix metallopeptidase 2 Rattus norvegicus 29-41 19508332-2 2010 In this study, we investigated the effects of finasteride on the location, gene expression and activities of matrix metalloproteinases -2 and -9, which are involved in the degradation of extracellular matrix components during tissue remodelling and prostate cancer progression, invasion and metastasis. Finasteride 46-57 matrix metallopeptidase 2 Rattus norvegicus 109-144 19508332-4 2010 Finasteride treatment reduced the epithelial immunostaining of MMP-2 but increased MMP-9 immunostaining in the epithelial cells and in the stroma. Finasteride 0-11 matrix metallopeptidase 2 Rattus norvegicus 63-68 19508332-5 2010 The mRNA expression of both MMP-2 and MMP-9 were significantly increased on day 7 of finasteride treatment, mainly for MMP-9 and returned to the control levels by day 30. Finasteride 85-96 matrix metallopeptidase 2 Rattus norvegicus 28-33 19508332-7 2010 Finasteride increases MMP-9 and reduces MMP-2 activities in the prostate, which may affect negatively and positively both normal and tumoural prostatic cell behaviour during the treatment. Finasteride 0-11 matrix metallopeptidase 2 Rattus norvegicus 40-45 20213142-0 2010 The role of matrix metalloproteinases 2 and 9 during rat tongue carcinogenesis induced by 4-nitroquinoline 1-oxide. 4-Nitroquinoline-1-oxide 90-114 matrix metallopeptidase 2 Rattus norvegicus 12-45 20213142-2 2010 The purpose of this study was to characterize the role of MMPs as depicted by the expression of MMP-2 and MMP-9 during 4-nitroquinoline 1-oxide-induced rat tongue carcinogenesis. 1-oxide 136-143 matrix metallopeptidase 2 Rattus norvegicus 58-62 20213142-2 2010 The purpose of this study was to characterize the role of MMPs as depicted by the expression of MMP-2 and MMP-9 during 4-nitroquinoline 1-oxide-induced rat tongue carcinogenesis. 4-Nitroquinoline 119-135 matrix metallopeptidase 2 Rattus norvegicus 58-62 20213142-2 2010 The purpose of this study was to characterize the role of MMPs as depicted by the expression of MMP-2 and MMP-9 during 4-nitroquinoline 1-oxide-induced rat tongue carcinogenesis. 1-oxide 136-143 matrix metallopeptidase 2 Rattus norvegicus 96-101 20213142-7 2010 MMP-2 and MMP-9 showed positive expression either in pre-neoplastic lesions at 12 weeks following carcinogen exposure or in well-differentiated squamous cell carcinoma induced after 20 weeks of treatment with 4NQO. 4-Nitroquinoline-1-oxide 209-213 matrix metallopeptidase 2 Rattus norvegicus 0-5 19811818-10 2010 Gelatinase A activities appeared lower in CCH than within NCH. 1-acetyl-2-(coumariniminecarboxamide-3-yl)hydrazine 42-45 matrix metallopeptidase 2 Rattus norvegicus 0-12 19837953-2 2010 NO can combine with superoxide to produce peroxynitrite, which activates matrix metalloproteinases (MMPs). Superoxides 20-30 matrix metallopeptidase 2 Rattus norvegicus 100-104 19837953-2 2010 NO can combine with superoxide to produce peroxynitrite, which activates matrix metalloproteinases (MMPs). Peroxynitrous Acid 42-55 matrix metallopeptidase 2 Rattus norvegicus 100-104 20823567-0 2010 Effects of captopril and telmisartan on matrix metalloproteinase-2 and -9 expressions and development of left ventricular fibrosis induced by isoprenaline in rats. Captopril 11-20 matrix metallopeptidase 2 Rattus norvegicus 40-73 20823567-0 2010 Effects of captopril and telmisartan on matrix metalloproteinase-2 and -9 expressions and development of left ventricular fibrosis induced by isoprenaline in rats. Telmisartan 25-36 matrix metallopeptidase 2 Rattus norvegicus 40-73 20823567-1 2010 The aim of this study was to clarify the effects of renin-angiotensin system (RAS) blockade by captopril, an angiotensin converting enzyme inhibitor, and telmisartan, an angiotensin II type 1 receptor antagonist, on matrix metalloproteinase (MMP)-2 and MMP-9 expressions and development of left ventricular (LV) fibrosis induced by isoprenaline in rats. Telmisartan 154-165 matrix metallopeptidase 2 Rattus norvegicus 216-248 20823567-8 2010 MMP-9 expression at the day 2 and MMP-2 expression at the day 8 increased significantly in LV from isoprenaline-treated rats. DL-Leucyl-DL-valine 91-93 matrix metallopeptidase 2 Rattus norvegicus 34-39 20823567-8 2010 MMP-9 expression at the day 2 and MMP-2 expression at the day 8 increased significantly in LV from isoprenaline-treated rats. Isoproterenol 99-111 matrix metallopeptidase 2 Rattus norvegicus 34-39 19578070-6 2009 Inhibition of MMPs (by GM6001) or EGFR (by AG1478) or suppressing the expression of MMP-2 or MMP-7 or the EGFR by small interfering RNA blunted the PI3K phosphorylation of Akt induced by PE. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 23-29 matrix metallopeptidase 2 Rattus norvegicus 14-18 21127388-4 2010 Intracerebroventricular administration of 500 pmol/day Ala(1,3,11,15)-ET-1, an ET(B)-receptor agonist, increased the mRNAs of MMP2 and MMP9 in rat hippocampus and cerebrum. ala(1,3,11,15)-et-1 55-74 matrix metallopeptidase 2 Rattus norvegicus 126-130 21127388-6 2010 Administration of Ala(1,3,11,15)-ET-1 for 7 days also increased the protein content and proteolytic activities of MMP2 and MMP9 in the cerebrum. Alanine 18-21 matrix metallopeptidase 2 Rattus norvegicus 114-118 21127388-8 2010 In rat cultured astrocytes, both Ala(1,3,11,15)-ET-1 (100 nM) and ET-1 (100 nM) increased MMP2 and MMP9 mRNAs. ala(1,3,11,15)-et-1 33-52 matrix metallopeptidase 2 Rattus norvegicus 90-94 20349720-1 2010 OBJECTIVE: To investigate the mechanism of salvianolic acid B (Sal B) action against liver fibrosis through preventing lipid peroxidation and regulating MMP-2 activity in liver. salvianolic acid 43-59 matrix metallopeptidase 2 Rattus norvegicus 153-158 20029543-3 2009 Therefore, we aimed to examine whether omega-3E (50 mg/kg per day for 4 weeks), a long-chain (n-3) polyunsaturated fatty acid enriched with vitamin E, has a beneficial effect on vascular dysfunction via affecting MMPs in streptozotocin-diabetic rat aorta. omega-3e 39-47 matrix metallopeptidase 2 Rattus norvegicus 213-217 19515067-3 2010 The present study investigated the effects of hypertonic saline in metalloproteinase (MMP) regulation and pancreatitis-associated hepatic injury. Sodium Chloride 57-63 matrix metallopeptidase 2 Rattus norvegicus 86-89 19723557-9 2009 Treatment with constant high glucose for 48 h significantly increase cell number, MMP-2 activation, OPN protein and mRNA expression compared with VSMCs treated with the cells normal glucose, and these effects were further enhanced when VSMCs were treated with intermittent high glucose. Glucose 29-36 matrix metallopeptidase 2 Rattus norvegicus 82-87 19723557-11 2009 CONCLUSIONS: In cultured VSMCs, constant high glucose concentrations enhanced MMP-2 activity, cell proliferation and OPN expression. Glucose 46-53 matrix metallopeptidase 2 Rattus norvegicus 78-83 20082249-10 2009 Compared with the model control, DBD group showed slighter hepatic fatty degeneration and collagen deposition, and had lower levels of ALT, AST and TBIL activities, lower contents of MDA, TG and Hyp, but higher SOD level and Alb content (P<0.05), and DBD also down-regulated MMP-2 mRNA expression and decreased MMP-2/9 activities in the fifibrotic livers (P<0.01). 4,4'-dibenzamido-2,2'-stilbenedisulfonic acid 33-36 matrix metallopeptidase 2 Rattus norvegicus 278-283 20082249-10 2009 Compared with the model control, DBD group showed slighter hepatic fatty degeneration and collagen deposition, and had lower levels of ALT, AST and TBIL activities, lower contents of MDA, TG and Hyp, but higher SOD level and Alb content (P<0.05), and DBD also down-regulated MMP-2 mRNA expression and decreased MMP-2/9 activities in the fifibrotic livers (P<0.01). 4,4'-dibenzamido-2,2'-stilbenedisulfonic acid 33-36 matrix metallopeptidase 2 Rattus norvegicus 314-319 20082249-11 2009 CONCLUSION: The action of DBD against liver fibrosis is related to prevent lipid peroxidation and inhibit MMP-2/9 activities in the fibrotic livers. 4,4'-dibenzamido-2,2'-stilbenedisulfonic acid 26-29 matrix metallopeptidase 2 Rattus norvegicus 106-111 19811527-10 2009 Nitrates/nitrites and TBARS, metabolites of MMPs activators, were increased in the diabetic placenta and reduced by 15dPGJ(2). Nitrates 0-8 matrix metallopeptidase 2 Rattus norvegicus 44-48 19811527-10 2009 Nitrates/nitrites and TBARS, metabolites of MMPs activators, were increased in the diabetic placenta and reduced by 15dPGJ(2). Nitrites 9-17 matrix metallopeptidase 2 Rattus norvegicus 44-48 19811527-10 2009 Nitrates/nitrites and TBARS, metabolites of MMPs activators, were increased in the diabetic placenta and reduced by 15dPGJ(2). Thiobarbituric Acid Reactive Substances 22-27 matrix metallopeptidase 2 Rattus norvegicus 44-48 19762547-11 2009 The effect of 5-ASA in UC may be caused by the down-regulation of expression of endostatin and angiostatin by modulation of MMP2 and MMP9 via inhibition of TNFalpha. Mesalamine 14-19 matrix metallopeptidase 2 Rattus norvegicus 124-128 19908197-5 2009 Proteolytic processing of DMP1 by MMP-2 produced two major peptides, one that contains the C-terminal region of the protein known to carry both the ASARM (aspartic acid and serine rich domain) domain involved in biomineralization and the DNA binding site of DMP1. Aspartic Acid 155-168 matrix metallopeptidase 2 Rattus norvegicus 34-39 19747956-7 2009 Subsequently, the expression of matrix metalloproteinase (MMP)-2 and MMP-9 were also inhibited by ghrelin injection. Ghrelin 98-105 matrix metallopeptidase 2 Rattus norvegicus 32-64 19908197-5 2009 Proteolytic processing of DMP1 by MMP-2 produced two major peptides, one that contains the C-terminal region of the protein known to carry both the ASARM (aspartic acid and serine rich domain) domain involved in biomineralization and the DNA binding site of DMP1. Serine 173-179 matrix metallopeptidase 2 Rattus norvegicus 34-39 19712057-3 2009 GM6001, a broad spectrum MMPs inhibitor, was injected (50 mg/kg or 100 mg/kg) intraperitoneally at 2 h and 24 h after HI injury. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 0-6 matrix metallopeptidase 2 Rattus norvegicus 25-29 19889233-12 2009 Dexamethasone inhibits E2-modulated changes in collagen density and expression of MMPs although these effects are variable. Dexamethasone 0-13 matrix metallopeptidase 2 Rattus norvegicus 82-86 19516001-1 2009 PURPOSE: Doxycycline, a broad-spectrum antibiotic, has certain antiangiogenic properties and can inhibit matrix metalloproteinases (MMPs/gelatinases). Doxycycline 9-20 matrix metallopeptidase 2 Rattus norvegicus 132-136 19516001-12 2009 However, the in vitro enzymatic activities of purified MMP-2 and MMP-9 declined significantly with doxycycline. Doxycycline 99-110 matrix metallopeptidase 2 Rattus norvegicus 55-60 19712057-5 2009 Doxycycline, another MMPs inhibitor, was injected (10 mg/kg or 30 mg/kg) intraperitoneally at 2 h after HI, then BBB integrity and brain edema were measured at 48 h post-HI using brain water content measurement and IgG staining. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 21-25 19712057-12 2009 These results suggest that early MMPs inhibition with a broad-spectrum inhibitor provides both acute and long-term neuroprotection in the developing brain by reducing TJPs degradation, preserving BBB integrity, and ameliorating brain edema after neonatal HI injury. tjps 167-171 matrix metallopeptidase 2 Rattus norvegicus 33-37 19958643-9 2009 CONCLUSION: Curcumine inhibits migration and invasion of activated HSC by reducing MMP-2 expression and activity. Curcumin 12-21 matrix metallopeptidase 2 Rattus norvegicus 83-88 19958643-6 2009 When treated with 25, 50 or 100 micromol/L curcumine, the expression of MMP-2 was reduced by 21.8%+/-5.1%, 65.5%+/-9.2% or 87.9%+/-11.5% (P < 0.05), and the activity of MMP-2 was also significantly reduced by curcumine. Curcumin 212-221 matrix metallopeptidase 2 Rattus norvegicus 72-77 19958643-0 2009 [Curcumine inhibits migration and invasion of hepatic stellate cells by reducing MMP-2 expression and activity]. Curcumin 1-10 matrix metallopeptidase 2 Rattus norvegicus 81-86 19958643-5 2009 RESULTS: Curcumine reduced the level and activity of MMP-2 expression in activated HSC in a dose-dependent manner. Curcumin 9-18 matrix metallopeptidase 2 Rattus norvegicus 53-58 19958643-6 2009 When treated with 25, 50 or 100 micromol/L curcumine, the expression of MMP-2 was reduced by 21.8%+/-5.1%, 65.5%+/-9.2% or 87.9%+/-11.5% (P < 0.05), and the activity of MMP-2 was also significantly reduced by curcumine. Curcumin 43-52 matrix metallopeptidase 2 Rattus norvegicus 72-77 19809219-17 2009 These results suggest that telmisartan could attenuate the monocrotaline-induced RV remodeling through improvements of RV hypertrophy, fibrosis, dysfunction, and inhibition of MMPs. Telmisartan 27-38 matrix metallopeptidase 2 Rattus norvegicus 176-180 19958643-6 2009 When treated with 25, 50 or 100 micromol/L curcumine, the expression of MMP-2 was reduced by 21.8%+/-5.1%, 65.5%+/-9.2% or 87.9%+/-11.5% (P < 0.05), and the activity of MMP-2 was also significantly reduced by curcumine. Curcumin 43-52 matrix metallopeptidase 2 Rattus norvegicus 172-177 19695229-5 2009 Compared with vehicle-treated MI rats, oral valsartan, but not PD123319, limited infarct size, normalized MMPs/TIMP-1 balance and restored FN level. Valsartan 44-53 matrix metallopeptidase 2 Rattus norvegicus 106-110 19801827-8 2009 MMP-2 activity also increased significantly in the ISO group, but decreased in the ISO+DOX group. Doxycycline 87-90 matrix metallopeptidase 2 Rattus norvegicus 0-5 19693770-3 2009 To further investigate the correlation between MMP-2 and protein kinase C alpha (PKC alpha), the expression of MMP-2 in the 12-O-tetradecanoylphorbol 13-acetate (TPA)-treated organotypic culture of decidual tissue was determined. Tetradecanoylphorbol Acetate 124-160 matrix metallopeptidase 2 Rattus norvegicus 111-116 19693770-3 2009 To further investigate the correlation between MMP-2 and protein kinase C alpha (PKC alpha), the expression of MMP-2 in the 12-O-tetradecanoylphorbol 13-acetate (TPA)-treated organotypic culture of decidual tissue was determined. Tetradecanoylphorbol Acetate 162-165 matrix metallopeptidase 2 Rattus norvegicus 111-116 19693770-4 2009 The results showed that the active form of MMP-2 was significantly increased in the TPA-treated cultures. Tetradecanoylphorbol Acetate 84-87 matrix metallopeptidase 2 Rattus norvegicus 43-48 19693770-6 2009 In addition, TPA also reversed the MMP-2 expression after by progesterone pretreatment in the primary decidual cells. Tetradecanoylphorbol Acetate 13-16 matrix metallopeptidase 2 Rattus norvegicus 35-40 19693770-6 2009 In addition, TPA also reversed the MMP-2 expression after by progesterone pretreatment in the primary decidual cells. Progesterone 61-73 matrix metallopeptidase 2 Rattus norvegicus 35-40 19581022-6 2009 Furthermore, DFO treatment of DRG cell cultures activated neuroprotective and antioxidative programs such as matrix metallopeptidase 2 and apolipoprotein D to promote neurite regeneration. Deferoxamine 13-16 matrix metallopeptidase 2 Rattus norvegicus 109-134 19628804-8 2009 However, minocycline treatment at 3 mg/kg IV decreased total protein expression of both MMP-2 (P=0.0034) and MMP-9 (P=0.001 for 92 kDa and P=0.0084 for 87 kDa). Minocycline 9-20 matrix metallopeptidase 2 Rattus norvegicus 88-93 19861263-0 2009 [Effects of Panax notoginsenoside on TNF-alpha and MMP-2 expressions in rats with post-myocardial infarction ventricular remodeling and the mechanism]. panax notoginsenoside 12-33 matrix metallopeptidase 2 Rattus norvegicus 51-56 19861263-1 2009 OBJECTIVE: To observe the effects of Panax notoginsenoside (PNS) on tumor necrosis factor-alpha (TNF-alpha) and matrix metalloproteinases-2 (MMP-2) expressions in rats with post-myocardial infarction ventricular remodeling and explore the mechanism. panax notoginsenoside 37-58 matrix metallopeptidase 2 Rattus norvegicus 112-139 19861263-1 2009 OBJECTIVE: To observe the effects of Panax notoginsenoside (PNS) on tumor necrosis factor-alpha (TNF-alpha) and matrix metalloproteinases-2 (MMP-2) expressions in rats with post-myocardial infarction ventricular remodeling and explore the mechanism. panax notoginsenoside 37-58 matrix metallopeptidase 2 Rattus norvegicus 141-146 19861263-1 2009 OBJECTIVE: To observe the effects of Panax notoginsenoside (PNS) on tumor necrosis factor-alpha (TNF-alpha) and matrix metalloproteinases-2 (MMP-2) expressions in rats with post-myocardial infarction ventricular remodeling and explore the mechanism. 4'-phosphopantetheine 60-63 matrix metallopeptidase 2 Rattus norvegicus 112-139 19861263-1 2009 OBJECTIVE: To observe the effects of Panax notoginsenoside (PNS) on tumor necrosis factor-alpha (TNF-alpha) and matrix metalloproteinases-2 (MMP-2) expressions in rats with post-myocardial infarction ventricular remodeling and explore the mechanism. 4'-phosphopantetheine 60-63 matrix metallopeptidase 2 Rattus norvegicus 141-146 19464279-0 2009 Inhibitory effect of penta-acetyl geniposide on C6 glioma cells metastasis by inhibiting matrix metalloproteinase-2 expression involved in both the PI3K and ERK signaling pathways. pentaacetyl geniposide 21-44 matrix metallopeptidase 2 Rattus norvegicus 89-115 19493954-10 2009 GSK-3beta kinase activity was significantly increased upon incubation with MMP-2 which was abrogated by the MMP inhibitor GM-6001. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 122-129 matrix metallopeptidase 2 Rattus norvegicus 75-80 19493954-15 2009 MMP-2 may cleave off the N-terminal of GSK-3beta where the inhibitory phosphorylation of serine-9 occurs. Serine 89-95 matrix metallopeptidase 2 Rattus norvegicus 0-5 19631747-5 2009 MMP-2 is upregulated after hUCB treatment in spinal cord injured rats and in spinal neurons injured either with staurosporine or hydrogen peroxide. Staurosporine 112-125 matrix metallopeptidase 2 Rattus norvegicus 0-5 19631747-5 2009 MMP-2 is upregulated after hUCB treatment in spinal cord injured rats and in spinal neurons injured either with staurosporine or hydrogen peroxide. Hydrogen Peroxide 129-146 matrix metallopeptidase 2 Rattus norvegicus 0-5 19582783-7 2009 The increased expression of Ctgf and Timp1 and the decreased expression of Akt1, Anpep, and Mmp2 and Tek (genes involved in stimulating angiogenesis) from AMPH exposure suggest that angiogenesis was arrested or disrupted in MAV to a greater extent by AMPH compared to EIH. Amphetamine 155-159 matrix metallopeptidase 2 Rattus norvegicus 92-96 19622063-5 2009 Studies have shown that fragments of laminin chains are generated from the laminin/integrin protein complex at the apical ES via the action of MMP-2 (matrix metalloprotease-2) at spermiation. Einsteinium 122-124 matrix metallopeptidase 2 Rattus norvegicus 143-148 19622063-5 2009 Studies have shown that fragments of laminin chains are generated from the laminin/integrin protein complex at the apical ES via the action of MMP-2 (matrix metalloprotease-2) at spermiation. Einsteinium 122-124 matrix metallopeptidase 2 Rattus norvegicus 150-174 19539802-7 2009 Both MMP-2 and MMP-9 levels were found to be increased in DEN-induced animals when compared to control. Diethylnitrosamine 58-61 matrix metallopeptidase 2 Rattus norvegicus 5-10 19501083-6 2009 Treatment with either dose of nifedipine reduced the extent of fibrosis, the collagen type I to type III mRNA ratio, and MMP-2 activity and its mRNA expression compared with those in Vehicle. Nifedipine 30-40 matrix metallopeptidase 2 Rattus norvegicus 121-126 19376089-8 2009 Zinc down-regulated ethanol- and acetaldehyde-induced production of TIMP-1 and TIMP-2 and decreased the activity of MMP-2. Ethanol 20-27 matrix metallopeptidase 2 Rattus norvegicus 116-121 19376089-8 2009 Zinc down-regulated ethanol- and acetaldehyde-induced production of TIMP-1 and TIMP-2 and decreased the activity of MMP-2. Acetaldehyde 33-45 matrix metallopeptidase 2 Rattus norvegicus 116-121 19401321-10 2009 MMP H scores were significantly lower in the group that received low-dose Dox in both epithelial and stromal MMP-2 and -9 immunostaining when compared with the control group [P = 0.048, P = 0.002, P = 0.007 and P = 0.002, respectively, MMP-2 (epithelia), MMP-2 (stroma), MMP-9 (epithelia) and MMP-9 (stroma)]. Doxycycline 74-77 matrix metallopeptidase 2 Rattus norvegicus 0-3 19401321-10 2009 MMP H scores were significantly lower in the group that received low-dose Dox in both epithelial and stromal MMP-2 and -9 immunostaining when compared with the control group [P = 0.048, P = 0.002, P = 0.007 and P = 0.002, respectively, MMP-2 (epithelia), MMP-2 (stroma), MMP-9 (epithelia) and MMP-9 (stroma)]. Doxycycline 74-77 matrix metallopeptidase 2 Rattus norvegicus 109-121 19401321-10 2009 MMP H scores were significantly lower in the group that received low-dose Dox in both epithelial and stromal MMP-2 and -9 immunostaining when compared with the control group [P = 0.048, P = 0.002, P = 0.007 and P = 0.002, respectively, MMP-2 (epithelia), MMP-2 (stroma), MMP-9 (epithelia) and MMP-9 (stroma)]. Doxycycline 74-77 matrix metallopeptidase 2 Rattus norvegicus 109-114 19401321-10 2009 MMP H scores were significantly lower in the group that received low-dose Dox in both epithelial and stromal MMP-2 and -9 immunostaining when compared with the control group [P = 0.048, P = 0.002, P = 0.007 and P = 0.002, respectively, MMP-2 (epithelia), MMP-2 (stroma), MMP-9 (epithelia) and MMP-9 (stroma)]. Doxycycline 74-77 matrix metallopeptidase 2 Rattus norvegicus 236-241 19357873-0 2009 Effect of all-trans retinoic acid on renal expressions of matrix metalloproteinase-2, matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 in rats with glomerulosclerosis. Tretinoin 10-33 matrix metallopeptidase 2 Rattus norvegicus 58-84 19391111-8 2009 An increase in the expression of matrix metalloproteinase-2 (MMP-2) was evident in CsA-induced groups of rats, which was moderately reduced in SAC treated rats. Cyclosporine 83-86 matrix metallopeptidase 2 Rattus norvegicus 33-59 19391111-8 2009 An increase in the expression of matrix metalloproteinase-2 (MMP-2) was evident in CsA-induced groups of rats, which was moderately reduced in SAC treated rats. Cyclosporine 83-86 matrix metallopeptidase 2 Rattus norvegicus 61-66 19357873-3 2009 Therefore, a rat model of GS was established to investigate the effect of all-trans retinoic acid (ATRA) on the renal expressions of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1). Tretinoin 74-97 matrix metallopeptidase 2 Rattus norvegicus 161-166 19357873-3 2009 Therefore, a rat model of GS was established to investigate the effect of all-trans retinoic acid (ATRA) on the renal expressions of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1). Tretinoin 99-103 matrix metallopeptidase 2 Rattus norvegicus 133-159 19357873-3 2009 Therefore, a rat model of GS was established to investigate the effect of all-trans retinoic acid (ATRA) on the renal expressions of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1). Tretinoin 74-97 matrix metallopeptidase 2 Rattus norvegicus 133-159 19357873-3 2009 Therefore, a rat model of GS was established to investigate the effect of all-trans retinoic acid (ATRA) on the renal expressions of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and tissue inhibitor of metalloproteinase-1 (TIMP-1). Tretinoin 99-103 matrix metallopeptidase 2 Rattus norvegicus 161-166 19041098-0 2009 Differential effect of 17-beta-estradiol on smooth muscle cell and aortic explant MMP2. Estradiol 23-40 matrix metallopeptidase 2 Rattus norvegicus 82-86 19357873-15 2009 In conclusion, ATRA may protect renal function and step down the progression of GS by reducing the expression of TIMP-1, enhancing the expression and activity of MMP-2 and MMP-9, and regulating the ratio of MMPs/TIMPs to dynamic balance, so as to reduce the accumulation of ECM. Tretinoin 15-19 matrix metallopeptidase 2 Rattus norvegicus 162-167 19357873-15 2009 In conclusion, ATRA may protect renal function and step down the progression of GS by reducing the expression of TIMP-1, enhancing the expression and activity of MMP-2 and MMP-9, and regulating the ratio of MMPs/TIMPs to dynamic balance, so as to reduce the accumulation of ECM. Tretinoin 15-19 matrix metallopeptidase 2 Rattus norvegicus 207-211 19148693-9 2009 Losartan, CsA or VIV abolished stretch-induced alterations in MMP-2/-9 and MT1-MMP expression and enzyme activity by normalizing the Cn-activity and the DNA binding activity of NFATc1. Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 62-70 19148693-9 2009 Losartan, CsA or VIV abolished stretch-induced alterations in MMP-2/-9 and MT1-MMP expression and enzyme activity by normalizing the Cn-activity and the DNA binding activity of NFATc1. Cyclosporine 10-13 matrix metallopeptidase 2 Rattus norvegicus 62-70 19513542-6 2009 However, induction of AT2R by Dox addition markedly decreased MMP-2 levels (P<0.01) and this downregulation was further promoted by CV-11974, a specific antagonist of AT1 receptor. Doxycycline 30-33 matrix metallopeptidase 2 Rattus norvegicus 62-67 19041098-9 2009 Aortas from males, females, and estradiol-treated males were stimulated with IL-1beta for 48-h, and MMP2 activity in the conditioned media was determined. Estradiol 32-41 matrix metallopeptidase 2 Rattus norvegicus 100-104 19041098-10 2009 RESULTS: Experiment I: MMP2 gene expression was 3-fold higher in male compared with female IL-1beta stimulated RASMCs (P<0.0001). rasmcs 111-117 matrix metallopeptidase 2 Rattus norvegicus 23-27 19041098-11 2009 MMP2:TIMP2 gene expression ratio was 7.5-fold greater in male versus female RASMCs. rasmcs 76-82 matrix metallopeptidase 2 Rattus norvegicus 0-4 19041098-12 2009 MMP2 protein levels were 3-fold higher (2.68 versus 0.96 o.d./mg total protein, P=0.003) in male versus female RASMCs. rasmcs 111-117 matrix metallopeptidase 2 Rattus norvegicus 0-4 19345729-4 2009 The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. Superoxides 29-39 matrix metallopeptidase 2 Rattus norvegicus 84-89 19041098-14 2009 Experiment II: MMP2 activity in male and female RASMCs was not altered by a wide range of 17-beta-estradiol concentrations. rasmcs 48-54 matrix metallopeptidase 2 Rattus norvegicus 15-19 19041098-15 2009 Experiment III: When pretreated with 17-beta-estradiol, MMP2 activity in the media of male rat whole-aortic explants decreased 2-fold (P=0.002). Estradiol 37-54 matrix metallopeptidase 2 Rattus norvegicus 56-60 19041098-17 2009 CONCLUSIONS: MMP2 is higher in male RASMCs compared to female RASMCs. rasmcs 36-42 matrix metallopeptidase 2 Rattus norvegicus 13-17 19041098-17 2009 CONCLUSIONS: MMP2 is higher in male RASMCs compared to female RASMCs. rasmcs 62-68 matrix metallopeptidase 2 Rattus norvegicus 13-17 19041098-18 2009 Exogenous 17-beta-estradiol did not alter MMP2 activity in vitro, but in vivo 17-beta-estradiol exposure greatly decreased male aortic MMP2 production to levels seen in the female aorta. Estradiol 78-95 matrix metallopeptidase 2 Rattus norvegicus 135-139 19345729-6 2009 Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. Glucose 0-7 matrix metallopeptidase 2 Rattus norvegicus 202-207 19345729-6 2009 Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. Superoxides 112-122 matrix metallopeptidase 2 Rattus norvegicus 53-58 19345729-4 2009 The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. Glucose 53-60 matrix metallopeptidase 2 Rattus norvegicus 84-89 19345729-6 2009 Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. Superoxides 112-122 matrix metallopeptidase 2 Rattus norvegicus 202-207 19345729-8 2009 Thus, MMP-2 has a proapoptotic role in the loss of retinal capillary cells in diabetes, and the activation of MMP-2 is under the control of superoxide. Superoxides 140-150 matrix metallopeptidase 2 Rattus norvegicus 110-115 19345729-4 2009 The effects of mitochondrial superoxide scavenger on glucose-induced alterations in MMP-2, and its proenzyme activator MT1-MMP and physiological inhibitor TIMP-2, were determined in retinal endothelial cells, and the regulation of their glucose-induced accelerated apoptosis by the inhibitors of MMP-2 was accessed. Glucose 53-60 matrix metallopeptidase 2 Rattus norvegicus 296-301 19345729-6 2009 Glucose-induced activation of retinal capillary cell MMP-2 and MT1-MMP and decrease in TIMP-2 were inhibited by superoxide scavengers, and their accelerated apoptosis was prevented by the inhibitors of MMP-2. Glucose 0-7 matrix metallopeptidase 2 Rattus norvegicus 53-58 19220677-0 2009 Antifibrotic activity of anisodamine in vivo is associated with changed intrahepatic levels of matrix metalloproteinase-2 and its inhibitor tissue inhibitors of metalloproteinases-2 and transforming growth factor beta1 in rats with carbon tetrachloride-induced liver injury. anisodamine 25-36 matrix metallopeptidase 2 Rattus norvegicus 95-121 19425180-4 2009 Because we have previously shown that matrix metalloproteinase-2 (MMP2) is activated in OM by alachlor, in the present studies we evaluated both MMP2 activation and changes in OM gene expression in response to carcinogenic and non-carcinogenic chloracetanilide treatments. alachlor 94-102 matrix metallopeptidase 2 Rattus norvegicus 38-64 19425180-4 2009 Because we have previously shown that matrix metalloproteinase-2 (MMP2) is activated in OM by alachlor, in the present studies we evaluated both MMP2 activation and changes in OM gene expression in response to carcinogenic and non-carcinogenic chloracetanilide treatments. alachlor 94-102 matrix metallopeptidase 2 Rattus norvegicus 66-70 19425180-4 2009 Because we have previously shown that matrix metalloproteinase-2 (MMP2) is activated in OM by alachlor, in the present studies we evaluated both MMP2 activation and changes in OM gene expression in response to carcinogenic and non-carcinogenic chloracetanilide treatments. chloracetanilide 244-260 matrix metallopeptidase 2 Rattus norvegicus 38-64 19425180-4 2009 Because we have previously shown that matrix metalloproteinase-2 (MMP2) is activated in OM by alachlor, in the present studies we evaluated both MMP2 activation and changes in OM gene expression in response to carcinogenic and non-carcinogenic chloracetanilide treatments. chloracetanilide 244-260 matrix metallopeptidase 2 Rattus norvegicus 66-70 19425180-5 2009 All three chloracetanilides activated MMP2, and >300 genes were significantly up- or downregulated between control and alachlor-treated rats. chloracetanilides 10-27 matrix metallopeptidase 2 Rattus norvegicus 38-42 18665326-0 2009 Silymarin attenuated mast cell recruitment thereby decreased the expressions of matrix metalloproteinases-2 and 9 in rat liver carcinogenesis. Silymarin 0-9 matrix metallopeptidase 2 Rattus norvegicus 80-113 18665326-5 2009 In the present study, we investigated whether dietary supplementation of silymarin has any role in mast cell density (MCD) and in the expressions of MMP-2 and MMP-9 in N-nitrosodiethylamine induced (NDEA) liver cancer in Wistar albino male rats. Silymarin 73-82 matrix metallopeptidase 2 Rattus norvegicus 149-154 18665326-6 2009 NDEA administered rats showed increased MCD as revealed by toluidine blue staining along with upregulated expressions of MMP-2 and MMP-9. Diethylnitrosamine 0-4 matrix metallopeptidase 2 Rattus norvegicus 121-126 18665326-7 2009 Silymarin treatment inhibited this increase in MCD and downregulated the expressions of MMP-2 and MMP-9 as revealed by Western blotting and immunohistochemistry. Silymarin 0-9 matrix metallopeptidase 2 Rattus norvegicus 88-93 18665326-8 2009 In conclusion, silymarin exerted beneficial effects on liver carcinogenesis by attenuating the recruitment of mast cells and thereby decreased the expressions of MMP-2 and MMP-9. Silymarin 15-24 matrix metallopeptidase 2 Rattus norvegicus 162-167 19220677-0 2009 Antifibrotic activity of anisodamine in vivo is associated with changed intrahepatic levels of matrix metalloproteinase-2 and its inhibitor tissue inhibitors of metalloproteinases-2 and transforming growth factor beta1 in rats with carbon tetrachloride-induced liver injury. Carbon Tetrachloride 232-252 matrix metallopeptidase 2 Rattus norvegicus 95-121 19220677-14 2009 The levels of MMP2 and TIMP2 mRNA and the protein of MMP2 in livers were significantly reduced in the anisodamine preventive group and therapeutic groups. anisodamine 102-113 matrix metallopeptidase 2 Rattus norvegicus 14-18 19220677-14 2009 The levels of MMP2 and TIMP2 mRNA and the protein of MMP2 in livers were significantly reduced in the anisodamine preventive group and therapeutic groups. anisodamine 102-113 matrix metallopeptidase 2 Rattus norvegicus 53-57 19210333-1 2009 BACKGROUND AND OBJECTIVE: Membrane type-I matrix metalloproteinase (MMP) and tissue inhibitor of metalloproteinase-2 (TIMP-2) regulate the activation of MMP-2; however, their roles in the activation of MMP-2 in gingiva during treatment with cyclosporine A are still unknown. Cyclosporine 241-255 matrix metallopeptidase 2 Rattus norvegicus 153-158 19210333-8 2009 The expression of MMP-2 mRNA was unaffected but the expression of MMP-2 protein showed a significant decrease upon treatment with cyclosporine A. Cyclosporine 130-144 matrix metallopeptidase 2 Rattus norvegicus 18-23 19210333-8 2009 The expression of MMP-2 mRNA was unaffected but the expression of MMP-2 protein showed a significant decrease upon treatment with cyclosporine A. Cyclosporine 130-144 matrix metallopeptidase 2 Rattus norvegicus 66-71 19210333-9 2009 In fibroblast culture medium, the presence of cyclosporine A induced a decrease in MMP-2 activity in a dose-dependent manner. Cyclosporine 46-60 matrix metallopeptidase 2 Rattus norvegicus 83-88 19210333-11 2009 CONCLUSION: Cyclosporine A inhibits the expression of membrane type-I MMP in gingiva and it may further reduce the activation of MMP-2. Cyclosporine 12-26 matrix metallopeptidase 2 Rattus norvegicus 129-134 19306293-9 2009 Interestingly, while MMP-2 mRNA levels increased in response to histamine H1 or H2 receptor activation, significantly larger increases were observed in cells co-treated with ICAT and histamine or the histamine receptor agonists, HTMT and dimaprit. Histamine 64-73 matrix metallopeptidase 2 Rattus norvegicus 21-26 19306293-10 2009 While both VEGF and histamine increase nuclear beta-catenin and MMP-2 production, the role of beta-catenin in MMP-2 regulation differs between the two stimuli. Histamine 20-29 matrix metallopeptidase 2 Rattus norvegicus 64-69 19306293-0 2009 Differential role of beta-catenin in VEGF and histamine-induced MMP-2 production in microvascular endothelial cells. Histamine 46-55 matrix metallopeptidase 2 Rattus norvegicus 64-69 19426551-7 2009 Progesterone (1 microM) significantly decreased both human and rat MMP-2 promoter activity (80.1% +/- 0.3 and 81.3% +/- 0.23, respectively). Progesterone 0-12 matrix metallopeptidase 2 Rattus norvegicus 67-72 19306293-3 2009 We hypothesized that beta-catenin acts as a positive regulator of MMP-2 and MT1-MMP transcription following VEGF or histamine stimulation. Histamine 116-125 matrix metallopeptidase 2 Rattus norvegicus 66-71 19306293-5 2009 Latent MMP-2 protein levels were increased following VEGF and histamine treatment as were MMP-2 mRNA transcript levels. Histamine 62-71 matrix metallopeptidase 2 Rattus norvegicus 7-12 18836702-8 2009 Doxycycline also prevented lead-induced increases in the MMP-2/TIMP-2 mRNA ratio. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 57-62 19248829-2 2009 Because MMPs are upregulated by increased formation of reactive oxygen species (ROS), we hypothesized that antioxidant approaches could attenuate the increases in MMP-2 expression/activity and the vascular dysfunction and remodeling associated with 2K-1C hypertension. Reactive Oxygen Species 55-78 matrix metallopeptidase 2 Rattus norvegicus 8-12 19248829-2 2009 Because MMPs are upregulated by increased formation of reactive oxygen species (ROS), we hypothesized that antioxidant approaches could attenuate the increases in MMP-2 expression/activity and the vascular dysfunction and remodeling associated with 2K-1C hypertension. Reactive Oxygen Species 80-83 matrix metallopeptidase 2 Rattus norvegicus 8-12 19248829-11 2009 Tempol was more effective than apocyanin in attenuating hypertension-induced increases in oxidative stress (both p<0.05), MMP-2 levels, and MMP-2 activity in hypertensive rats (all p<0.05). tempol 0-6 matrix metallopeptidase 2 Rattus norvegicus 125-130 19248829-11 2009 Tempol was more effective than apocyanin in attenuating hypertension-induced increases in oxidative stress (both p<0.05), MMP-2 levels, and MMP-2 activity in hypertensive rats (all p<0.05). tempol 0-6 matrix metallopeptidase 2 Rattus norvegicus 143-148 19516083-7 2009 We have shown that rats treated by Tetracycline reduce the MMP-2 expression and HSP-70. Tetracycline 35-47 matrix metallopeptidase 2 Rattus norvegicus 59-64 18821853-0 2009 Hyperbaric oxygen activates discoidin domain receptor 2 via tumour necrosis factor-alpha and the p38 MAPK pathway to increase vascular smooth muscle cell migration through matrix metalloproteinase 2. Oxygen 11-17 matrix metallopeptidase 2 Rattus norvegicus 172-198 19111676-6 2009 Finally, when the cisplatin-induced ROS generation was blocked by using NAD(P)H oxidase inhibitors, a decrease in cisplatin-induced MMP-2 enhancement, MAPK/p38 and EGFR activation, and caspase-7 proteolysis occurred. Cisplatin 114-123 matrix metallopeptidase 2 Rattus norvegicus 132-137 19555562-1 2009 OBJECTIVE: Based on establishment of four rat models of experimental pulmonary hypertension (PH), the authors examined the inhibition of matrix metalloproteinases (MMPs) by doxycycline and its effect on the development of PH and associated pulmonary vascular remodeling. Doxycycline 173-184 matrix metallopeptidase 2 Rattus norvegicus 164-168 19555562-11 2009 (3) The activity of MMPs was inhibited by doxycycline effectively as assessed by gelatin zymography (P < 0.01). Doxycycline 42-53 matrix metallopeptidase 2 Rattus norvegicus 20-24 19111676-3 2009 It was found that cisplatin provoked (1) the activation (phosphorylation) and internalization of EGFR, (2) the phosphorylation of mitogen-activated protein kinase (MAPK)/p38, (3) the activation of PKC-epsilon, (4) the enhancement of matrix metalloproteinase-2 (MMP-2) expression and activity, (5) the generation of reactive oxygen species (ROS) and (6) the activation of the apoptotic intrinsic pathway. Cisplatin 18-27 matrix metallopeptidase 2 Rattus norvegicus 233-259 19003945-4 2009 In the presence of high glucose, the levels of matrix metalloproteinase-2 (MMP-2), matrix metalloproteinase-9 (MMP-9) and extracellular matrix metalloproteinase inducer (EMMPRIN) were decreased significantly, and the levels of tissue inhibitor of metalloproteinase-2 (TIMP-2), tissue inhibitor of metalloproteinase-1 (TIMP-1) and plasminogen activator inhibitor-1 (PAI-1) were increased significantly. Glucose 24-31 matrix metallopeptidase 2 Rattus norvegicus 47-73 19111676-7 2009 In conclusion, these findings supported a model in which cisplatin provokes an oxidant-induced MMP-2-dependent EGFR transactivation responsible for the induction of cell apoptosis, a process ascribable to the intracellular signalling of PKC-epsilon and MAPK/p38. Cisplatin 57-66 matrix metallopeptidase 2 Rattus norvegicus 95-100 19111676-3 2009 It was found that cisplatin provoked (1) the activation (phosphorylation) and internalization of EGFR, (2) the phosphorylation of mitogen-activated protein kinase (MAPK)/p38, (3) the activation of PKC-epsilon, (4) the enhancement of matrix metalloproteinase-2 (MMP-2) expression and activity, (5) the generation of reactive oxygen species (ROS) and (6) the activation of the apoptotic intrinsic pathway. Cisplatin 18-27 matrix metallopeptidase 2 Rattus norvegicus 261-266 19294534-2 2009 Matrix metalloproteinases (MMPs) can get activated by ROS and contribute to loss of myocardial contractile function in oxidative stress injury. Reactive Oxygen Species 54-57 matrix metallopeptidase 2 Rattus norvegicus 27-31 19111676-6 2009 Finally, when the cisplatin-induced ROS generation was blocked by using NAD(P)H oxidase inhibitors, a decrease in cisplatin-induced MMP-2 enhancement, MAPK/p38 and EGFR activation, and caspase-7 proteolysis occurred. Cisplatin 18-27 matrix metallopeptidase 2 Rattus norvegicus 132-137 19111676-6 2009 Finally, when the cisplatin-induced ROS generation was blocked by using NAD(P)H oxidase inhibitors, a decrease in cisplatin-induced MMP-2 enhancement, MAPK/p38 and EGFR activation, and caspase-7 proteolysis occurred. Reactive Oxygen Species 36-39 matrix metallopeptidase 2 Rattus norvegicus 132-137 19292920-0 2009 Gamma-linolenic acid inhibits both tumour cell cycle progression and angiogenesis in the orthotopic C6 glioma model through changes in VEGF, Flt1, ERK1/2, MMP2, cyclin D1, pRb, p53 and p27 protein expression. gamma-Linolenic Acid 0-20 matrix metallopeptidase 2 Rattus norvegicus 155-159 19294534-3 2009 Previously we have shown that either a MMP-2 inhibitor doxycycline or an antioxidant selenium treatment in vivo prevented diabetes-induced cardiac dysfunction significantly. Doxycycline 55-66 matrix metallopeptidase 2 Rattus norvegicus 39-44 19320892-11 2009 The levels of matrix metalloproteases (MMP-2 and MMP-9) decreased in the propranolol- and atenolol-treated animals. Propranolol 73-84 matrix metallopeptidase 2 Rattus norvegicus 39-44 19462901-11 2009 CONCLUSION: The captopril and losartan induced attenuation of PAH and pulmonary vascular remodeling is likely to be associated with the regulation of the expressions of MMP-2, 9, TIMP-1. Captopril 16-25 matrix metallopeptidase 2 Rattus norvegicus 169-177 19462901-11 2009 CONCLUSION: The captopril and losartan induced attenuation of PAH and pulmonary vascular remodeling is likely to be associated with the regulation of the expressions of MMP-2, 9, TIMP-1. Losartan 30-38 matrix metallopeptidase 2 Rattus norvegicus 169-177 19462901-0 2009 [Changes of MMP-2,9 and TIMP-1 expressions in rats with pulmonary arterial hypertension after captopril and losartan interventions]. Captopril 94-103 matrix metallopeptidase 2 Rattus norvegicus 12-19 19462901-0 2009 [Changes of MMP-2,9 and TIMP-1 expressions in rats with pulmonary arterial hypertension after captopril and losartan interventions]. Losartan 108-116 matrix metallopeptidase 2 Rattus norvegicus 12-19 19462901-1 2009 OBJECTIVE: To determine the effect of captopril and losartan on the expressions of matrix metalloproteinase-2,9 (MMP-2,9) and metalloproteinase-1 (TIMP-1) in rats with pulmonary arterial hypertension, and the mechanisms of captopril and losartan in intervening the development of pulmonary arterial hypertension. Captopril 38-47 matrix metallopeptidase 2 Rattus norvegicus 83-111 19462901-1 2009 OBJECTIVE: To determine the effect of captopril and losartan on the expressions of matrix metalloproteinase-2,9 (MMP-2,9) and metalloproteinase-1 (TIMP-1) in rats with pulmonary arterial hypertension, and the mechanisms of captopril and losartan in intervening the development of pulmonary arterial hypertension. Captopril 38-47 matrix metallopeptidase 2 Rattus norvegicus 113-120 19462901-1 2009 OBJECTIVE: To determine the effect of captopril and losartan on the expressions of matrix metalloproteinase-2,9 (MMP-2,9) and metalloproteinase-1 (TIMP-1) in rats with pulmonary arterial hypertension, and the mechanisms of captopril and losartan in intervening the development of pulmonary arterial hypertension. Losartan 52-60 matrix metallopeptidase 2 Rattus norvegicus 83-111 19462901-1 2009 OBJECTIVE: To determine the effect of captopril and losartan on the expressions of matrix metalloproteinase-2,9 (MMP-2,9) and metalloproteinase-1 (TIMP-1) in rats with pulmonary arterial hypertension, and the mechanisms of captopril and losartan in intervening the development of pulmonary arterial hypertension. Losartan 52-60 matrix metallopeptidase 2 Rattus norvegicus 113-120 19320892-11 2009 The levels of matrix metalloproteases (MMP-2 and MMP-9) decreased in the propranolol- and atenolol-treated animals. Atenolol 90-98 matrix metallopeptidase 2 Rattus norvegicus 39-44 19178771-11 2009 CONCLUSIONS: FDP-Sr or testosterone propionate significantly normalized expression and activity of the MMPs-TIMPs system to attenuate changes in serum testosterone, marker enzymes and histology in testis. Testosterone Propionate 23-46 matrix metallopeptidase 2 Rattus norvegicus 103-107 19259351-0 2009 Early and late changes of MMP-2 and MMP-9 in bleomycin-induced pulmonary fibrosis. Bleomycin 45-54 matrix metallopeptidase 2 Rattus norvegicus 26-31 19259351-3 2009 MATERIALS AND METHODS: The level of MMPs in BAL fluid of 54 bleomycin-treated rats was assessed by zymography from 1 to 28 days after intratracheal bleomycin instillation. Bleomycin 60-69 matrix metallopeptidase 2 Rattus norvegicus 36-40 19259351-3 2009 MATERIALS AND METHODS: The level of MMPs in BAL fluid of 54 bleomycin-treated rats was assessed by zymography from 1 to 28 days after intratracheal bleomycin instillation. Bleomycin 148-157 matrix metallopeptidase 2 Rattus norvegicus 36-40 19259351-5 2009 RESULTS: MMP-2 and MMP-9 were markedly increased in both the BAL fluid and in the lung parenchyma of the bleomycin-treated rats, especially in the early phase with the peak on the 4th day. Bleomycin 105-114 matrix metallopeptidase 2 Rattus norvegicus 9-14 19259351-9 2009 CONCLUSION: In bleomycin-induced pulmonary fibrosis, MMP-2 and MMP-9 may play important roles, especially in the early phase. Bleomycin 15-24 matrix metallopeptidase 2 Rattus norvegicus 53-58 19052882-3 2009 Marked increases in GST-P 7-7-positive PNL development, PCNA labeling indices, MMP-2 (pro, intermediate and active forms) and pro-MMP-9 activity were observed after proliferative stimulus induced by 2-acetylaminofluorene (2-AAF) exposure cycles. 2-Acetylaminofluorene 199-220 matrix metallopeptidase 2 Rattus norvegicus 79-84 19178771-11 2009 CONCLUSIONS: FDP-Sr or testosterone propionate significantly normalized expression and activity of the MMPs-TIMPs system to attenuate changes in serum testosterone, marker enzymes and histology in testis. Testosterone 23-35 matrix metallopeptidase 2 Rattus norvegicus 103-107 19173736-11 2009 Consistent with suppression in ECM proteolysis with tamoxifen treatment, matrix metalloproteinase-2 levels and activity were decreased. Tamoxifen 52-61 matrix metallopeptidase 2 Rattus norvegicus 73-99 21186625-0 2009 [The expression of matrix metalloproteinase-2,9 on atherosclerosis in experimental rats by treatment of 2,3,4",5-tetrahydroxystilbene -2-0-beta-D glucoside]. 2,3,4",5-tetrahydroxystilbene -2-0-beta-d glucoside 104-155 matrix metallopeptidase 2 Rattus norvegicus 19-45 21186625-1 2009 AIM: To observe the changes of MMP-2, 9 level on atherosclerosis in experimental rats by treatment of 2,3,4",5-tetrahydroxystilbene-2-0-beta-D glucoside (TSG) and to investigate the mechanism of TSG in stabilizing plaque and anti-atherosclerosis. 2,3,4",5-tetrahydroxystilbene-2-0-beta-d glucoside 102-152 matrix metallopeptidase 2 Rattus norvegicus 31-36 21186625-1 2009 AIM: To observe the changes of MMP-2, 9 level on atherosclerosis in experimental rats by treatment of 2,3,4",5-tetrahydroxystilbene-2-0-beta-D glucoside (TSG) and to investigate the mechanism of TSG in stabilizing plaque and anti-atherosclerosis. tsg 154-157 matrix metallopeptidase 2 Rattus norvegicus 31-36 19023275-9 2009 Treatment with 17beta-estradiol (E(2)), tempol, or aminoguanidine for 6 weeks prevented Ovx-induced blood pressure elevation and apparently reversed the MMPs changes. Estradiol 15-31 matrix metallopeptidase 2 Rattus norvegicus 153-157 19023275-9 2009 Treatment with 17beta-estradiol (E(2)), tempol, or aminoguanidine for 6 weeks prevented Ovx-induced blood pressure elevation and apparently reversed the MMPs changes. tempol 40-46 matrix metallopeptidase 2 Rattus norvegicus 153-157 19023275-9 2009 Treatment with 17beta-estradiol (E(2)), tempol, or aminoguanidine for 6 weeks prevented Ovx-induced blood pressure elevation and apparently reversed the MMPs changes. pimagedine 51-65 matrix metallopeptidase 2 Rattus norvegicus 153-157 18772236-9 2009 Sorbinil treatment also decreased the expression of TNF-alpha, matrix metalloproteinase-2, matrix metalloproteinase-9, and increased tissue inhibitor of metalloproteinase-3 in vascular smooth muscle cells treated with HG and in balloon-injured carotid arteries of diabetic rats. sorbinil 0-8 matrix metallopeptidase 2 Rattus norvegicus 63-117 19159581-6 2008 The expression levels of MMP-2 and MMP-9 decreased in the high-glucose-cultured RMC cells and increased in the high-glucose-cultured HK-2 cells, however, adenovirus-mediated transfection of decorin gene reversed all of these changes, and had almost the same effects on reducing the protein expression of TGF-beta 1 collagen type IV, MMP-2, and MMP-9 as anti-TGF-beta 1 antibody. Glucose 63-70 matrix metallopeptidase 2 Rattus norvegicus 25-30 19154928-9 2009 Compared with the saline solution injection group, tannic acid treatment inhibited the matrix metalloproteinase-2/-9 activity and increased the collagen content at the early post-myocardial infarction stage (48.6 +/- 7.2 vs 37.3 +/- 6 microg/mg dry weight). Tannins 51-62 matrix metallopeptidase 2 Rattus norvegicus 87-116 19159581-6 2008 The expression levels of MMP-2 and MMP-9 decreased in the high-glucose-cultured RMC cells and increased in the high-glucose-cultured HK-2 cells, however, adenovirus-mediated transfection of decorin gene reversed all of these changes, and had almost the same effects on reducing the protein expression of TGF-beta 1 collagen type IV, MMP-2, and MMP-9 as anti-TGF-beta 1 antibody. Glucose 116-123 matrix metallopeptidase 2 Rattus norvegicus 25-30 18806806-7 2008 Gelatin zymography and western blot data indicated that the diabetes-induced alterations in MMP-2 activity and protein level, level of tissue inhibitor of matrix metalloproteinase-4 and loss of troponin I were restored to control levels with doxycycline. Doxycycline 242-253 matrix metallopeptidase 2 Rattus norvegicus 92-97 18930722-2 2008 Because hyperglycemia increase MMPs activities through increased oxidative stress, we hypothesized that antioxidant effects produced by lercanidipine could attenuate the increases in MMP-2 expression/activity in diabetic rats. lercanidipine 136-149 matrix metallopeptidase 2 Rattus norvegicus 31-35 18930722-2 2008 Because hyperglycemia increase MMPs activities through increased oxidative stress, we hypothesized that antioxidant effects produced by lercanidipine could attenuate the increases in MMP-2 expression/activity in diabetic rats. lercanidipine 136-149 matrix metallopeptidase 2 Rattus norvegicus 183-188 18930722-10 2008 Lercandipine attenuated the increases in oxidative stress and in MMP-2 (both P<0.05). lercandipine 0-12 matrix metallopeptidase 2 Rattus norvegicus 65-70 18930722-11 2008 While diabetes induced no major structural changes, it caused a 16-fold increase in the ratio of MMP-2/TIMP-2 mRNA expression, which was completely reversed by lercanidipine (both P<0.001). lercanidipine 160-173 matrix metallopeptidase 2 Rattus norvegicus 97-102 18930722-12 2008 These results show that antioxidant and beneficial vascular effects produced by lercanidipine in diabetic rats are associated with reversion of the imbalance in vascular MMP-2/TIMP-2 expression. lercanidipine 80-93 matrix metallopeptidase 2 Rattus norvegicus 170-175 18806806-8 2008 CONCLUSIONS AND IMPLICATIONS: Our data suggest that these beneficial effects of doxycycline on the mechanical, electrical and biochemical properties of the diabetic rat heart appear, at least in part, to be related to inhibition of MMP activity, implying a role for MMPs in the development of diabetic cardiomyopathy. Doxycycline 80-91 matrix metallopeptidase 2 Rattus norvegicus 266-270 18810485-0 2008 Matrix metallopeptidase 2 activity in tendon regions: effects of mechanical loading exercise associated to anabolic-androgenic steroids. Steroids 127-135 matrix metallopeptidase 2 Rattus norvegicus 0-25 18665442-10 2008 Furthermore, rosiglitazone significantly decreased MMP-2 mRNA expression (0.98 +/- 0.08 vs 0.71 +/- 0.05, P < 0.05), protein expression (0.80 +/- 0.04 vs 0.64 +/- 0.03, P < 0.05) and MMP-2 activity (320 +/- 25% vs 248 +/- 21%, P < 0.05). Rosiglitazone 13-26 matrix metallopeptidase 2 Rattus norvegicus 51-56 18665442-10 2008 Furthermore, rosiglitazone significantly decreased MMP-2 mRNA expression (0.98 +/- 0.08 vs 0.71 +/- 0.05, P < 0.05), protein expression (0.80 +/- 0.04 vs 0.64 +/- 0.03, P < 0.05) and MMP-2 activity (320 +/- 25% vs 248 +/- 21%, P < 0.05). Rosiglitazone 13-26 matrix metallopeptidase 2 Rattus norvegicus 189-194 18665442-11 2008 CONCLUSION: Rosiglitazone significantly inhibited VSMC proliferation, at least in part by inhibiting high glucose-induced G(1)-->S phase transition, PCNA expression and MMP-2 synthesis. Rosiglitazone 12-25 matrix metallopeptidase 2 Rattus norvegicus 172-177 24692823-14 2008 Mean (SD) MMP-2 activity in the silymarin group (57.35 [9.89] mug/mL; P = 0.04) and the PTX group (46.88 [9.56] mug/mL; P = 0.04) was significantly lower than that observed in the control group (232.32 [79.76] mug/mL). Silymarin 32-41 matrix metallopeptidase 2 Rattus norvegicus 10-15 18713279-0 2008 The effects of N-acetylcysteine on the expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase-2 in hepatic fibrosis in bile duct ligated rats. Acetylcysteine 15-31 matrix metallopeptidase 2 Rattus norvegicus 53-130 18929613-7 2008 Oral administration of EHT reduced the levels of alpha-smooth muscle actin (alpha-SMA) and the activity of metalloproteinases (MMPs) in rats injured by treatment with CCl(4). Cefaclor 167-170 matrix metallopeptidase 2 Rattus norvegicus 127-131 18929613-8 2008 In addition, we performed experiments with the rat hepatic stellate cell line HSC-T6 in which we induced the expression of MMP-2 and alpha-SMA with phorbol-12-myristate-13-acetate (PMA). Tetradecanoylphorbol Acetate 148-179 matrix metallopeptidase 2 Rattus norvegicus 123-128 18929613-8 2008 In addition, we performed experiments with the rat hepatic stellate cell line HSC-T6 in which we induced the expression of MMP-2 and alpha-SMA with phorbol-12-myristate-13-acetate (PMA). Tetradecanoylphorbol Acetate 181-184 matrix metallopeptidase 2 Rattus norvegicus 123-128 18713279-3 2008 We investigated the effects of N-acetylcysteine on the expression of matrix metalloproteinase-2 and tissue inhibitor of matrix metalloproteinase-2. Acetylcysteine 31-47 matrix metallopeptidase 2 Rattus norvegicus 69-146 18713279-10 2008 N-acetylcysteine treatment also significantly decreased matrix metalloproteinase-2 activity and normalized tissue inhibitor of matrix metalloproteinase-2 expression. Acetylcysteine 0-16 matrix metallopeptidase 2 Rattus norvegicus 56-82 18713279-10 2008 N-acetylcysteine treatment also significantly decreased matrix metalloproteinase-2 activity and normalized tissue inhibitor of matrix metalloproteinase-2 expression. Acetylcysteine 0-16 matrix metallopeptidase 2 Rattus norvegicus 127-153 18713279-11 2008 CONCLUSION: Collectively, N-acetylcysteine showed inhibition of matrix metalloproteinase-2 expression and activity. Acetylcysteine 26-42 matrix metallopeptidase 2 Rattus norvegicus 64-90 18713279-12 2008 In addition, administration of N-acetylcysteine was associated with downregulation of the expression of tissue inhibitor of matrix metalloproteinase-2 and amelioration of oxidative stress in the liver of bile duct ligated rats. Acetylcysteine 31-47 matrix metallopeptidase 2 Rattus norvegicus 124-150 19050521-13 2008 Cellular proliferation, myofibroblast density, collagen deposition, and active matrix metalloproteinase-2 levels were reduced in the control group compared with the propranolol-treated group 63 days after burning. Propranolol 165-176 matrix metallopeptidase 2 Rattus norvegicus 79-105 19020766-9 2008 Importantly, the inhibitory effect of valsartan on MMP-2 and MMP-9 expression was also confirmed using isolated peritoneal macrophages from a rat AAA model. Valsartan 38-47 matrix metallopeptidase 2 Rattus norvegicus 51-56 19057128-0 2008 Captopril attenuates matrix metalloproteinase-2 and -9 in monocrotaline-induced right ventricular hypertrophy in rats. Captopril 0-9 matrix metallopeptidase 2 Rattus norvegicus 21-54 19057128-2 2008 We investigated the effect of captopril, an ACE inhibitor, on MMP-2 and MMP-9 in monocrotaline-induced right ventricular hypertrophy. Captopril 30-39 matrix metallopeptidase 2 Rattus norvegicus 62-67 19057128-12 2008 MMP-2 and MMP-9 expressions and activities in right ventricles increased significantly in monocrotaline-injected rats and captopril inhibited them. Monocrotaline 90-103 matrix metallopeptidase 2 Rattus norvegicus 0-5 19057128-12 2008 MMP-2 and MMP-9 expressions and activities in right ventricles increased significantly in monocrotaline-injected rats and captopril inhibited them. Captopril 122-131 matrix metallopeptidase 2 Rattus norvegicus 0-5 19057128-13 2008 These findings indicate that captopril attenuates the development of monocrotaline-induced right ventricular hypertrophy in association with inhibition of MMP-2 and MMP-9 in rats. Captopril 29-38 matrix metallopeptidase 2 Rattus norvegicus 155-160 19272247-0 2008 [Influence of pyrrolidine dithiocarbamate (PDTC) on expression of transforming growth factor beta(1), matrix metalloproteinase-2 and tissue inhibitor-1 of metalloproteinase in rats with pulmonary damage induced by paraquat]. pyrrolidine dithiocarbamic acid 14-41 matrix metallopeptidase 2 Rattus norvegicus 102-128 18792988-2 2008 Here we explored whether cocaine-primed reinstatement was associated with increased activity of the gelatinases, MMP-2 or MMP-9, in the medial prefrontal cortex (mPFC) or dorsal hippocampus. Cocaine 25-32 matrix metallopeptidase 2 Rattus norvegicus 113-118 18782565-0 2008 Sinomenine ameliorates arthritis via MMPs, TIMPs, and cytokines in rats. sinomenine 0-10 matrix metallopeptidase 2 Rattus norvegicus 37-41 18782565-5 2008 Sinomenine suppressed the production of proinflammatory cytokines IL-1beta and IL-6 in serum, inhibited the protein expressions and activities of MMP-2 and MMP-9, and elevated the protein expressions and activities of TIMP-1 and TIMP-3 in rat paw tissues. sinomenine 0-10 matrix metallopeptidase 2 Rattus norvegicus 146-151 18931819-6 2008 Treatment with physiological doses of dihydrotestosterone (25 mg topically) and estrogen (5 microg/0.1 ml subcutaneously) restored the antioxidant levels significantly (p < 0.05) and reduced the levels of TNF-alpha and MMP-2, with estrogen exhibiting a higher potency. Dihydrotestosterone 38-57 matrix metallopeptidase 2 Rattus norvegicus 222-227 18624955-3 2008 We, herein, investigated whether melatonin would ameliorate MMP-2 and MMP-9 activation and expression in a rat model of transient focal cerebral ischemia. Melatonin 33-42 matrix metallopeptidase 2 Rattus norvegicus 60-65 19080331-9 2008 In cultured adventitial fibroblasts isolated from rat aorta, 100 micromol/L L-homocysteine (L-Hcy) significantly down-regulated matrix metalloproteinase-2 activity by 43% as determined by in vitro gelatin zymography (P < 0.05) and up-regulated the expression of collagen type I by 187% (P < 0.05) assessed by Western blotting. Homocysteine 76-90 matrix metallopeptidase 2 Rattus norvegicus 128-154 19080331-9 2008 In cultured adventitial fibroblasts isolated from rat aorta, 100 micromol/L L-homocysteine (L-Hcy) significantly down-regulated matrix metalloproteinase-2 activity by 43% as determined by in vitro gelatin zymography (P < 0.05) and up-regulated the expression of collagen type I by 187% (P < 0.05) assessed by Western blotting. Homocysteine 92-97 matrix metallopeptidase 2 Rattus norvegicus 128-154 18782572-8 2008 To investigate the mechanism by which cordycepin inhibits the remodeling of the vessel wall and/or the accumulation of cells and ECM, we examined the activation of MMP systems in collagen type I-activated RaoSMCs. cordycepin 38-48 matrix metallopeptidase 2 Rattus norvegicus 164-167 18782572-9 2008 Cordycepin markedly inhibited the activation of MMP-2 and -9 as well as the expression of extracellular matrix metalloproteinase inducer (EMMPRIN) in a dose-dependent manner in collagen type I-activated RaoSMCs. cordycepin 0-10 matrix metallopeptidase 2 Rattus norvegicus 48-60 19021703-1 2008 BACKGROUND: The study was performed to determine whether sucrose-induced insulin resistance could increase the expression of cardiac matrix metalloproteinases (MMPs), indices of matrix remodelling, and whether the addition of 1.25 g day(-1) of L-arginine (ARG) to a sucrose diet could prevent both the sucrose-induced metabolic abnormalities and elevated cardiac expression of matrix metalloproteinases in an insulin resistant stage that precedes frank type 2 diabetes. Sucrose 57-64 matrix metallopeptidase 2 Rattus norvegicus 160-164 18846337-12 2008 ATRA treatment increased the protein levels of MMP2 and MMP13. Tretinoin 0-4 matrix metallopeptidase 2 Rattus norvegicus 47-51 18846337-15 2008 It was concluded that ATRA could inhibit CBDL-induced liver fibrosis in rats by suppressing the expression of TGF-beta1 and CTGF so as to diminish the inhibition of TIMP-1 on MMP2 and MMP13 and increase the activity of MMP2 and MMP13. Tretinoin 22-26 matrix metallopeptidase 2 Rattus norvegicus 175-179 18846337-15 2008 It was concluded that ATRA could inhibit CBDL-induced liver fibrosis in rats by suppressing the expression of TGF-beta1 and CTGF so as to diminish the inhibition of TIMP-1 on MMP2 and MMP13 and increase the activity of MMP2 and MMP13. Tretinoin 22-26 matrix metallopeptidase 2 Rattus norvegicus 219-223 18846337-15 2008 It was concluded that ATRA could inhibit CBDL-induced liver fibrosis in rats by suppressing the expression of TGF-beta1 and CTGF so as to diminish the inhibition of TIMP-1 on MMP2 and MMP13 and increase the activity of MMP2 and MMP13. cbdl 41-45 matrix metallopeptidase 2 Rattus norvegicus 219-223 19272247-0 2008 [Influence of pyrrolidine dithiocarbamate (PDTC) on expression of transforming growth factor beta(1), matrix metalloproteinase-2 and tissue inhibitor-1 of metalloproteinase in rats with pulmonary damage induced by paraquat]. pyrrolidine dithiocarbamic acid 43-47 matrix metallopeptidase 2 Rattus norvegicus 102-128 19272247-1 2008 OBJECTIVE: To investigate the influence of pyrrolidine dithiocarbamate (PDTC) on the expression of transforming growth factor beta(1) (TGF-beta(1)), matrix metalloproteinase-2 (MMP-2) and tissue inhibitor-1 of metalloproteinase (TIMP-1) in rats with pulmonary damage induced by paraquat (PQ). pyrrolidine dithiocarbamic acid 43-70 matrix metallopeptidase 2 Rattus norvegicus 149-175 19272247-1 2008 OBJECTIVE: To investigate the influence of pyrrolidine dithiocarbamate (PDTC) on the expression of transforming growth factor beta(1) (TGF-beta(1)), matrix metalloproteinase-2 (MMP-2) and tissue inhibitor-1 of metalloproteinase (TIMP-1) in rats with pulmonary damage induced by paraquat (PQ). pyrrolidine dithiocarbamic acid 43-70 matrix metallopeptidase 2 Rattus norvegicus 177-182 19272247-1 2008 OBJECTIVE: To investigate the influence of pyrrolidine dithiocarbamate (PDTC) on the expression of transforming growth factor beta(1) (TGF-beta(1)), matrix metalloproteinase-2 (MMP-2) and tissue inhibitor-1 of metalloproteinase (TIMP-1) in rats with pulmonary damage induced by paraquat (PQ). pyrrolidine dithiocarbamic acid 72-76 matrix metallopeptidase 2 Rattus norvegicus 149-175 19272247-1 2008 OBJECTIVE: To investigate the influence of pyrrolidine dithiocarbamate (PDTC) on the expression of transforming growth factor beta(1) (TGF-beta(1)), matrix metalloproteinase-2 (MMP-2) and tissue inhibitor-1 of metalloproteinase (TIMP-1) in rats with pulmonary damage induced by paraquat (PQ). pyrrolidine dithiocarbamic acid 72-76 matrix metallopeptidase 2 Rattus norvegicus 177-182 19272247-6 2008 RESULTS: The TGF-beta(1) protein, TGF-beta(1) and MMP-2 mRNA expression were increased significantly in the earlier stage and then decreased after PQ administration (P < 0.05 or P < 0.01), while the mRNA level of TIMP-1 was augmented continuously (P < 0.01) throughout the study compared to the control group. Paraquat 147-149 matrix metallopeptidase 2 Rattus norvegicus 50-55 19272247-8 2008 CONCLUSION: PDTC could attenuate paraquat-induced up-regulation of TGF-beta(1) and its mRNA expression, MMP-2 and TIMP-1 mRNA levels, which indicates that PDTC may exert its protective effects on paraquat-induced pulmonary damage by alleviating the earlier inflammation damage and adjust-ing the balance between MMPs and TIMPs. Paraquat 33-41 matrix metallopeptidase 2 Rattus norvegicus 104-109 19272247-8 2008 CONCLUSION: PDTC could attenuate paraquat-induced up-regulation of TGF-beta(1) and its mRNA expression, MMP-2 and TIMP-1 mRNA levels, which indicates that PDTC may exert its protective effects on paraquat-induced pulmonary damage by alleviating the earlier inflammation damage and adjust-ing the balance between MMPs and TIMPs. Paraquat 33-41 matrix metallopeptidase 2 Rattus norvegicus 312-316 18664596-2 2008 Four hours of insulin infusion (4.8 mU.kg(-1).min(-1)) without or with lipid-heparin infusion (to produce insulin resistance) decreased hepatic MMP-2 mRNA (by RT-PCR), pro-MMP-2, MMP-2, MMP-9, and MT1-MMP (all by Western blots) and the gelatinolytic activity of MMP-2 (by gelatin zymography) by approximately 60-80%. Heparin 77-84 matrix metallopeptidase 2 Rattus norvegicus 144-149 18634778-0 2008 Lercanidipine reduces matrix metalloproteinase-2 activity and reverses vascular dysfunction in renovascular hypertensive rats. lercanidipine 0-13 matrix metallopeptidase 2 Rattus norvegicus 22-48 18512095-5 2008 The MMP inhibitors, o-phenanthroline (Phen, 100 microM) or doxycycline (Doxy, 30 microM) an inhibitors of MMPs, were added to the perfusion solution 10 min before ischemia and for the first 10 min of reperfusion. Doxycycline 59-70 matrix metallopeptidase 2 Rattus norvegicus 106-110 18512095-5 2008 The MMP inhibitors, o-phenanthroline (Phen, 100 microM) or doxycycline (Doxy, 30 microM) an inhibitors of MMPs, were added to the perfusion solution 10 min before ischemia and for the first 10 min of reperfusion. Doxycycline 72-76 matrix metallopeptidase 2 Rattus norvegicus 106-110 18806744-9 2008 RESULTS: Zymography revealed an increased activity of MMP 2 in tumors from animals treated with 5-ALA PDT. 5-amino levulinic acid 96-101 matrix metallopeptidase 2 Rattus norvegicus 54-59 18634778-2 2008 Here, we hypothesized that lercanidipine, a calcium channel blocker, could attenuate the increases in oxidative stress and MMP-2 expression/activity in the two-kidney, one-clip (2K-1C) hypertensive rats. lercanidipine 27-40 matrix metallopeptidase 2 Rattus norvegicus 123-128 18634778-12 2008 Lercandipine attenuated 2K-1C-induced increases in MMP-2 by more than 60% and blunted 2K-1C-induced increases in oxidative stress (both P<0.001). lercandipine 0-12 matrix metallopeptidase 2 Rattus norvegicus 51-56 18634778-14 2008 These results suggest that lercanidipine produces antihypertensive effects and reverses the endothelial dysfunction associated with 2K-1C hypertension, probably through mechanisms involving antioxidant effects leading to lower MMP-2 activation. lercanidipine 27-40 matrix metallopeptidase 2 Rattus norvegicus 227-232 18806744-12 2008 In the same time CS reduced MMP 2 activity. Chitosan 17-19 matrix metallopeptidase 2 Rattus norvegicus 28-33 18502086-13 2008 In vein segments under 2 g tension for 24 hours and treated with TIMP-1, Phe, AngII, and KCl contractions were partially restored, suggesting the involvement of MMPs. Potassium Chloride 89-92 matrix metallopeptidase 2 Rattus norvegicus 161-165 18429971-4 2008 However, no reports are available on the relationship between the activity and expression of MMPs and anti-inflammatory effect of melatonin. Melatonin 130-139 matrix metallopeptidase 2 Rattus norvegicus 93-97 18429971-5 2008 The aim of the present study was to evaluate whether melatonin prevents the experimental colitis in rats by regulating MMP-9 and MMP-2 activity and expression. Melatonin 53-62 matrix metallopeptidase 2 Rattus norvegicus 129-134 18429971-8 2008 Biochemical methods and zymography were used to analyse MMP-9 and MMP-2 activities in colon tissues from DNBS-injured rats. 2,4-dinitrofluorobenzene sulfonic acid 105-109 matrix metallopeptidase 2 Rattus norvegicus 66-71 18429971-10 2008 Melatonin also reduced proMMP-9 and MMP-2 activities that were induced in the colon tissues by DNBS administration. Melatonin 0-9 matrix metallopeptidase 2 Rattus norvegicus 36-41 18429971-10 2008 Melatonin also reduced proMMP-9 and MMP-2 activities that were induced in the colon tissues by DNBS administration. 2,4-dinitrofluorobenzene sulfonic acid 95-99 matrix metallopeptidase 2 Rattus norvegicus 36-41 18429971-12 2008 We conclude that melatonin"s ability to reduce DNBS-induced colon injury in rats is related to a reduction in proMMP-9 and MMP-2 activities and expression. Melatonin 17-26 matrix metallopeptidase 2 Rattus norvegicus 123-128 18429971-12 2008 We conclude that melatonin"s ability to reduce DNBS-induced colon injury in rats is related to a reduction in proMMP-9 and MMP-2 activities and expression. 2,4-dinitrofluorobenzene sulfonic acid 47-51 matrix metallopeptidase 2 Rattus norvegicus 123-128 18953089-10 2008 The treatment of animals subjected to HI with 1-methylnicotinamide (MNA), the anti-inflammatory agent, led to the inhibition of MMP-9 in an acute phase of ischemic damage and to the activation of MMP-2 in the later stages after injury. hi 38-40 matrix metallopeptidase 2 Rattus norvegicus 196-201 18953089-10 2008 The treatment of animals subjected to HI with 1-methylnicotinamide (MNA), the anti-inflammatory agent, led to the inhibition of MMP-9 in an acute phase of ischemic damage and to the activation of MMP-2 in the later stages after injury. N(1)-methylnicotinamide 46-66 matrix metallopeptidase 2 Rattus norvegicus 196-201 18953089-10 2008 The treatment of animals subjected to HI with 1-methylnicotinamide (MNA), the anti-inflammatory agent, led to the inhibition of MMP-9 in an acute phase of ischemic damage and to the activation of MMP-2 in the later stages after injury. N(1)-methylnicotinamide 68-71 matrix metallopeptidase 2 Rattus norvegicus 196-201 18668563-10 2008 Treatment of FLS from DA rats with an MMP-2 inhibitor reduced cell invasion to a level similar to that in DA.F344(Cia5d) rats, demonstrating that MMP-2 activity accounted for the difference between FLS from these 2 strains. CHEMBL1232769 13-16 matrix metallopeptidase 2 Rattus norvegicus 38-43 18502086-18 2008 Both MMP-2 and MMP-9 caused significant inhibition of Phe contraction in IVC segments. Phenylephrine 54-57 matrix metallopeptidase 2 Rattus norvegicus 5-10 18509851-4 2008 The influence of distinct classes of antidepressants, namely, electroconvulsive seizure, fluoxetine, tranylcypromine, and desipramine, on the gene expression of MMP-2, MMP-9, and TIMPs 1-4 in the hippocampus was determined using radioactive in situ hybridization. Fluoxetine 89-99 matrix metallopeptidase 2 Rattus norvegicus 161-166 18509851-4 2008 The influence of distinct classes of antidepressants, namely, electroconvulsive seizure, fluoxetine, tranylcypromine, and desipramine, on the gene expression of MMP-2, MMP-9, and TIMPs 1-4 in the hippocampus was determined using radioactive in situ hybridization. Tranylcypromine 101-116 matrix metallopeptidase 2 Rattus norvegicus 161-166 18509851-4 2008 The influence of distinct classes of antidepressants, namely, electroconvulsive seizure, fluoxetine, tranylcypromine, and desipramine, on the gene expression of MMP-2, MMP-9, and TIMPs 1-4 in the hippocampus was determined using radioactive in situ hybridization. Desipramine 122-133 matrix metallopeptidase 2 Rattus norvegicus 161-166 18050056-2 2008 The aim of this study was to investigate MMP-2 activity in gastrocnemius, soleus, extensor digitorium longus (EDL) and tibialis anterior (TA) muscles after exercise associated with an anabolic androgenic steroid (AAS). Steroids 204-211 matrix metallopeptidase 2 Rattus norvegicus 41-46 18596315-2 2008 We have previously demonstrated that MMP-2 expression correlates with increased inducible nitric oxide synthase (iNOS) production in the stomach and that iNOS is upregulated in the postischemic gut by the luminal nutrient arginine and repressed by luminal glutamine. Glutamine 256-265 matrix metallopeptidase 2 Rattus norvegicus 37-42 18596315-3 2008 We therefore hypothesized that arginine would enhance expression of MMP-2 in the postischemic gut. Arginine 31-39 matrix metallopeptidase 2 Rattus norvegicus 68-73 18596315-7 2008 Arginine maintained while glutamine inhibited the increase in iNOS, MT1-MMP, and MMP-2 expression in the postischemic gut. Glutamine 26-35 matrix metallopeptidase 2 Rattus norvegicus 81-86 18596315-8 2008 Pretreatment of the arginine group with a selective iNOS inhibitor blunted the induction of MMP-2 in the postischemic gut. Arginine 20-28 matrix metallopeptidase 2 Rattus norvegicus 92-97 18596315-10 2008 CONCLUSIONS: The arginine-induced upregulation of iNOS may contribute to increased activity of MT1-MMP and MMP-2. Arginine 17-25 matrix metallopeptidase 2 Rattus norvegicus 107-112 18347835-8 2008 Six weeks (w) after STZ-injection, MMP-2 mRNA expression and pro-MMP-2 levels were 2.7-fold (P < 0.005) and 1.3-fold (P < 0.05) reduced versus controls, respectively, whereas active MMP-2 was decreased to undetectable levels 6 w post-STZ. Streptozocin 20-23 matrix metallopeptidase 2 Rattus norvegicus 35-40 18347835-8 2008 Six weeks (w) after STZ-injection, MMP-2 mRNA expression and pro-MMP-2 levels were 2.7-fold (P < 0.005) and 1.3-fold (P < 0.05) reduced versus controls, respectively, whereas active MMP-2 was decreased to undetectable levels 6 w post-STZ. Streptozocin 20-23 matrix metallopeptidase 2 Rattus norvegicus 65-70 18347835-8 2008 Six weeks (w) after STZ-injection, MMP-2 mRNA expression and pro-MMP-2 levels were 2.7-fold (P < 0.005) and 1.3-fold (P < 0.05) reduced versus controls, respectively, whereas active MMP-2 was decreased to undetectable levels 6 w post-STZ. Streptozocin 20-23 matrix metallopeptidase 2 Rattus norvegicus 65-70 18347835-8 2008 Six weeks (w) after STZ-injection, MMP-2 mRNA expression and pro-MMP-2 levels were 2.7-fold (P < 0.005) and 1.3-fold (P < 0.05) reduced versus controls, respectively, whereas active MMP-2 was decreased to undetectable levels 6 w post-STZ. Streptozocin 240-243 matrix metallopeptidase 2 Rattus norvegicus 35-40 18935914-9 2008 L-NAME administration for 5 to 10 days resulted in decreases in MMP2 and MMP9 with increasing TIMP2. NG-Nitroarginine Methyl Ester 0-6 matrix metallopeptidase 2 Rattus norvegicus 64-68 18799821-6 2008 L-thyroxin treatment resulted in increased mRNA expression and MMP-2 and MMP-9 activities, along with decreased TIMP-1 and TIMP-2 mRNA expression. Thyroxine 0-10 matrix metallopeptidase 2 Rattus norvegicus 63-68 18935914-10 2008 After L-NAME for 15 days, opposite changes (increases in MMP2 and MMP9 with a decrease in TIMP2) were observed. NG-Nitroarginine Methyl Ester 6-12 matrix metallopeptidase 2 Rattus norvegicus 57-61 18935914-11 2008 FR139317 cotreatment ameliorated the L-NAME-induced changes in MMP2 and MMP9 throughout the 30-day observation period. NG-Nitroarginine Methyl Ester 37-43 matrix metallopeptidase 2 Rattus norvegicus 63-67 18054360-14 2008 Our results suggest that MMP-2 plays a role in 2K-1C hypertension and its structural and functional vascular changes, which were attenuated by doxycycline. Doxycycline 143-154 matrix metallopeptidase 2 Rattus norvegicus 25-30 18493299-10 2008 Over-expression of calpain-1 in young VSMC results in cleavage of intact vimentin, and an increased migratory capacity mimicking that of old VSMC, which is blocked by the MMP inhibitor, GM6001. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 186-192 matrix metallopeptidase 2 Rattus norvegicus 171-174 18583228-8 2008 RESULTS: Both perindopril and losartan treatment significantly reduced the pulmonary fibrosis score, content of hydroxyproline, protein expression of TGF-beta1, DNA binding activity of NF-kappaB and MMP-2, 9 activity, and increased cytoplasmic protein expression of IkappaBalpha. Perindopril 14-25 matrix metallopeptidase 2 Rattus norvegicus 199-204 18583228-8 2008 RESULTS: Both perindopril and losartan treatment significantly reduced the pulmonary fibrosis score, content of hydroxyproline, protein expression of TGF-beta1, DNA binding activity of NF-kappaB and MMP-2, 9 activity, and increased cytoplasmic protein expression of IkappaBalpha. Losartan 30-38 matrix metallopeptidase 2 Rattus norvegicus 199-204 18583228-10 2008 CONCLUSION: Perindopril and losartan may inhibit bleomycin A5-induced pulmonary fibrosis in rats by reducing the protein expression of TGF-beta1 and suppressing the DNA binding activity of NF-kappaB and MMP-2, 9 activity. Perindopril 12-23 matrix metallopeptidase 2 Rattus norvegicus 203-208 18583228-10 2008 CONCLUSION: Perindopril and losartan may inhibit bleomycin A5-induced pulmonary fibrosis in rats by reducing the protein expression of TGF-beta1 and suppressing the DNA binding activity of NF-kappaB and MMP-2, 9 activity. Losartan 28-36 matrix metallopeptidase 2 Rattus norvegicus 203-208 18583228-10 2008 CONCLUSION: Perindopril and losartan may inhibit bleomycin A5-induced pulmonary fibrosis in rats by reducing the protein expression of TGF-beta1 and suppressing the DNA binding activity of NF-kappaB and MMP-2, 9 activity. bleomycetin 49-61 matrix metallopeptidase 2 Rattus norvegicus 203-208 21141515-1 2008 AIM: To observe the effects of inulicin on the neointimal hyperplasia and expression of matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) after balloon injury in rat aorta. inulicin 31-39 matrix metallopeptidase 2 Rattus norvegicus 88-114 18403593-0 2008 The benefit of docosahexanoic acid on the migration of vascular smooth muscle cells is partially dependent on Notch regulation of MMP-2/-9. Docosahexaenoic Acids 15-34 matrix metallopeptidase 2 Rattus norvegicus 130-138 18374903-6 2008 We have therefore intended to investigate the induction and expression of MMPs with special emphasis on the regulation of MMPs by dexamethasone and antibiotics in therapy of pneumococcal meningitis. Dexamethasone 130-143 matrix metallopeptidase 2 Rattus norvegicus 74-78 18374903-6 2008 We have therefore intended to investigate the induction and expression of MMPs with special emphasis on the regulation of MMPs by dexamethasone and antibiotics in therapy of pneumococcal meningitis. Dexamethasone 130-143 matrix metallopeptidase 2 Rattus norvegicus 122-126 18415800-0 2008 Plasma concentrations of matrix metalloproteinase-2, tissue inhibitor of metalloproteinase-1 and osteopontin reflect severity of heart failure in DOCA-salt hypertensive rat. Desoxycorticosterone Acetate 146-150 matrix metallopeptidase 2 Rattus norvegicus 25-92 18415800-0 2008 Plasma concentrations of matrix metalloproteinase-2, tissue inhibitor of metalloproteinase-1 and osteopontin reflect severity of heart failure in DOCA-salt hypertensive rat. Salts 151-155 matrix metallopeptidase 2 Rattus norvegicus 25-92 18415800-3 2008 In this study the effect of spironolactone treatment on plasma MMP-2, TIMP-1 and OPN levels was assessed in a heart failure animal model. Spironolactone 28-42 matrix metallopeptidase 2 Rattus norvegicus 63-68 18415800-7 2008 DOCA treatment increased plasma MMP-2, TIMP-1 and OPN concentrations. Desoxycorticosterone Acetate 0-4 matrix metallopeptidase 2 Rattus norvegicus 32-37 18415800-10 2008 In DOCA-salt hypertensive rats, plasma concentrations of MMP-2, TIMP-1 and OPN reflected heart failure associated with haemodynamic, functional and morphological changes. Desoxycorticosterone Acetate 3-7 matrix metallopeptidase 2 Rattus norvegicus 57-62 18415800-10 2008 In DOCA-salt hypertensive rats, plasma concentrations of MMP-2, TIMP-1 and OPN reflected heart failure associated with haemodynamic, functional and morphological changes. Salts 8-12 matrix metallopeptidase 2 Rattus norvegicus 57-62 18177476-12 2008 These effects were completely abolished by the ET(A) receptor-selective antagonist YM598 (1 micromol/L); however, the ET(B) receptor-selective antagonist BQ-788 (1 micromol/L) and the AVP receptor antagonists YM218 and SR 121463A did not inhibit ET-1-induced inhibition of MMP-2 synthesis and ECM production. N-(6-methoxy-5-(2-methoxyphenoxy)-2-(pyrimidin-2-yl)pyrimidin-4-yl)-2-phenylethenesulfonamide 83-88 matrix metallopeptidase 2 Rattus norvegicus 273-278 18177476-13 2008 In addition, AVP-induced inhibition of MMP-2 synthesis and ECM production were partly inhibited by YM598. N-(6-methoxy-5-(2-methoxyphenoxy)-2-(pyrimidin-2-yl)pyrimidin-4-yl)-2-phenylethenesulfonamide 99-104 matrix metallopeptidase 2 Rattus norvegicus 39-44 19099751-0 2008 [Retinoic acid diminished the expression of lung tissue matrix metalloproteinase-2 and matrix metalloproteinase-9 in hyperoxia-exposed premature rats through regulating mitogen-activated protein kinases]. Tretinoin 1-14 matrix metallopeptidase 2 Rattus norvegicus 56-113 19099751-9 2008 RESULTS: Exposure to oxygen for 4 d, 7 d, and 14 d resulted in increased mRNA levels of MMP-2 and MMP-9 compared with air-exposed control group (P < 0.01 for all). Oxygen 21-27 matrix metallopeptidase 2 Rattus norvegicus 88-93 19099751-10 2008 The mean protein levels of active MMP-2 and pro/active MMP-9 after exposure to O2 were higher than air control groups on each experimental day (P < 0.01 or < 0.05). Oxygen 79-81 matrix metallopeptidase 2 Rattus norvegicus 34-39 19099751-12 2008 The pups treated with RA in the hyperoxic environment expressed significantly lower mRNA levels of MMP-2 and MMP-9 than the hyperoxic control pups on each experimental day (P < 0.05 for all). Tretinoin 22-24 matrix metallopeptidase 2 Rattus norvegicus 99-104 19099751-13 2008 The levels of active MMP-2 and pro/active MMP-9 decreased to a different degree after RA treatment in hyperoxia exposure rat pups. Tretinoin 86-88 matrix metallopeptidase 2 Rattus norvegicus 21-26 19099751-15 2008 CONCLUSION: Hyperoxia exposure elevated the expression of MMP-2 and MMP-9 markedly, which played a role in oxygen-induced lung injury. Oxygen 107-113 matrix metallopeptidase 2 Rattus norvegicus 58-63 19099751-16 2008 RA could have a protective effect on hyperoxia induced lung injury by decreasing active levels of JNK and p38, which subsequently reduce the expression and activation of MMP-2 and MMP-9. Tretinoin 0-2 matrix metallopeptidase 2 Rattus norvegicus 170-175 21141515-6 2008 The proteolytic activity and the expression of MMP-2 and ratio of MMP-2 and TIMP-2 were also returned to control level by inulicin after balloon injury. inulicin 122-130 matrix metallopeptidase 2 Rattus norvegicus 47-52 21141515-6 2008 The proteolytic activity and the expression of MMP-2 and ratio of MMP-2 and TIMP-2 were also returned to control level by inulicin after balloon injury. inulicin 122-130 matrix metallopeptidase 2 Rattus norvegicus 66-71 21141515-7 2008 CONCLUSION: Inulicin inhibits hyperplasia of neointima by modulating the balance of MMP-2 and TIMP-2. inulicin 12-20 matrix metallopeptidase 2 Rattus norvegicus 84-89 18309148-9 2008 In quantitative polymerase chain reaction and immunohistochemistry, simvastatin significantly inhibited upregulated expression of interleukin-1beta, inducible nitric oxide synthase, matrix metalloproteinase-2, and matrix metalloproteinase-9 associated with CA progression. Simvastatin 68-79 matrix metallopeptidase 2 Rattus norvegicus 182-208 18309148-10 2008 Gelatin zymography revealed decreased activity of matrix metalloproteinase-2 and matrix metalloproteinase-9 in aneurysmal walls by simvastatin treatment. Simvastatin 131-142 matrix metallopeptidase 2 Rattus norvegicus 50-107 18242597-10 2008 LPS caused significantly greater MMP-2 activity in endothelium-intact aortae which was attenuated by doxycycline. Doxycycline 101-112 matrix metallopeptidase 2 Rattus norvegicus 33-38 18255236-8 2008 Finally, we report that pharmacological inhibition of MMPs by N-[(2R)-2-(hydroxamidocarbonyl-methyl)-4-methylpenthanoyl]-L-tryptophan methylamide (GM6001) significantly reduces brain infarct volume induced by transient MCAo. n-[(2r)-2-(hydroxamidocarbonyl-methyl)-4-methylpenthanoyl]-l-tryptophan methylamide 62-145 matrix metallopeptidase 2 Rattus norvegicus 54-58 18257543-0 2008 Carbamoylphosphonate matrix metalloproteinase inhibitors 6: cis-2-aminocyclohexylcarbamoylphosphonic acid, a novel orally active antimetastatic matrix metalloproteinase-2 selective inhibitor--synthesis and pharmacodynamic and pharmacokinetic analysis. carbamoylphosphonate 0-20 matrix metallopeptidase 2 Rattus norvegicus 144-170 18257543-0 2008 Carbamoylphosphonate matrix metalloproteinase inhibitors 6: cis-2-aminocyclohexylcarbamoylphosphonic acid, a novel orally active antimetastatic matrix metalloproteinase-2 selective inhibitor--synthesis and pharmacodynamic and pharmacokinetic analysis. adenosylcobinamide 2-chlorophenyl phosphate 60-105 matrix metallopeptidase 2 Rattus norvegicus 144-170 18255236-8 2008 Finally, we report that pharmacological inhibition of MMPs by N-[(2R)-2-(hydroxamidocarbonyl-methyl)-4-methylpenthanoyl]-L-tryptophan methylamide (GM6001) significantly reduces brain infarct volume induced by transient MCAo. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 147-153 matrix metallopeptidase 2 Rattus norvegicus 54-58 18289020-13 2008 Immunohistochemistry and gelatin zymography showed that the expression and activity of MMP-2 was also reduced by nifedipine. Nifedipine 113-123 matrix metallopeptidase 2 Rattus norvegicus 87-92 18178727-5 2008 Additionally, the substantial increase in MMP-2 activation in the untreated fistula at 1 day was prevented following bosentan treatment (1.6 +/- 0.3 vs. 0.9 +/- 0.1 arbitrary activity units, Fist vs. Fist + Bos, P <or= 0.01). Bosentan 117-125 matrix metallopeptidase 2 Rattus norvegicus 42-47 18352832-8 2008 Inhibitor studies showed that, with an intrathecal injection of SB-3CT (a selective MMP-2/MMP-9 inhibitor), the MMP activity, Evans blue extravasation, and apoptotic cell death decreased after SCI. SB 3CT compound 64-70 matrix metallopeptidase 2 Rattus norvegicus 84-89 18352832-8 2008 Inhibitor studies showed that, with an intrathecal injection of SB-3CT (a selective MMP-2/MMP-9 inhibitor), the MMP activity, Evans blue extravasation, and apoptotic cell death decreased after SCI. SB 3CT compound 64-70 matrix metallopeptidase 2 Rattus norvegicus 84-87 18293166-7 2008 Meanwhile, GW0742 pretreatment exerted inhibition on mRNA expression augmentation of such cytokines as MMP9, MMP2, and IL-1beta in hypertrophic myocytes. GW0742 11-17 matrix metallopeptidase 2 Rattus norvegicus 109-113 17763951-11 2008 In the BDL + enalapril group, MMP-2 was significantly higher than the BDL group at the fourth and sixth weeks. Enalapril 13-22 matrix metallopeptidase 2 Rattus norvegicus 30-35 17763951-11 2008 In the BDL + enalapril group, MMP-2 was significantly higher than the BDL group at the fourth and sixth weeks. N-(biphenyl-4-ylsulfonyl)-D-leucine 7-10 matrix metallopeptidase 2 Rattus norvegicus 30-35 17763951-12 2008 These results suggest that enalapril reduces the liver tissue TGF-beta1 and has an ameliorating effect on the fibrosis markers TGF-beta1 and MMP-2. Enalapril 27-36 matrix metallopeptidase 2 Rattus norvegicus 141-146 18042615-2 2008 We hypothesized that matrix and TBM degradation by metalloproteinases (MMPs) could promote cyst formation. metsulfuron methyl 32-35 matrix metallopeptidase 2 Rattus norvegicus 71-75 18042615-8 2008 Sirolimus treatment leads to decreased protein expression of MMP-2 and MMP-14 in Cy/+, whereas MMP-2 and MMP-14 mRNA levels and TIMP-2 protein levels were not affected by sirolimus. Sirolimus 0-9 matrix metallopeptidase 2 Rattus norvegicus 61-66 18042615-10 2008 Sirolimus treatment was associated with a marked improvement of MMP-2 and MMP-14 overexpression, and this correlated also with less matrix and TBM alterations and milder cystic disease. Sirolimus 0-9 matrix metallopeptidase 2 Rattus norvegicus 64-69 18071296-1 2008 BACKGROUND AND PURPOSE: The potent oxidant peroxynitrite (ONOO(-)) induces mechanical dysfunction in the intact heart in part through activation of matrix metalloproteinase-2 (MMP-2). Peroxynitrous Acid 43-56 matrix metallopeptidase 2 Rattus norvegicus 148-174 18071296-1 2008 BACKGROUND AND PURPOSE: The potent oxidant peroxynitrite (ONOO(-)) induces mechanical dysfunction in the intact heart in part through activation of matrix metalloproteinase-2 (MMP-2). Peroxynitrous Acid 43-56 matrix metallopeptidase 2 Rattus norvegicus 176-181 18071296-1 2008 BACKGROUND AND PURPOSE: The potent oxidant peroxynitrite (ONOO(-)) induces mechanical dysfunction in the intact heart in part through activation of matrix metalloproteinase-2 (MMP-2). onoo(-) 58-65 matrix metallopeptidase 2 Rattus norvegicus 148-174 18071296-1 2008 BACKGROUND AND PURPOSE: The potent oxidant peroxynitrite (ONOO(-)) induces mechanical dysfunction in the intact heart in part through activation of matrix metalloproteinase-2 (MMP-2). onoo(-) 58-65 matrix metallopeptidase 2 Rattus norvegicus 176-181 18071296-10 2008 Myocytes subjected to 300 microM ONOO(-) had a shorter CCT than decomposed ONOO(-) (14.9+1.5 vs 32.2+3.5 min, n=7-8; P<0.05) and showed increased MMP-2 activity. onoo 33-37 matrix metallopeptidase 2 Rattus norvegicus 149-154 18071296-10 2008 Myocytes subjected to 300 microM ONOO(-) had a shorter CCT than decomposed ONOO(-) (14.9+1.5 vs 32.2+3.5 min, n=7-8; P<0.05) and showed increased MMP-2 activity. onoo(-) 33-40 matrix metallopeptidase 2 Rattus norvegicus 149-154 18071296-11 2008 The MMP inhibitors doxycycline (100 microM) or PD 166793 (2 microM) reduced the decline in CCT induced by 300 microM ONOO(-). Doxycycline 19-30 matrix metallopeptidase 2 Rattus norvegicus 4-7 18071296-11 2008 The MMP inhibitors doxycycline (100 microM) or PD 166793 (2 microM) reduced the decline in CCT induced by 300 microM ONOO(-). onoo 117-121 matrix metallopeptidase 2 Rattus norvegicus 4-7 18071296-13 2008 CONCLUSIONS AND IMPLICATIONS: This is the first demonstration that inhibition of MMPs protects the cardiac myocyte from ONOO(-)-induced contractile failure via an action unrelated to proteolysis of extracellular matrix proteins. onoo(-) 120-127 matrix metallopeptidase 2 Rattus norvegicus 81-85 18192847-9 2008 Valsartan/NEPI and ACEI/NEPI increased vascular matrix metalloproteinase-2 activity, and decreased tissue inhibitors of metalloproteinase-2 activity and macrophage infiltration. Valsartan 0-9 matrix metallopeptidase 2 Rattus norvegicus 48-74 18031379-9 2007 In vitro studies using the rat hepatic stellate cell line HSC-T6 using northern blot analysis and zymography, respectively, showed that high concentrations of triiodotyronine (T(3)) enhanced transforming growth factor (TGF)-beta-induced collagen I gene expression, and reduced metalloproteinase (MMP)-2 secretion, implying that reducing the levels of T(3) may contribute to resolution of fibrosis. triiodotyronine 159-174 matrix metallopeptidase 2 Rattus norvegicus 277-302 18097624-0 2008 Ethanol extract from Epimedium brevicornum attenuates left ventricular dysfunction and cardiac remodeling through down-regulating matrix metalloproteinase-2 and -9 activity and myocardial apoptosis in rats with congestive heart failure. Ethanol 0-7 matrix metallopeptidase 2 Rattus norvegicus 130-163 18354258-6 2008 Ang II-induced MMP-2 activation is inhibited by N(G)-nitro-L-arginine and MnTMPyP. Nitroarginine 48-69 matrix metallopeptidase 2 Rattus norvegicus 15-20 17884979-11 2008 Compared with control-fed C+CsA+Cer rats, their ethanol-fed E+CsA+Cer counterparts showed marked increases in pancreatic NF-kappaB activation and cytokine/chemokine mRNA expression, collagen and fibronectin, the expression and activities of matrix metalloproteinase-2 and -9, and activation of pancreatic stellate cells. Ethanol 48-55 matrix metallopeptidase 2 Rattus norvegicus 241-274 18354258-9 2008 CONCLUSIONS: Infusion of Ang II induced vascular expression of VEGF and peroxynitrite-dependent activation of MMP-2, with both effects being prevented by RWPs intake. Peroxynitrous Acid 72-85 matrix metallopeptidase 2 Rattus norvegicus 110-115 18031379-12 2007 This beneficial effect may in part be due to prevention of T(3)-induced stimulation of collagen synthesis and reduction of MMP-2 secretion. Triiodothyronine 59-63 matrix metallopeptidase 2 Rattus norvegicus 123-128 17937863-0 2007 [Effect of triptolide on the expression of matrix metalloproteinases 2 and 9 in lungs of experimental pulmonary hypertension]. triptolide 11-21 matrix metallopeptidase 2 Rattus norvegicus 43-76 17481882-6 2007 Moreover, EGCG markedly attenuated HSC activation as well as matrix metalloproteinase (MMP)-2 activity. epigallocatechin gallate 10-14 matrix metallopeptidase 2 Rattus norvegicus 61-93 17481882-7 2007 In cultured stellate cell, the expression of MMP-2 mRNA and protein were substantially reduced by EGCG treatment. epigallocatechin gallate 98-102 matrix metallopeptidase 2 Rattus norvegicus 45-50 17481882-8 2007 Concanavalin A-induced activation of secreted MMP-2 was inhibited by EGCG through the influence of membrane type 1-MMP activity. epigallocatechin gallate 69-73 matrix metallopeptidase 2 Rattus norvegicus 46-51 18000599-3 2007 We describe the effects of different doses of rt-PA (saline, 0.9, 9, or 18 mg rt-PA/kg body weight) on the MMPs, their specific inhibitors (TIMPs), and also their inducer protein EMMPRIN following experimental cerebral ischemia (3 hours [h], 24 h reperfusion, suture model) in rats. Sodium Chloride 53-59 matrix metallopeptidase 2 Rattus norvegicus 107-111 18251166-9 2007 The positive signals of TGF-beta1, MMP-2 and TIMP-1 were observed more frequently (P<0.05) in the CCl4-treated group compared to those in the IL-10-treated group and the control group. Carbon Tetrachloride 101-105 matrix metallopeptidase 2 Rattus norvegicus 35-40 17670915-8 2007 Increased MMP-2 activity in diabetes was prevented by atrasentan treatment. Atrasentan 54-64 matrix metallopeptidase 2 Rattus norvegicus 10-15 18028129-8 2007 Suppression of ERK1/2 activation with nontoxic concentrations of PD98059, a specific inhibitor of ERK activation, was associated with a reduction of CTGF-stimulated MMP-2 activity and protein expression. 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 65-72 matrix metallopeptidase 2 Rattus norvegicus 165-170 17982970-1 2007 OBJECTIVE: The present study was designed to examine the changes of MMP-2/TIMP-2 in the hearts of streptozotocin-induced diabetic rats and gain insight into their roles in extracellular matrix (ECM) remodelling on an experimental animal model of diabetic cardiomyopathy. Streptozocin 98-112 matrix metallopeptidase 2 Rattus norvegicus 68-73 17854826-0 2007 Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury. Peroxynitrous Acid 78-91 matrix metallopeptidase 2 Rattus norvegicus 0-26 17854826-1 2007 Matrix metalloproteinase (MMP)-2 mediates myocardial ischemia-reperfusion injury which is characterized by enhanced peroxynitrite biosynthesis during early reperfusion. Peroxynitrous Acid 116-129 matrix metallopeptidase 2 Rattus norvegicus 0-32 17854826-11 2007 Cardiac dysfunction induced by peroxynitrite involves degradation of alpha-actinin that may be mediated by the proteolytic action of MMP-2. Peroxynitrous Acid 31-44 matrix metallopeptidase 2 Rattus norvegicus 133-138 17937863-13 2007 CONCLUSIONS: Triptolide attenuates the development of pulmonary hypertention and right ventricular hypertrophy and promotes regression of pulmonary arterial neointimal formation in pneumonectomized rats that received MCT, possibly through an inhibition of MMPs activity. triptolide 13-23 matrix metallopeptidase 2 Rattus norvegicus 256-260 17665443-9 2007 The expression and activity of matrix metalloproteinases 2 and 9, which participate in angiogenesis, was impaired in response to IL-13 as compared with AxCANI and PBS treatment. pbs 163-166 matrix metallopeptidase 2 Rattus norvegicus 31-64 17890296-0 2007 The role of nitric oxide on matrix metalloproteinase 2 (MMP2) and MMP9 in placenta and fetus from diabetic rats. Nitric Oxide 12-24 matrix metallopeptidase 2 Rattus norvegicus 56-60 18037780-8 2007 Pioglitazone did not decrease blood pressure, but partially normalized LV geometry in addition to decreasing myocyte diameter, interstitial fibrosis and number of myofibroblasts; mRNA levels of collagen type I and BNP; MMP2 activity; and protein level of CTGF. Pioglitazone 0-12 matrix metallopeptidase 2 Rattus norvegicus 219-223 17903365-0 2007 [Hypoxia induced by CoCl2 influencing the expression and the activity of matrix metalloproteinase-2 in rat hepatic stellate cells]. cobaltous chloride 20-25 matrix metallopeptidase 2 Rattus norvegicus 73-99 17903365-1 2007 OBJECTIVE: To investigate the effects of hypoxia induced by cobalt chloride on the expression and the activity of matrix metalloproteinase-2 (MMP-2) in rat hepatic stellate cells (HSC-T6) and to clarify the possible mechanisms. cobaltous chloride 60-75 matrix metallopeptidase 2 Rattus norvegicus 114-140 17903365-1 2007 OBJECTIVE: To investigate the effects of hypoxia induced by cobalt chloride on the expression and the activity of matrix metalloproteinase-2 (MMP-2) in rat hepatic stellate cells (HSC-T6) and to clarify the possible mechanisms. cobaltous chloride 60-75 matrix metallopeptidase 2 Rattus norvegicus 142-147 17903365-7 2007 RESULTS: When the concentration of CoCl2 increased from 0 micromol/L to 200 micromol/L, the expressions of MMP-2 mRNA (the rate of light density) were increased from 0.53+0.12 to 1.57+0.11 and the differences among these four groups were significant (F=34.21). cobaltous chloride 35-40 matrix metallopeptidase 2 Rattus norvegicus 107-112 17903365-10 2007 The shift band in the lane of the nuclear protein extraction and the MMP-2 probe containing hypoxia response element showed delays when compared with the lane of the sole probe, and the binding was partially abolished when competing sense oligonucleotides were used. Oligonucleotides 239-255 matrix metallopeptidase 2 Rattus norvegicus 69-74 17392157-5 2007 Chronic treatment with the hydrophilic rosuvastatin had renoprotective effects in terms of morphology and inflammation and prevented the changes in plasmin, MMP-2, and MMP-9 activity. Rosuvastatin Calcium 39-51 matrix metallopeptidase 2 Rattus norvegicus 157-162 17691971-1 2007 The present study was designed to investigate whether the neuroprotective effect of nimesulide was mediated by inhibiting expression of matrix metalloproteinase-9 (MMP-9) and/or matrix metalloproteinase-2 (MMP-2) in a rat model of thrombolytic reperfusion after the embolic focal cerebral ischemia (FCI). nimesulide 84-94 matrix metallopeptidase 2 Rattus norvegicus 178-204 17691971-1 2007 The present study was designed to investigate whether the neuroprotective effect of nimesulide was mediated by inhibiting expression of matrix metalloproteinase-9 (MMP-9) and/or matrix metalloproteinase-2 (MMP-2) in a rat model of thrombolytic reperfusion after the embolic focal cerebral ischemia (FCI). nimesulide 84-94 matrix metallopeptidase 2 Rattus norvegicus 206-211 17691971-5 2007 Our results demonstrate that nimesulide significantly reduces the degree of neuronal injury and hemorrhage transformation caused by thrombolytic reperfusion after the embolic FCI, and that inhibition of MMP-9 and MMP-2 expression contributes at least in part to the neuroprotection. nimesulide 29-39 matrix metallopeptidase 2 Rattus norvegicus 213-218 17496904-6 2007 Both MMP-2 and MMP-9 mRNA metanephric expressions and activities were dramatically downregulated in kidneys issued from diabetic fetuses and in metanephros cultured in the presence of high glucose concentration. Glucose 189-196 matrix metallopeptidase 2 Rattus norvegicus 5-10 17308006-4 2007 To this end, MMP-2 activity in LV tissue extracted from rats with an aortocaval (AV) fistula was assessed by in vitro incubation as well as in vivo treatment with captopril, lisinopril, or quinapril. Captopril 163-172 matrix metallopeptidase 2 Rattus norvegicus 13-18 17308006-4 2007 To this end, MMP-2 activity in LV tissue extracted from rats with an aortocaval (AV) fistula was assessed by in vitro incubation as well as in vivo treatment with captopril, lisinopril, or quinapril. Quinapril 189-198 matrix metallopeptidase 2 Rattus norvegicus 13-18 17308006-6 2007 In vitro incubation with captopril, lisinopril, or quinapril significantly reduced MMP-2 activity, as did in vivo treatment. Captopril 25-34 matrix metallopeptidase 2 Rattus norvegicus 83-88 17308006-6 2007 In vitro incubation with captopril, lisinopril, or quinapril significantly reduced MMP-2 activity, as did in vivo treatment. Lisinopril 36-46 matrix metallopeptidase 2 Rattus norvegicus 83-88 17308006-6 2007 In vitro incubation with captopril, lisinopril, or quinapril significantly reduced MMP-2 activity, as did in vivo treatment. Quinapril 51-60 matrix metallopeptidase 2 Rattus norvegicus 83-88 17374421-3 2007 The present research aimed to study the effects of Chinese yellow wine on the production of homocysteine (Hcy)-induced extracellular MMP-2 in cultured rats vascular smooth muscle cells (VSMCs). Homocysteine 92-104 matrix metallopeptidase 2 Rattus norvegicus 133-138 17374421-3 2007 The present research aimed to study the effects of Chinese yellow wine on the production of homocysteine (Hcy)-induced extracellular MMP-2 in cultured rats vascular smooth muscle cells (VSMCs). Homocysteine 106-109 matrix metallopeptidase 2 Rattus norvegicus 133-138 17374421-4 2007 METHODS: We examined the effects of different Hcy levels (0-1000 micromol/l) on MMP-2 production, and the effects of Chinese yellow wine with low alcohol concentrations (12-19%) on Hcy-induced MMP-2 in cultured rat (VSMCs) using gelatin zymography and western blotting. Homocysteine 181-184 matrix metallopeptidase 2 Rattus norvegicus 193-198 17374421-6 2007 Increased production of MMP-2 induced by Hcy was reduced by extracellularly added Chinese yellow wine. Homocysteine 41-44 matrix metallopeptidase 2 Rattus norvegicus 24-29 17374421-7 2007 Production of MMP-2 under various treatments for 48 h increased more than 12 and 24 h. CONCLUSIONS: Extracellularly added Chinese yellow wine decreased Hcy-induced MMP-2 secretion. Homocysteine 152-155 matrix metallopeptidase 2 Rattus norvegicus 14-19 17374421-7 2007 Production of MMP-2 under various treatments for 48 h increased more than 12 and 24 h. CONCLUSIONS: Extracellularly added Chinese yellow wine decreased Hcy-induced MMP-2 secretion. Homocysteine 152-155 matrix metallopeptidase 2 Rattus norvegicus 164-169 17374421-8 2007 The inhibitory effect of yellow wine on the activation of MMP-2 might contribute to their beneficial effects on the cardiovascular system. yellow wine 25-36 matrix metallopeptidase 2 Rattus norvegicus 58-63 17660580-13 2007 Moreover, application of diazoxide inhibited the activities of tissue matrix metalloproteinases (MMP-2). Diazoxide 25-34 matrix metallopeptidase 2 Rattus norvegicus 97-102 17531121-19 2007 The activities of MMP-2 and MMP-9 were enhanced significantly by curcumin. Curcumin 65-73 matrix metallopeptidase 2 Rattus norvegicus 18-23 17531121-20 2007 CONCLUSIONS: Curcumin can inhibit the proliferation and activation of HSCs, induce the apoptosis of activated HSCs and enhance the activities of MMP-2 and MMP-9. Curcumin 13-21 matrix metallopeptidase 2 Rattus norvegicus 145-150 17237246-9 2007 In hypertension, MMP-2 expression and activity in the aorta were increased (59.1 +/- 3.7 and 74.5 +/- 6.1 units in sham and DOCA, respectively, P < 0.05); similar elevations were not observed in the vena cava. Desoxycorticosterone Acetate 124-128 matrix metallopeptidase 2 Rattus norvegicus 17-22 17437609-4 2007 In this study, we established an experimental model by implanting 9L glioma cells stereotactically into Fisher344 (F344) rat"s brain, and the expression and enzymatic activity of MMP-2 and MMP-9 in 9L glioma cells and in tumor tissue was determined by means of reverse transcription polymerase chain reaction (RT-PCR), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) zymography, in situ film zymography and immunostaining. Sodium Dodecyl Sulfate 319-341 matrix metallopeptidase 2 Rattus norvegicus 179-184 17437609-4 2007 In this study, we established an experimental model by implanting 9L glioma cells stereotactically into Fisher344 (F344) rat"s brain, and the expression and enzymatic activity of MMP-2 and MMP-9 in 9L glioma cells and in tumor tissue was determined by means of reverse transcription polymerase chain reaction (RT-PCR), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) zymography, in situ film zymography and immunostaining. polyacrylamide 342-356 matrix metallopeptidase 2 Rattus norvegicus 179-184 17437609-4 2007 In this study, we established an experimental model by implanting 9L glioma cells stereotactically into Fisher344 (F344) rat"s brain, and the expression and enzymatic activity of MMP-2 and MMP-9 in 9L glioma cells and in tumor tissue was determined by means of reverse transcription polymerase chain reaction (RT-PCR), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) zymography, in situ film zymography and immunostaining. Sodium Dodecyl Sulfate 378-381 matrix metallopeptidase 2 Rattus norvegicus 179-184 17437609-6 2007 SDS-PAGE zymography revealed that the expression of MMP-2 and MMP-9 were significantly increased in tumor tissues, and the MMP-9 wasn"t detected in normal tissue. Sodium Dodecyl Sulfate 0-3 matrix metallopeptidase 2 Rattus norvegicus 52-57 17024442-2 2007 Our study was designed to investigate the involvement of MMPs and of tissue inhibitors of metalloproteinases (TIMPs) in rat retinal ischemic injury, the effect of nitric oxide synthase (NOS) inhibitors on MMPs" activity in this model and whether minocycline (an MMP inhibitor) is protective in retinal ischemia. Minocycline 246-257 matrix metallopeptidase 2 Rattus norvegicus 205-209 17024442-14 2007 Minocyline (0.5 mg/ml or 5 mg/ml) inhibited MMPs" activities in ischemic retinal extracts in vitro. minocyline 0-10 matrix metallopeptidase 2 Rattus norvegicus 44-48 17639988-10 2007 Compared to model control, FZHY recipe and methylprednisolone obviously attenuated pulmonary collagen deposition, decreased lung/body ratio and Hyp content, downregulated MMP-2 protein expression and activity, in particular active MMP-2 activity, and FZHU recipe had some better actions than methylprednisolone on lung/body ratio, type IV collagen expression and active MMP-2 activity. Methylprednisolone 43-61 matrix metallopeptidase 2 Rattus norvegicus 171-176 17639988-10 2007 Compared to model control, FZHY recipe and methylprednisolone obviously attenuated pulmonary collagen deposition, decreased lung/body ratio and Hyp content, downregulated MMP-2 protein expression and activity, in particular active MMP-2 activity, and FZHU recipe had some better actions than methylprednisolone on lung/body ratio, type IV collagen expression and active MMP-2 activity. Methylprednisolone 43-61 matrix metallopeptidase 2 Rattus norvegicus 231-236 17639988-10 2007 Compared to model control, FZHY recipe and methylprednisolone obviously attenuated pulmonary collagen deposition, decreased lung/body ratio and Hyp content, downregulated MMP-2 protein expression and activity, in particular active MMP-2 activity, and FZHU recipe had some better actions than methylprednisolone on lung/body ratio, type IV collagen expression and active MMP-2 activity. Methylprednisolone 43-61 matrix metallopeptidase 2 Rattus norvegicus 231-236 17650800-0 2007 [Effect of curcumin on activity of matrix metalloproteinase 2, 9 and nuclear expression of RelA in rat hepatic stellate cells by activating peroxisome proliferator-activated receptor gamma signal]. Curcumin 11-19 matrix metallopeptidase 2 Rattus norvegicus 35-61 17650800-1 2007 OBJECTIVE: To study the effect of curcumin on the activity of matrix metalloproteinases (MMPs) and nuclear expression of RelA in rat hepatic stellate cells (HSCs) by activating peroxisome proliferator-activated receptor gamma (PPARgamma) signal in vitro. Curcumin 34-42 matrix metallopeptidase 2 Rattus norvegicus 89-93 17376290-1 2007 AIM: To examine the role of atorvastatin on volume-overload-induced heart failure and to test the hypothesis that atorvastatin inhibits MMP-2 and 9 expression in heart failure with non-ischemic etiology. Atorvastatin 114-126 matrix metallopeptidase 2 Rattus norvegicus 136-147 17376290-7 2007 Protein expression and enzyme activity of MMP-2 and 9 in the left ventricle tissue were significantly increased 18 weeks after surgery and atorvastatin also prevented those changes. Atorvastatin 139-151 matrix metallopeptidase 2 Rattus norvegicus 42-53 17376290-10 2007 These positive effects of atorvastatin on heart failure were associated with decreased MMP-2 and 9 protein expression and enzyme activity. Atorvastatin 26-38 matrix metallopeptidase 2 Rattus norvegicus 87-98 17189321-6 2007 Decreased PA remodeling in ROSI-treated animals was associated with decreased smooth muscle cell proliferation, decreased collagen and elastin deposition, and increased matrix metalloproteinase-2 activity in the PA wall. Protactinium 10-12 matrix metallopeptidase 2 Rattus norvegicus 169-195 17189321-6 2007 Decreased PA remodeling in ROSI-treated animals was associated with decreased smooth muscle cell proliferation, decreased collagen and elastin deposition, and increased matrix metalloproteinase-2 activity in the PA wall. Rosiglitazone 27-31 matrix metallopeptidase 2 Rattus norvegicus 169-195 17189321-6 2007 Decreased PA remodeling in ROSI-treated animals was associated with decreased smooth muscle cell proliferation, decreased collagen and elastin deposition, and increased matrix metalloproteinase-2 activity in the PA wall. Protactinium 212-214 matrix metallopeptidase 2 Rattus norvegicus 169-195 17197075-4 2007 To address the molecular mechanisms involved, we performed experiments with specific inhibitors against putative targets of curcumin, including IkappaB kinase (IKK), epidermal growth factor receptor (EGFR), phosphatidylinositol-3 kinase (PI3K)/Akt, and matrix metalloproteinases (MMPs). Curcumin 124-132 matrix metallopeptidase 2 Rattus norvegicus 280-284 17197075-6 2007 Western blot analysis and gelatin zymography revealed that curcumin, but not berberine, has an inhibitory effect on the phosphorylation of Akt and enzymatic activity of MMP-2 in TR-LE cells. Curcumin 59-67 matrix metallopeptidase 2 Rattus norvegicus 169-174 17197075-7 2007 These results suggest that curcumin exerts its inhibitory effect on lymphangiogenesis partly through Akt and MMP-2. Curcumin 27-35 matrix metallopeptidase 2 Rattus norvegicus 109-114 17587759-6 2007 Trandolapril treatment significantly reduced MMP-9 and MMP-2 activities to 68.5% and 53.2%, respectively. trandolapril 0-12 matrix metallopeptidase 2 Rattus norvegicus 55-60 17650800-4 2007 RESULTS: The PPARgamma expression decreased gradually with increasing of HSC activation, which was up-regulated by curcumin (P < 0.01); curcumin inhibited the expression of aSMA, the production of collagen type I, and the nuclear expression of activated RelA (P < 0.01), and elevated the activity of MMP2 and MMP9 significantly (P < 0.01). Curcumin 139-147 matrix metallopeptidase 2 Rattus norvegicus 306-310 17650800-6 2007 CONCLUSION: By activating PPARgamma signal transduction pathway curcumin treatment can inhibit HSC activation, increase the activity of MMP2 and MMP9 and inhibit/ interfere nuclear translocation of NFkappaB. Curcumin 64-72 matrix metallopeptidase 2 Rattus norvegicus 136-140 17164434-1 2007 Retinoic acid (RA) is a signaling molecule in the morphogenesis of the mammary gland, modulating the expression of matrix metalloproteinases (MMPs). Tretinoin 0-13 matrix metallopeptidase 2 Rattus norvegicus 142-146 17380220-0 2007 Effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Heparin 11-18 matrix metallopeptidase 2 Rattus norvegicus 75-101 17187281-1 2007 Animal experiments were performed to investigate whether and how the administration of hyperbaric oxygen (HBO) affects gene expressions of procollagens, matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in injured medial collateral ligament (MCL) and anterior cruciate ligament (ACL). Oxygen 98-104 matrix metallopeptidase 2 Rattus norvegicus 180-184 17380220-0 2007 Effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Homocysteine 40-52 matrix metallopeptidase 2 Rattus norvegicus 75-101 17380220-1 2007 OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells. Heparin 35-42 matrix metallopeptidase 2 Rattus norvegicus 99-125 17380220-1 2007 OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells. Heparin 35-42 matrix metallopeptidase 2 Rattus norvegicus 127-132 17380220-1 2007 OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells. Homocysteine 64-76 matrix metallopeptidase 2 Rattus norvegicus 99-125 17380220-1 2007 OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells. Homocysteine 64-76 matrix metallopeptidase 2 Rattus norvegicus 127-132 17380220-3 2007 The changes in MMP-2 were further compared with various treatments for 24 h, 48 h and 72 h. RESULTS: Homocysteine (50 micromol/L to 1000 micromol/L) increased the production of MMP-2 significantly in a dose-dependent manner. Homocysteine 101-113 matrix metallopeptidase 2 Rattus norvegicus 15-20 17380220-3 2007 The changes in MMP-2 were further compared with various treatments for 24 h, 48 h and 72 h. RESULTS: Homocysteine (50 micromol/L to 1000 micromol/L) increased the production of MMP-2 significantly in a dose-dependent manner. Homocysteine 101-113 matrix metallopeptidase 2 Rattus norvegicus 177-182 17380220-4 2007 Increased production of MMP-2 induced by homocysteine was reduced by the extracellular addition of heparin in a dose-dependent manner. Homocysteine 41-53 matrix metallopeptidase 2 Rattus norvegicus 24-29 17380220-4 2007 Increased production of MMP-2 induced by homocysteine was reduced by the extracellular addition of heparin in a dose-dependent manner. Heparin 99-106 matrix metallopeptidase 2 Rattus norvegicus 24-29 17380220-5 2007 Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion. Heparin 136-143 matrix metallopeptidase 2 Rattus norvegicus 14-19 17380220-5 2007 Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion. Heparin 136-143 matrix metallopeptidase 2 Rattus norvegicus 175-180 17380220-5 2007 Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion. Homocysteine 154-166 matrix metallopeptidase 2 Rattus norvegicus 14-19 17380220-5 2007 Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion. Homocysteine 154-166 matrix metallopeptidase 2 Rattus norvegicus 175-180 17184751-8 2007 The activity of MMP-2 and MMP-9 was significantly reduced by DPI/DMSO but not by DMSO alone. diphenyleneiodonium 61-64 matrix metallopeptidase 2 Rattus norvegicus 16-21 17295775-7 2007 Naltrexone treatment in BDL rats led to a decrease in the level of liver MMP-2 activity, which had already increased during cholestasis. Naltrexone 0-10 matrix metallopeptidase 2 Rattus norvegicus 73-78 17241522-8 2007 Dex treatment significantly ameliorated CHF in association with the reversion of the abnormalities of MMP-2/9, TIMP-1/2, TNF-alpha, and ROS. Dexamethasone 0-3 matrix metallopeptidase 2 Rattus norvegicus 102-109 17241522-10 2007 CONCLUSION: Dex improves CHF by inhibiting TNF-alpha, MMP-2, MMP-9, and ROS. Dexamethasone 12-15 matrix metallopeptidase 2 Rattus norvegicus 54-59 17166729-0 2007 Doxycycline inhibits MMPs via modulation of plasminogen activators in focal cerebral ischemia. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 21-25 17166729-1 2007 Tetracyclines inhibit matrix metalloproteinases (MMPs) and reduce infarction volume following cerebral ischemia. Tetracyclines 0-13 matrix metallopeptidase 2 Rattus norvegicus 49-53 17184751-12 2007 The combination of DPI and DMSO reduced the activity of MMP-2 and MMP-9, attenuated the postischemic blood-brain barrier damage and improved neurological outcome. Dimethyl Sulfoxide 27-31 matrix metallopeptidase 2 Rattus norvegicus 56-61 17184751-8 2007 The activity of MMP-2 and MMP-9 was significantly reduced by DPI/DMSO but not by DMSO alone. Dimethyl Sulfoxide 65-69 matrix metallopeptidase 2 Rattus norvegicus 16-21 17184751-8 2007 The activity of MMP-2 and MMP-9 was significantly reduced by DPI/DMSO but not by DMSO alone. Dimethyl Sulfoxide 81-85 matrix metallopeptidase 2 Rattus norvegicus 16-21 17184751-10 2007 The combination of DMSO with DPI partly augmented this effect, presumably due to the additional inhibition of MMP-2 and MMP-9 by DPI. Dimethyl Sulfoxide 19-23 matrix metallopeptidase 2 Rattus norvegicus 110-115 17184751-10 2007 The combination of DMSO with DPI partly augmented this effect, presumably due to the additional inhibition of MMP-2 and MMP-9 by DPI. diphenyleneiodonium 29-32 matrix metallopeptidase 2 Rattus norvegicus 110-115 17184751-10 2007 The combination of DMSO with DPI partly augmented this effect, presumably due to the additional inhibition of MMP-2 and MMP-9 by DPI. diphenyleneiodonium 129-132 matrix metallopeptidase 2 Rattus norvegicus 110-115 17184751-12 2007 The combination of DPI and DMSO reduced the activity of MMP-2 and MMP-9, attenuated the postischemic blood-brain barrier damage and improved neurological outcome. diphenyleneiodonium 19-22 matrix metallopeptidase 2 Rattus norvegicus 56-61 16899336-0 2007 Terazosin modifies the content of glycosaminoglycans and the activity of matrix metalloproteinase 2 in the rat ventral prostate. Terazosin 0-9 matrix metallopeptidase 2 Rattus norvegicus 73-99 16899336-7 2007 Terazosin evoked a significant increase in the activity of proMMP-2 and MMP-2 but did not affect TIMP. Terazosin 0-9 matrix metallopeptidase 2 Rattus norvegicus 62-67 16980344-4 2007 MMP-2 inhibition with cyclic CTTHWGFTLC (CTT) reduced contraction to phenylephrine (PE) in aortae and mesenteric arteries from rats exposed to hypoxia for 7 days but not in vessels from normoxic rats. cyclo(Cys-Thr-Thr-His-Trp-Gly-Phe-Thr-Leu-Cys) 22-39 matrix metallopeptidase 2 Rattus norvegicus 0-5 16899336-9 2007 The effect of terazosin on GAGs and MMP-2 may contribute in the molecular mechanisms of terazosin-induced apoptosis because HS and CS have a proapoptotic effect, whereas DS and MMP-2 are antiapoptotic. Terazosin 14-23 matrix metallopeptidase 2 Rattus norvegicus 177-182 16899336-9 2007 The effect of terazosin on GAGs and MMP-2 may contribute in the molecular mechanisms of terazosin-induced apoptosis because HS and CS have a proapoptotic effect, whereas DS and MMP-2 are antiapoptotic. Terazosin 88-97 matrix metallopeptidase 2 Rattus norvegicus 36-41 16899336-9 2007 The effect of terazosin on GAGs and MMP-2 may contribute in the molecular mechanisms of terazosin-induced apoptosis because HS and CS have a proapoptotic effect, whereas DS and MMP-2 are antiapoptotic. Terazosin 88-97 matrix metallopeptidase 2 Rattus norvegicus 177-182 16899336-9 2007 The effect of terazosin on GAGs and MMP-2 may contribute in the molecular mechanisms of terazosin-induced apoptosis because HS and CS have a proapoptotic effect, whereas DS and MMP-2 are antiapoptotic. Heparitin Sulfate 124-126 matrix metallopeptidase 2 Rattus norvegicus 36-41 16899336-9 2007 The effect of terazosin on GAGs and MMP-2 may contribute in the molecular mechanisms of terazosin-induced apoptosis because HS and CS have a proapoptotic effect, whereas DS and MMP-2 are antiapoptotic. Chondroitin Sulfates 131-133 matrix metallopeptidase 2 Rattus norvegicus 36-41 21882490-14 2007 CONCLUSION: Streptozotocin induced diabetes led to increased LV/bodyweight, increased collagen content, and diminished MMP-2 with no change in PCr/ATP. Streptozocin 12-26 matrix metallopeptidase 2 Rattus norvegicus 119-124 17365669-1 2007 OBJECTIVE: Ischemic angiogenesis is dependent on vascular nitric oxide (NO) bioavailability, in part by reducing matrix metalloproteinases (MMP)-2 and -9 activity and angiostatin production. Nitric Oxide 58-70 matrix metallopeptidase 2 Rattus norvegicus 113-153 16980344-4 2007 MMP-2 inhibition with cyclic CTTHWGFTLC (CTT) reduced contraction to phenylephrine (PE) in aortae and mesenteric arteries from rats exposed to hypoxia for 7 days but not in vessels from normoxic rats. CTTHWGFTLC peptide 29-32 matrix metallopeptidase 2 Rattus norvegicus 0-5 16980344-4 2007 MMP-2 inhibition with cyclic CTTHWGFTLC (CTT) reduced contraction to phenylephrine (PE) in aortae and mesenteric arteries from rats exposed to hypoxia for 7 days but not in vessels from normoxic rats. Phenylephrine 69-82 matrix metallopeptidase 2 Rattus norvegicus 0-5 16980344-4 2007 MMP-2 inhibition with cyclic CTTHWGFTLC (CTT) reduced contraction to phenylephrine (PE) in aortae and mesenteric arteries from rats exposed to hypoxia for 7 days but not in vessels from normoxic rats. Phenylephrine 84-86 matrix metallopeptidase 2 Rattus norvegicus 0-5 16676162-7 2007 The histological examination showed the PBL extract protected liver from the damage induced by CCl(4) by decreasing alpha-smooth muscle actin (alpha-sma) expression, inducing active matrix metalloproteinase-2 (MMP2) expression though Ras/Erk pathway, and inhibiting TIMP2 level that consequently attenuated the fibrosis of liver. Cefaclor 95-98 matrix metallopeptidase 2 Rattus norvegicus 210-214 17678975-7 2007 Pharmacological manipulation of MMPs activity, using the broad spectrum MMPs inhibitor GM6001, reduces the increase in IL-1beta immunoreactivity and the neuronal apoptosis induced by gp120. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 87-93 matrix metallopeptidase 2 Rattus norvegicus 32-36 17053025-9 2007 Myogenic reactivity was inhibited in small renal arteries isolated from nonpregnant rats treated with rhRLX for 4-6 h (P < 0.01 vs. vehicle) and was completely restored by incubation with MMP-9, but not MMP-2 neutralizing antibodies in vitro. rhrlx 102-107 matrix metallopeptidase 2 Rattus norvegicus 206-211 17678960-5 2007 The latter effect appears to be instrumental for development of delayed brain damage since administration of a broad spectrum, highly specific MMPs inhibitor, GM6001, but not by its negative control, results in a significant (50%) reduction in ischemic brain volume. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 159-165 matrix metallopeptidase 2 Rattus norvegicus 143-147 17678960-7 2007 More importantly, when administered at a neuroprotective dose GM6001 abolishes the early IL-1beta increase in the ischemic cortex and reduces the cleavage of the cytokine proform supporting the deduction that MMPs may initiate IL-1beta processing. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 62-68 matrix metallopeptidase 2 Rattus norvegicus 209-213 17505812-10 2007 Blockage of ERK1/2 phosphorylation by treatment with MEK inhibitor (PD98059) decreased the expression of MMP2 in cancer cells grown in rat astrocyte-conditioned media. 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one 68-75 matrix metallopeptidase 2 Rattus norvegicus 105-109 17678975-7 2007 Pharmacological manipulation of MMPs activity, using the broad spectrum MMPs inhibitor GM6001, reduces the increase in IL-1beta immunoreactivity and the neuronal apoptosis induced by gp120. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 87-93 matrix metallopeptidase 2 Rattus norvegicus 72-76 17215740-11 2007 BALF MMP-2 expression was attenuated by 11% with HSPTX (p = 0.09). hsptx 49-54 matrix metallopeptidase 2 Rattus norvegicus 5-10 16935385-8 2007 Pravastatin decreased liver matrix metalloproteinase (MMP)-9 activity and mostly suppressed MMP-2 activation (p<0.004), likely because it decreased expression of MMP-14 and tissue inhibitor of matrix metalloproteinases-2 (p<0.01), required for MMP-2 activation. Pravastatin 0-11 matrix metallopeptidase 2 Rattus norvegicus 92-97 16935385-8 2007 Pravastatin decreased liver matrix metalloproteinase (MMP)-9 activity and mostly suppressed MMP-2 activation (p<0.004), likely because it decreased expression of MMP-14 and tissue inhibitor of matrix metalloproteinases-2 (p<0.01), required for MMP-2 activation. Pravastatin 0-11 matrix metallopeptidase 2 Rattus norvegicus 250-255 17122420-7 2007 A selective inhibitor for MMP-2, -9 and -12, tolylsam, was used to examine the effect of inhibition of MMP-2 and MMP-9. 3-methyl-2-(4-(3-p-tolyl(1,2,4)oxadiazol-5-yl)benzenesulfonylamino)butyric acid 45-53 matrix metallopeptidase 2 Rattus norvegicus 26-31 17356310-8 2007 In addition, acute treatment with pioglitazone dose-dependently increased PPARgamma expression and decreased MMP-2 expression at protein and mRNA levels. Pioglitazone 34-46 matrix metallopeptidase 2 Rattus norvegicus 109-114 17522763-10 2007 the active MMP-2 and MMP-9 levels decreased in the azelnidipine group. azelnidipine 51-63 matrix metallopeptidase 2 Rattus norvegicus 11-16 17522763-13 2007 Azelnidipine therefore appears to influence the inflammatory oxidative response seen in AAAs while also decreasing the MMP-2 and MMP-9 levels. azelnidipine 0-12 matrix metallopeptidase 2 Rattus norvegicus 119-124 17112415-3 2006 The present study investigates whether EGCG inhibits activation of the major gelatinase matrix metalloproteinase-2 (MMP-2) in rat hepatic stellate cells (HSC). epigallocatechin gallate 39-43 matrix metallopeptidase 2 Rattus norvegicus 88-114 17112415-3 2006 The present study investigates whether EGCG inhibits activation of the major gelatinase matrix metalloproteinase-2 (MMP-2) in rat hepatic stellate cells (HSC). epigallocatechin gallate 39-43 matrix metallopeptidase 2 Rattus norvegicus 116-121 17112415-0 2006 Green tea polyphenol epigallocatechin-3-gallate suppresses rat hepatic stellate cell invasion by inhibition of MMP-2 expression and its activation. polyphenol epigallocatechin-3-gallate 10-47 matrix metallopeptidase 2 Rattus norvegicus 111-116 17112415-7 2006 RESULTS: The expression of MMP-2 mRNA and protein in HSC was substantially reduced by EGCG treatment. epigallocatechin gallate 86-90 matrix metallopeptidase 2 Rattus norvegicus 27-32 17112415-8 2006 EGCG treatment also reduced concanavalin A (ConA)-induced activation of secreted MMP-2 and reduced MT1-MMP activity in a dose-dependent manner. epigallocatechin gallate 0-4 matrix metallopeptidase 2 Rattus norvegicus 81-86 17112415-10 2006 CONCLUSION: The abilities of EGCG to suppress MMP-2 activation and HSC invasiveness suggest that EGCG may be useful in the treatment and prevention of hepatic fibrosis. epigallocatechin gallate 29-33 matrix metallopeptidase 2 Rattus norvegicus 46-51 17112415-10 2006 CONCLUSION: The abilities of EGCG to suppress MMP-2 activation and HSC invasiveness suggest that EGCG may be useful in the treatment and prevention of hepatic fibrosis. epigallocatechin gallate 97-101 matrix metallopeptidase 2 Rattus norvegicus 46-51 16979164-14 2006 In retinas of rats with oxygen-induced neovascularization, the expression of LRP-1 and alpha2M was increased along with an enhanced activity of MMPs, suggesting that LRP-1 expression may play a role in modulating retinal neovascularization by regulating proteolytic activity. Oxygen 24-30 matrix metallopeptidase 2 Rattus norvegicus 144-148 16543289-6 2006 RESULTS: Naltrexone markedly attenuated the development of hepatic fibrosis as well as MMP-2 activity (p<0.01), and decreased the number of activated HSCs in BDL rats (p<0.05). Naltrexone 9-19 matrix metallopeptidase 2 Rattus norvegicus 87-92 17262995-8 2006 BBIC reduced the activity of matrix metalloproteinase (MMP)-2 and -9 in spleen cell supernatants and was detected in the CNS of treated rats. bbic 0-4 matrix metallopeptidase 2 Rattus norvegicus 29-68 16733664-6 2006 Here we report that treatment with bleomycin downregulates caveolin-1 and increases CD147 and MMP-2 and -9 expression/activity in R3/1 cells using RT-PCR, Western blot analysis, MMP-2 activity assay and immunocytochemistry. Bleomycin 35-44 matrix metallopeptidase 2 Rattus norvegicus 94-106 16733664-6 2006 Here we report that treatment with bleomycin downregulates caveolin-1 and increases CD147 and MMP-2 and -9 expression/activity in R3/1 cells using RT-PCR, Western blot analysis, MMP-2 activity assay and immunocytochemistry. Bleomycin 35-44 matrix metallopeptidase 2 Rattus norvegicus 94-99 29699252-6 2006 That dehydroepiandrosterone (DHEA) treatment caused the formation of cysts from antral follicles in the ovaries of immature rats while depressing MMP-2 collagenolytic activity and enhancing lysyl oxidase expression highlights the importance of collagen degradation in the process of ovulation and suggests that changes in the activities of these enzymes play a key role in ovarian cystogenesis in polycystic ovary syndrome patients. Dehydroepiandrosterone 5-27 matrix metallopeptidase 2 Rattus norvegicus 146-151 29699252-6 2006 That dehydroepiandrosterone (DHEA) treatment caused the formation of cysts from antral follicles in the ovaries of immature rats while depressing MMP-2 collagenolytic activity and enhancing lysyl oxidase expression highlights the importance of collagen degradation in the process of ovulation and suggests that changes in the activities of these enzymes play a key role in ovarian cystogenesis in polycystic ovary syndrome patients. Dehydroepiandrosterone 29-33 matrix metallopeptidase 2 Rattus norvegicus 146-151 17071857-4 2006 In addition, MMP-2, as well as its reported inducers concanavalin A and 17beta-estradiol, can trigger the migration of retinal progenitor cells into explanted retinas. Estradiol 72-88 matrix metallopeptidase 2 Rattus norvegicus 13-18 17288771-9 2006 Up-regulated expressions of MMP-2, 3, 9 and down-regulated TIMP-1 and FN expressions in IS and LVFW could be significantly attenuated by valsartan but not by PD123319. Valsartan 137-146 matrix metallopeptidase 2 Rattus norvegicus 28-33 17008622-7 2006 RESULTS: In the rats treated with a relatively selective MMP-2 inhibitor, AG3340, the WM lesions after chronic cerebral hypoperfusion were significantly less severe, and the number of activated astroglia and microglia were also significantly lower as compared with the vehicle-treated rats. prinomastat 74-80 matrix metallopeptidase 2 Rattus norvegicus 57-62 16721810-6 2006 Treatment of H-Ras WB cells with GM6001 and NS398, the inhibitors of MMPs and COX-2, respectively, significantly inhibited the H-Ras-induced invasive and migrative phenotypes. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 33-39 matrix metallopeptidase 2 Rattus norvegicus 69-73 17036385-9 2006 DMN treatment induced a highly up-regulated expression of TNF-alpha, TGF-beta, TIMP-1, TIMP-2, PDGF-beta, and MMP-2. Dimethylnitrosamine 0-3 matrix metallopeptidase 2 Rattus norvegicus 110-115 17036385-10 2006 Of these, the gene expression encoding PDGF-beta and MMP-2 was still further enhanced 2 wk after secession of the 4-wk DMN treatment, and was remarkably ameliorated by CGX administration. Dimethylnitrosamine 119-122 matrix metallopeptidase 2 Rattus norvegicus 53-58 17036385-10 2006 Of these, the gene expression encoding PDGF-beta and MMP-2 was still further enhanced 2 wk after secession of the 4-wk DMN treatment, and was remarkably ameliorated by CGX administration. N4-cyclopropyl-5-ethyl-6-piperidin-1-yl-pyrimidine-2,4-diamine 168-171 matrix metallopeptidase 2 Rattus norvegicus 53-58 16728425-3 2006 METHODS: In this study, we attempted to characterize changes in MMP-2 and TIMP-2 in streptozotocin-induced diabetic rats. Streptozocin 84-98 matrix metallopeptidase 2 Rattus norvegicus 64-69 16854986-9 2006 Together, these findings suggest that changes in MMP-2 expression are part of the program of VSMC phenotypic modulation and that both PDGF-BB and IGF-I, despite their different abilities to induce proliferation in this model, are capable of inducing VSMC activation. vsmc 93-97 matrix metallopeptidase 2 Rattus norvegicus 49-54 16857167-7 2006 Interestingly, MMP-2 antibody (30 microg/ml), or the MMP-2 inhibitors Doxycycline (Dox, 1-50 micromol/l) or GM6001 (GM, 10 micromol/l), prior to TNFalpha insult, decreased myocardial MMP-2 activity and reduced the percent of TUNEL-positive myocytes and DNA fragmentation. Doxycycline 70-81 matrix metallopeptidase 2 Rattus norvegicus 53-58 16857167-7 2006 Interestingly, MMP-2 antibody (30 microg/ml), or the MMP-2 inhibitors Doxycycline (Dox, 1-50 micromol/l) or GM6001 (GM, 10 micromol/l), prior to TNFalpha insult, decreased myocardial MMP-2 activity and reduced the percent of TUNEL-positive myocytes and DNA fragmentation. Doxycycline 70-81 matrix metallopeptidase 2 Rattus norvegicus 53-58 16857167-7 2006 Interestingly, MMP-2 antibody (30 microg/ml), or the MMP-2 inhibitors Doxycycline (Dox, 1-50 micromol/l) or GM6001 (GM, 10 micromol/l), prior to TNFalpha insult, decreased myocardial MMP-2 activity and reduced the percent of TUNEL-positive myocytes and DNA fragmentation. Doxycycline 70-73 matrix metallopeptidase 2 Rattus norvegicus 53-58 16857167-7 2006 Interestingly, MMP-2 antibody (30 microg/ml), or the MMP-2 inhibitors Doxycycline (Dox, 1-50 micromol/l) or GM6001 (GM, 10 micromol/l), prior to TNFalpha insult, decreased myocardial MMP-2 activity and reduced the percent of TUNEL-positive myocytes and DNA fragmentation. Doxycycline 70-73 matrix metallopeptidase 2 Rattus norvegicus 53-58 16935996-3 2006 Here, we report the identification of a calcium-dependent high molecular weight complex composed of MMP-9, MMP-3, MMP-2, tissue inhibitor of metalloproteinase 1 (TIMP-1) and TIMP-2, identified by zymography and western blotting. Calcium 40-47 matrix metallopeptidase 2 Rattus norvegicus 114-119 16728425-11 2006 CONCLUSIONS: High glucose or Ang-II treatment induce alterations in MMP-2 and TIMP-2 balance, which favour TIMP-2 over-activity. Glucose 18-25 matrix metallopeptidase 2 Rattus norvegicus 68-73 16728425-7 2006 In cultured cells, both high glucose and Ang-II induced significant increases in TGF-beta1, TIMP-2, and in collagen synthesis, and significant decreases in MMP-2 gene expression and activity, and thus disrupted the balance between MMP-2 and TIMP-2. Glucose 29-36 matrix metallopeptidase 2 Rattus norvegicus 156-161 16728425-7 2006 In cultured cells, both high glucose and Ang-II induced significant increases in TGF-beta1, TIMP-2, and in collagen synthesis, and significant decreases in MMP-2 gene expression and activity, and thus disrupted the balance between MMP-2 and TIMP-2. Glucose 29-36 matrix metallopeptidase 2 Rattus norvegicus 231-236 16618940-9 2006 Pups that were exposed antenatally to CsA presented several pathologic findings in all immature parenchyma and an increase in iNOS and MMP2 expression. Cyclosporine 38-41 matrix metallopeptidase 2 Rattus norvegicus 135-139 17034719-1 2006 OBJECTIVE: To explore the effect of N-acetyl L-cysteine (NAC) on expressions of matrix metalloproteinases-2, 9 (MMP-2, MMP-9) in lung fibroblasts of SiO(2) exposed rats. Acetylcysteine 36-55 matrix metallopeptidase 2 Rattus norvegicus 80-110 17034719-1 2006 OBJECTIVE: To explore the effect of N-acetyl L-cysteine (NAC) on expressions of matrix metalloproteinases-2, 9 (MMP-2, MMP-9) in lung fibroblasts of SiO(2) exposed rats. Acetylcysteine 36-55 matrix metallopeptidase 2 Rattus norvegicus 112-117 17034719-1 2006 OBJECTIVE: To explore the effect of N-acetyl L-cysteine (NAC) on expressions of matrix metalloproteinases-2, 9 (MMP-2, MMP-9) in lung fibroblasts of SiO(2) exposed rats. Acetylcysteine 57-60 matrix metallopeptidase 2 Rattus norvegicus 80-110 17034719-1 2006 OBJECTIVE: To explore the effect of N-acetyl L-cysteine (NAC) on expressions of matrix metalloproteinases-2, 9 (MMP-2, MMP-9) in lung fibroblasts of SiO(2) exposed rats. Acetylcysteine 57-60 matrix metallopeptidase 2 Rattus norvegicus 112-117 17034719-11 2006 CONCLUSION: NAC inhibits the expressions of MMP-2, MMP-9 in lung fibroblasts. Acetylcysteine 12-15 matrix metallopeptidase 2 Rattus norvegicus 44-49 16846501-0 2006 Delayed minocycline inhibits ischemia-activated matrix metalloproteinases 2 and 9 after experimental stroke. Minocycline 8-19 matrix metallopeptidase 2 Rattus norvegicus 48-81 16846501-5 2006 In this study we investigated whether delayed minocycline inhibits brain MMPs activated by ischemia in a model of temporary occlusion in Wistar rats. Minocycline 46-57 matrix metallopeptidase 2 Rattus norvegicus 73-77 16846501-7 2006 Intraperitoneal minocycline at 45 mg/kg concentration twice a day (first dose immediately after the onset of reperfusion) significantly reduced gelatinolytic activity of ischemia-elevated MMP-2 and MMP-9 (p < 0.0003). Minocycline 16-27 matrix metallopeptidase 2 Rattus norvegicus 188-193 16846501-9 2006 In vitro incubation of minocycline in concentrations as low as 0.1 mug/ml with recombinant MMP-2 and MMP-9 impaired enzymatic activity and MMP-9 was more sensitive at lower minocycline concentrations (p < 0.05). Minocycline 23-34 matrix metallopeptidase 2 Rattus norvegicus 91-96 16846501-9 2006 In vitro incubation of minocycline in concentrations as low as 0.1 mug/ml with recombinant MMP-2 and MMP-9 impaired enzymatic activity and MMP-9 was more sensitive at lower minocycline concentrations (p < 0.05). Minocycline 173-184 matrix metallopeptidase 2 Rattus norvegicus 91-96 16360173-14 2006 These data suggest that MMPs may play a role in the ability of salicylate to exacerbate gastric injury from irritants, but likely do not play a role in mediating the deleterious effects of L-NAME. Salicylates 63-73 matrix metallopeptidase 2 Rattus norvegicus 24-28 16690877-6 2006 Interestingly, in old untreated rings or VSMCs, the increased TGF-beta1, fibronectin, and collagen were also substantially reduced by inhibition of MMP-2. vsmcs 41-46 matrix metallopeptidase 2 Rattus norvegicus 148-153 16457997-13 2006 Placenta active MMP-2 and active MMP-9 (gelatinase) production was suppressed significantly by 30-43% in the 0.7 en% DHA group in comparison to the 0.7 en% LnA group, and 2.0 en% DHA did not enhance this suppression. Docosahexaenoic Acids 117-120 matrix metallopeptidase 2 Rattus norvegicus 16-21 16575906-0 2006 Nitric oxide and p38 MAP kinase mediate shear stress-dependent inhibition of MMP-2 production in microvascular endothelial cells. Nitric Oxide 0-12 matrix metallopeptidase 2 Rattus norvegicus 77-82 16575906-4 2006 We analyzed the production of MMP-2, using both the in vivo model of prazosin-induced angiogenesis in rat skeletal muscle, and cultured microvascular endothelial cells exposed to laminar shear stress. Prazosin 69-77 matrix metallopeptidase 2 Rattus norvegicus 30-35 16575906-7 2006 This effect on MMP-2 was reversed by nitric oxide (NO) synthase inhibition using LNNA. Nitric Oxide 37-49 matrix metallopeptidase 2 Rattus norvegicus 15-20 16575906-10 2006 Treatment of shear stress-exposed cells with the p38 MAPK inhibitor, SB203580, abolished the shear stress-mediated reduction in MMP-2 mRNA. SB 203580 69-77 matrix metallopeptidase 2 Rattus norvegicus 128-133 16732983-14 2006 All diabetes-associated changes in renal function and MMP/TIMP were attenuated after benazepril treatment with reduced IV-C accumulation. benazepril 85-95 matrix metallopeptidase 2 Rattus norvegicus 54-57 16484357-8 2006 MMP-2 mRNA as measured by real-time PCR was increased in small renal arteries from pregnant and Rlx-treated nonpregnant rats compared with their respective controls. Relaxin 96-99 matrix metallopeptidase 2 Rattus norvegicus 0-5 16484357-10 2006 Thus increases in MMP-2 mRNA and protein expression are major factors contributing to increased MMP-2 activity in small arteries from pregnant and Rlx-treated nonpregnant rats. Relaxin 147-150 matrix metallopeptidase 2 Rattus norvegicus 18-23 16484357-10 2006 Thus increases in MMP-2 mRNA and protein expression are major factors contributing to increased MMP-2 activity in small arteries from pregnant and Rlx-treated nonpregnant rats. Relaxin 147-150 matrix metallopeptidase 2 Rattus norvegicus 96-101 16484357-3 2006 We first corroborated our earlier work by showing that pro- and active forms of MMP-2 were increased in small renal arteries from pregnant compared with virgin rats and Rlx-treated compared with vehicle-treated nonpregnant rats. Relaxin 169-172 matrix metallopeptidase 2 Rattus norvegicus 80-85 16732983-0 2006 Effects of benazepril on renal function and kidney expression of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 in diabetic rats. benazepril 11-21 matrix metallopeptidase 2 Rattus norvegicus 65-91 16732983-16 2006 Benazepril could exert protective effects on diabetic nephropathy, owing to the upregulation of MMP-2 and downregulation of TIMP-2 expressions, which further inhibits the excessive deposition of extracellular matrix in the glomerulus. benazepril 0-10 matrix metallopeptidase 2 Rattus norvegicus 96-101 16647925-7 2006 Matrix metalloproteinase-2 expression increased after the administration of mifepristone. Mifepristone 76-88 matrix metallopeptidase 2 Rattus norvegicus 0-26 16722033-11 2006 RESULTS: In rats receiving PD fluids containing more than 0.66 mmol/L MGO, peritoneal function decreased significantly and levels of type IV collagen-7S and MMP-2 in drained dialysate increased significantly. Pyruvaldehyde 70-73 matrix metallopeptidase 2 Rattus norvegicus 157-162 16680016-11 2006 RESULTS: Aminoguanidine treatment decreased LPS-induced macroscopic gastric injury as well as MMP-2 and MT1-MMP protein production while having no effect on TIMP-2 protein levels. pimagedine 9-23 matrix metallopeptidase 2 Rattus norvegicus 94-99 16478919-5 2006 Finally, morphological changes were assessed following early or delayed administration of CGS-27023-A, a synthetic inhibitor of MMPs. CGS 27023A 90-101 matrix metallopeptidase 2 Rattus norvegicus 128-132 16502514-0 2006 Effect of matrine and carvedilol on collagen and MMPs activity of hypertrophy myocardium induced by pressure overload. matrine 10-17 matrix metallopeptidase 2 Rattus norvegicus 49-53 16701099-3 2006 The aim of this study is to examine the inhibitory effects of ONO-4817 (oral inhibitor of MMPs) in rats. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 62-70 matrix metallopeptidase 2 Rattus norvegicus 90-94 16701099-9 2006 MMP-9 and MMP-2 activities also were inhibited in the ONO-4817 group as shown by gelatin zymography. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 54-62 matrix metallopeptidase 2 Rattus norvegicus 10-15 16701099-13 2006 CONCLUSIONS: Hepatic ischemia/reperfusion injury was improved by a novel MMP inhibitor, ONO-4817, not only by inhibition of gelatinolytic activity but also by a decrease in release of inflammatory cytokines. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 88-96 matrix metallopeptidase 2 Rattus norvegicus 73-76 16864425-5 2006 The results show that crocetin blocked the development of left ventricular hypertrophy induced by NE, decreased the level of collagen in myocardium, enhanced both the Na+-K+ ATPase activity in cardiac tissue and the Ca2+-Mg2+ ATPase activity in mitochondria and inhibited significantly the activity of MMP-2 and the expressions of MMP-2 and MMP-9. crocetin 22-30 matrix metallopeptidase 2 Rattus norvegicus 302-307 16864425-5 2006 The results show that crocetin blocked the development of left ventricular hypertrophy induced by NE, decreased the level of collagen in myocardium, enhanced both the Na+-K+ ATPase activity in cardiac tissue and the Ca2+-Mg2+ ATPase activity in mitochondria and inhibited significantly the activity of MMP-2 and the expressions of MMP-2 and MMP-9. crocetin 22-30 matrix metallopeptidase 2 Rattus norvegicus 331-336 16502514-0 2006 Effect of matrine and carvedilol on collagen and MMPs activity of hypertrophy myocardium induced by pressure overload. Carvedilol 22-32 matrix metallopeptidase 2 Rattus norvegicus 49-53 16502514-13 2006 CONCLUSION: Matrine was shown to be able to prevent cardiac remodelling of hypertrophy cardium induced by pressure overload including myocardial hypertrophy and fibrosis which may be associated with the decrease in MMP-2 activity of heart. matrine 12-19 matrix metallopeptidase 2 Rattus norvegicus 215-220 16166267-9 2006 Early treatment with ramipril completely prevented renal damage in Ren2 and restored mRNA expression of TGF-beta1, MMP-2, and TIMP-1 to SD control levels. Ramipril 21-29 matrix metallopeptidase 2 Rattus norvegicus 115-120 16165109-7 2006 The activities of MMP2 and MMP9 and the abundance of TIMP1 and TIMP2 in LV tissue were increased at 18 weeks of age, and pravastatin also prevented these changes. Pravastatin 121-132 matrix metallopeptidase 2 Rattus norvegicus 18-22 16213474-0 2006 Matrix metalloproteinase-2 and -9 are induced differently by doxorubicin in H9c2 cells: The role of MAP kinases and NAD(P)H oxidase. Doxorubicin 61-72 matrix metallopeptidase 2 Rattus norvegicus 0-33 16213474-3 2006 This study investigates the effects of doxorubicin on myocardial MMP-2 and MMP-9 activation. Doxorubicin 39-50 matrix metallopeptidase 2 Rattus norvegicus 65-70 16239374-1 2006 Although past studies have demonstrated decreased renal matrix metalloproteinase (MMP) activity in type 1 diabetes and in mesangial cells grown under high glucose conditions, renal MMP expression and activity in type 2 diabetes and the regulation of MMPs by profibrotic factors involved in diabetic renal complications such as endothelin-1 (ET-1) remained unknown. Glucose 155-162 matrix metallopeptidase 2 Rattus norvegicus 250-254 16449942-2 2006 Therefore, we used a novel MMP inhibitor (ONO-4817) with high affinities for MMP-2 and MMP-9 to investigate the roles of MMPs in reperfusion injury of the lungs. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 42-50 matrix metallopeptidase 2 Rattus norvegicus 77-82 16377938-0 2006 Effects of folic acid and magnesium on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Folic Acid 11-21 matrix metallopeptidase 2 Rattus norvegicus 92-118 16377938-0 2006 Effects of folic acid and magnesium on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Magnesium 26-35 matrix metallopeptidase 2 Rattus norvegicus 92-118 16377938-0 2006 Effects of folic acid and magnesium on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Homocysteine 57-69 matrix metallopeptidase 2 Rattus norvegicus 92-118 16377938-2 2006 The aim of this study was to test whether homocysteine increases the production of matrix metalloproteinase-2 (MMP-2) and if extracellular additional magnesium and folic acid alters MMP-2 secretion. Homocysteine 42-54 matrix metallopeptidase 2 Rattus norvegicus 83-109 16377938-2 2006 The aim of this study was to test whether homocysteine increases the production of matrix metalloproteinase-2 (MMP-2) and if extracellular additional magnesium and folic acid alters MMP-2 secretion. Magnesium 150-159 matrix metallopeptidase 2 Rattus norvegicus 182-187 16377938-2 2006 The aim of this study was to test whether homocysteine increases the production of matrix metalloproteinase-2 (MMP-2) and if extracellular additional magnesium and folic acid alters MMP-2 secretion. Folic Acid 164-174 matrix metallopeptidase 2 Rattus norvegicus 182-187 16377938-4 2006 Furthermore, the changes in MMP-2 were compared under various treatments for 24 h, 48 h and 72 h. Homocysteine (50-1,000 micromol/L) increased the production of MMP-2 significantly in a dose-dependent manner and at a high level (5,000 micromol/L) reduced the production of MMP-2. Homocysteine 98-110 matrix metallopeptidase 2 Rattus norvegicus 28-33 16377938-4 2006 Furthermore, the changes in MMP-2 were compared under various treatments for 24 h, 48 h and 72 h. Homocysteine (50-1,000 micromol/L) increased the production of MMP-2 significantly in a dose-dependent manner and at a high level (5,000 micromol/L) reduced the production of MMP-2. Homocysteine 98-110 matrix metallopeptidase 2 Rattus norvegicus 161-166 16377938-4 2006 Furthermore, the changes in MMP-2 were compared under various treatments for 24 h, 48 h and 72 h. Homocysteine (50-1,000 micromol/L) increased the production of MMP-2 significantly in a dose-dependent manner and at a high level (5,000 micromol/L) reduced the production of MMP-2. Homocysteine 98-110 matrix metallopeptidase 2 Rattus norvegicus 161-166 16377938-5 2006 Increased production of MMP-2 induced by homocysteine was reduced by additional extracellular folic acid in a dose-dependent manner. Homocysteine 41-53 matrix metallopeptidase 2 Rattus norvegicus 24-29 16377938-5 2006 Increased production of MMP-2 induced by homocysteine was reduced by additional extracellular folic acid in a dose-dependent manner. Folic Acid 94-104 matrix metallopeptidase 2 Rattus norvegicus 24-29 16377938-6 2006 Magnesium also reduced the increase of MMP-2 production induced by homocysteine. Magnesium 0-9 matrix metallopeptidase 2 Rattus norvegicus 39-44 16377938-6 2006 Magnesium also reduced the increase of MMP-2 production induced by homocysteine. Homocysteine 67-79 matrix metallopeptidase 2 Rattus norvegicus 39-44 16377938-7 2006 Production of MMP-2 under various treatments for 72 h increased more than during 24 or 48 h. CONCLUSIONS: Homocysteine (50-1,000 micromol/L) significantly increased the production of MMP-2 in a dose-dependent manner. Homocysteine 106-118 matrix metallopeptidase 2 Rattus norvegicus 14-19 16377938-7 2006 Production of MMP-2 under various treatments for 72 h increased more than during 24 or 48 h. CONCLUSIONS: Homocysteine (50-1,000 micromol/L) significantly increased the production of MMP-2 in a dose-dependent manner. Homocysteine 106-118 matrix metallopeptidase 2 Rattus norvegicus 183-188 16377938-8 2006 Added extracellular folic acid and magnesium decreased the homocysteine-induced MMP-2 secretion. Folic Acid 20-30 matrix metallopeptidase 2 Rattus norvegicus 80-85 16377938-8 2006 Added extracellular folic acid and magnesium decreased the homocysteine-induced MMP-2 secretion. Magnesium 35-44 matrix metallopeptidase 2 Rattus norvegicus 80-85 16377938-8 2006 Added extracellular folic acid and magnesium decreased the homocysteine-induced MMP-2 secretion. Homocysteine 59-71 matrix metallopeptidase 2 Rattus norvegicus 80-85 16183705-0 2006 YC-1 [3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole] inhibits neointima formation in balloon-injured rat carotid through suppression of expressions and activities of matrix metalloproteinases 2 and 9. 3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole 6-53 matrix metallopeptidase 2 Rattus norvegicus 168-201 16183705-2 2006 We investigated the inhibitory effect of 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole (YC-1), a benzyl indazole compound, on MMP-2 and MMP-9 activity in a balloon-injury rat carotid artery model. 3-(5'-hydroxymethyl-2'-furyl)-1-benzylindazole 41-88 matrix metallopeptidase 2 Rattus norvegicus 128-133 16183705-2 2006 We investigated the inhibitory effect of 3-(5"-hydroxymethyl-2"-furyl)-1-benzyl indazole (YC-1), a benzyl indazole compound, on MMP-2 and MMP-9 activity in a balloon-injury rat carotid artery model. benzyl indazole 73-88 matrix metallopeptidase 2 Rattus norvegicus 128-133 16183705-6 2006 On the other hand, YC-1 inhibited hydrolysis of the fluorogenic quenching substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH(2) by recombinant MMP-2 and MMP-9 with IC(50) values = 2.07 and 8.20 muM, respectively. Methylcholanthrene 84-87 matrix metallopeptidase 2 Rattus norvegicus 137-142 16183705-6 2006 On the other hand, YC-1 inhibited hydrolysis of the fluorogenic quenching substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH(2) by recombinant MMP-2 and MMP-9 with IC(50) values = 2.07 and 8.20 muM, respectively. pro-leu-gly-leu-dpa 88-107 matrix metallopeptidase 2 Rattus norvegicus 137-142 16183705-6 2006 On the other hand, YC-1 inhibited hydrolysis of the fluorogenic quenching substrate Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH(2) by recombinant MMP-2 and MMP-9 with IC(50) values = 2.07 and 8.20 muM, respectively. L-Arginine, L-alanyl- 108-115 matrix metallopeptidase 2 Rattus norvegicus 137-142 16213474-9 2006 ERK and JNK modulate the transcription of the NAD(P)H oxidase subunit Nox1, while the JNK/ERK NAD(P)H oxidase cascade is an important pathway that mediates doxorubicin signaling to MMP-2. Doxorubicin 156-167 matrix metallopeptidase 2 Rattus norvegicus 181-186 16213474-11 2006 CONCLUSIONS: Enhancement of MMP-2 and MMP-9 in cardiac myocytes in response to doxorubicin is mediated by the cooperation of ERK, JNK, and p38 kinase pathways, most of which are redox dependent. Doxorubicin 79-90 matrix metallopeptidase 2 Rattus norvegicus 28-33 16166272-9 2006 A reduction of infarct size in nonpreconditioned hearts from both control and cholesterol-fed group was produced by the MMP inhibitor ilomastat at 0.25 microM, a concentration producing MMP-2 inhibition comparable with that of preconditioning in the control group. Cholesterol 78-89 matrix metallopeptidase 2 Rattus norvegicus 186-191 16166272-9 2006 A reduction of infarct size in nonpreconditioned hearts from both control and cholesterol-fed group was produced by the MMP inhibitor ilomastat at 0.25 microM, a concentration producing MMP-2 inhibition comparable with that of preconditioning in the control group. ilomastat 134-143 matrix metallopeptidase 2 Rattus norvegicus 186-191 15878156-7 2005 The number of periodontal ligament cells expressing MMP-2 was also significantly reduced in tissues treated with the two higher doses of PGE2 (p<0.001) comparing with both matched controls and the placebo-treated group. Dinoprostone 137-141 matrix metallopeptidase 2 Rattus norvegicus 52-57 16456445-12 2006 RESULTS: PTX treatment decreased BAL IL-8 levels, BAL MMP-2, and plasma MMP-9 activity. Pentoxifylline 9-12 matrix metallopeptidase 2 Rattus norvegicus 54-59 16735800-2 2006 Halofuginone is a nontoxic alkaloid, used as a coccidiostat, and is a potent inhibitor of collagen alpha(1)(I) and matrix metalloproteinase-2 (MMP-2) expression. halofuginone 0-12 matrix metallopeptidase 2 Rattus norvegicus 115-141 16735800-2 2006 Halofuginone is a nontoxic alkaloid, used as a coccidiostat, and is a potent inhibitor of collagen alpha(1)(I) and matrix metalloproteinase-2 (MMP-2) expression. halofuginone 0-12 matrix metallopeptidase 2 Rattus norvegicus 143-148 16735800-15 2006 CONCLUSIONS: Halofuginone exhibits antifibrotic effects in rat renal papillary fibroblasts in culture, in terms of inhibition of proliferation and inhibition of MMP-2. halofuginone 13-25 matrix metallopeptidase 2 Rattus norvegicus 161-166 15878156-9 2005 Furthermore, the same doses of PGE2 also significantly reduced the expression of MMP-2 by the periodontal cells. Dinoprostone 31-35 matrix metallopeptidase 2 Rattus norvegicus 81-86 16435072-11 2005 Our work suggest that effective MMPs" inhibition in the infarcted and remote myocardium by doxycycline does not prevent LV remodeling and dysfunction but impairs angiogenesis and compensatory LV hypertrophy. Doxycycline 91-102 matrix metallopeptidase 2 Rattus norvegicus 32-36 16251426-7 2005 The MMP inhibitor GM6001 and the AT1 receptor antagonist Losartan inhibited these effects. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 18-24 matrix metallopeptidase 2 Rattus norvegicus 4-7 16304337-0 2005 L-arginine attenuates acute pulmonary embolism-induced increases in lung matrix metalloproteinase-2 and matrix metalloproteinase-9. Arginine 0-10 matrix metallopeptidase 2 Rattus norvegicus 73-130 16251426-8 2005 The alpha-adrenoreceptor agonist phenylephrine increased arterial Ang II protein, causing MMP2 activation and intima and media thickening. Phenylephrine 33-46 matrix metallopeptidase 2 Rattus norvegicus 90-94 16251426-9 2005 Exposure of young VSMCs to phenylephrine in vitro increased Ang II protein and MMP2 activity to the levels of old VSMCs; Losartan abolished these effects. Phenylephrine 27-40 matrix metallopeptidase 2 Rattus norvegicus 79-83 16304337-1 2005 STUDY OBJECTIVES: To evaluate the effects of L-arginine on acute pulmonary embolism (APE)-induced pulmonary hypertension and increases in lung matrix metalloproteinase (MMP)-2 and MMP-9 activities. Arginine 45-55 matrix metallopeptidase 2 Rattus norvegicus 143-175 16304337-10 2005 While L-arginine at 0.5 mmol/L produced no effect on MMPs, L-arginine 3 at mmol/L and 10 mmol/L attenuated the increases in MMP-2 and MMP-9 activities after APE (both p < 0.05). Arginine 59-69 matrix metallopeptidase 2 Rattus norvegicus 124-129 16304337-11 2005 CONCLUSIONS: L-arginine attenuates APE-induced pulmonary hypertension through mechanisms involving increased NO synthesis and maybe attenuation of lung MMP-2 and MMP-9 activities. Arginine 13-23 matrix metallopeptidase 2 Rattus norvegicus 152-157 16033810-7 2005 Moreover, Bay-X-1005 induced a reduction in the gelatinolytic activity of matrix metalloproteinase-2 (MMP-2) and a decrease in mRNA expression of tissue inhibitor of MMP-2. 2-(4-(quinolin-2-yl-methoxy)phenyl)-2-cyclopentylacetic acid 10-20 matrix metallopeptidase 2 Rattus norvegicus 74-100 16212944-3 2005 In the present study, we determined effects of 17beta-estradiol (E2) on BBB disruption induced by transient focal cerebral ischemia and its effects on MMP2 and MMP9 activation. Estradiol 47-63 matrix metallopeptidase 2 Rattus norvegicus 151-155 16254495-6 2005 In addition, postganglionic nerve crush induced an increase in the beta-DG 30-kDa fragment produced by the MMP-dependent degradation of DG. beta-dg 67-74 matrix metallopeptidase 2 Rattus norvegicus 107-110 16033810-7 2005 Moreover, Bay-X-1005 induced a reduction in the gelatinolytic activity of matrix metalloproteinase-2 (MMP-2) and a decrease in mRNA expression of tissue inhibitor of MMP-2. 2-(4-(quinolin-2-yl-methoxy)phenyl)-2-cyclopentylacetic acid 10-20 matrix metallopeptidase 2 Rattus norvegicus 102-107 16033810-7 2005 Moreover, Bay-X-1005 induced a reduction in the gelatinolytic activity of matrix metalloproteinase-2 (MMP-2) and a decrease in mRNA expression of tissue inhibitor of MMP-2. 2-(4-(quinolin-2-yl-methoxy)phenyl)-2-cyclopentylacetic acid 10-20 matrix metallopeptidase 2 Rattus norvegicus 166-171 16150113-3 2005 Our objective was to investigate the effect of melatonin (N-acetyl-5 methoxytryptamine) on the regulation of MMP-9 and MMP-2 activity during prevention of gastric ulcer. Melatonin 47-56 matrix metallopeptidase 2 Rattus norvegicus 119-124 16150113-3 2005 Our objective was to investigate the effect of melatonin (N-acetyl-5 methoxytryptamine) on the regulation of MMP-9 and MMP-2 activity during prevention of gastric ulcer. Melatonin 58-86 matrix metallopeptidase 2 Rattus norvegicus 119-124 16150113-6 2005 Furthermore, melatonin prevents gastric ulceration in a dose-dependent manner through upregulation (approximately two- to threefold) of both pro-MMP-2 and active MMP-2 at the level of induction as well as secretion. Melatonin 13-22 matrix metallopeptidase 2 Rattus norvegicus 145-150 16150113-6 2005 Furthermore, melatonin prevents gastric ulceration in a dose-dependent manner through upregulation (approximately two- to threefold) of both pro-MMP-2 and active MMP-2 at the level of induction as well as secretion. Melatonin 13-22 matrix metallopeptidase 2 Rattus norvegicus 162-167 16150113-8 2005 The novel findings of this study are attributed to the attenuation of the pro-MMP-9 and increase of MMP-2 activity by pretreatment with melatonin. Melatonin 136-145 matrix metallopeptidase 2 Rattus norvegicus 100-105 16150113-9 2005 The finding defines one of the MMP-mediated pathways for melatonin"s action in gastric ulcer. Melatonin 57-66 matrix metallopeptidase 2 Rattus norvegicus 31-34 16086306-8 2005 Furthermore, pharmacologic inhibition of MMP-2 activity in fetal lung explants cultured at 21% O(2) resulted in increased TN-C deposition within the mesenchyme, as well as enhanced branching morphogenesis. Oxygen 95-99 matrix metallopeptidase 2 Rattus norvegicus 41-46 16123349-4 2005 Zymography of islet extracts revealed a concurrent, >10-fold increase in MMP-2 protease activity in islets from 9-week-old male ZDF rats. zdf 131-134 matrix metallopeptidase 2 Rattus norvegicus 76-81 15860571-2 2005 In the present study, we investigated whether 6-ethyl chenodeoxycholic acid (6-ECDCA or INT-747), a semisynthetic derivative of chenodeoxycholic acid (CDCA), modulates tissue metalloproteinase inhibitor (TIMP)-1 and matrix metalloprotease (MMP)-2 expression/activity in HSCs and in the liver of rats rendered cirrhotic by 4-week administration of CCl(4). obeticholic acid 46-75 matrix metallopeptidase 2 Rattus norvegicus 216-246 16043662-5 2005 Aldosterone (50 nmol/L) increased MMP-2 (43+/-5%) and MMP-9 (55+/-15%; P<0.001 for both) activities. Aldosterone 0-11 matrix metallopeptidase 2 Rattus norvegicus 34-39 16470485-9 2005 Lysyl oxidase, MMP-1 and MMP-2 activity were inhibited by arphamenine A in the conditioned media of control and TGF-ss1-treated cardiac fibroblasts. arphamenine A 58-71 matrix metallopeptidase 2 Rattus norvegicus 25-30 16093917-9 2005 Bosentan decreased MMP-2 (78.9 +/- 3.8 versus 117.4 +/- 12.2 AU; P = 0.014) and proMMP-2 activity (P < 0.006) in the senescent SHR group. Bosentan 0-8 matrix metallopeptidase 2 Rattus norvegicus 19-24 16093917-13 2005 However, bosentan decreased pro and active MMP-2 activity in senescent SHR rats, indicating that ET modulates late events in vascular remodelling in hypertension. Bosentan 9-17 matrix metallopeptidase 2 Rattus norvegicus 43-48 15967562-10 2005 CAPE subcutaneous administration (15 micromol/kg/day) improved cardiac cytoarchitecture, decreased the levels and the expression of MMP2, and increased those of TIMP2 proteins. caffeic acid phenethyl ester 0-4 matrix metallopeptidase 2 Rattus norvegicus 132-136 16097048-16 2005 Perindopril treatment significantly reduced mean fibrosis score, protein levels of AT1R, TGF-beta1 and PDGF-BB, serum levels of HA and LN, and the activity of MMP-2,9. Perindopril 0-11 matrix metallopeptidase 2 Rattus norvegicus 159-166 16097048-18 2005 CONCLUSION: Perindopril attenuates CCl(4)-induced hepatic fibrogenesis of rat by inhibiting TGF-beta1, PDGF-BB, NF-kappaB and MMP-2,9. Perindopril 12-23 matrix metallopeptidase 2 Rattus norvegicus 126-133 16128366-0 2005 Effects of copper and zinc on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Copper 11-17 matrix metallopeptidase 2 Rattus norvegicus 83-109 16128366-0 2005 Effects of copper and zinc on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells. Homocysteine 48-60 matrix metallopeptidase 2 Rattus norvegicus 83-109 16128366-1 2005 OBJECTIVE: To study the effects of copper and zinc on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rats vascular smooth muscle cells. Copper 35-41 matrix metallopeptidase 2 Rattus norvegicus 107-133 16128366-1 2005 OBJECTIVE: To study the effects of copper and zinc on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rats vascular smooth muscle cells. Homocysteine 72-84 matrix metallopeptidase 2 Rattus norvegicus 107-133 16128366-4 2005 RESULTS: Homocysteine (50-1000 micromol/l) increased the production of MMP-2 significantly in a dose-dependent manner. Homocysteine 9-21 matrix metallopeptidase 2 Rattus norvegicus 71-76 16128366-5 2005 Copper decreased the homocysteine-induced MMP-2 under these conditions in a dose-dependent manner, but zinc did not. Copper 0-6 matrix metallopeptidase 2 Rattus norvegicus 42-47 16128366-5 2005 Copper decreased the homocysteine-induced MMP-2 under these conditions in a dose-dependent manner, but zinc did not. Homocysteine 21-33 matrix metallopeptidase 2 Rattus norvegicus 42-47 16128366-6 2005 Production of MMP-2 under various treatments for 72 h increased more than 24 h and 48 h. CONCLUSIONS: Extracellular added copper decreased homocysteine-induced MMP-2 secretion. Copper 122-128 matrix metallopeptidase 2 Rattus norvegicus 14-19 16128366-6 2005 Production of MMP-2 under various treatments for 72 h increased more than 24 h and 48 h. CONCLUSIONS: Extracellular added copper decreased homocysteine-induced MMP-2 secretion. Copper 122-128 matrix metallopeptidase 2 Rattus norvegicus 160-165 16128366-6 2005 Production of MMP-2 under various treatments for 72 h increased more than 24 h and 48 h. CONCLUSIONS: Extracellular added copper decreased homocysteine-induced MMP-2 secretion. Homocysteine 139-151 matrix metallopeptidase 2 Rattus norvegicus 14-19 16128366-6 2005 Production of MMP-2 under various treatments for 72 h increased more than 24 h and 48 h. CONCLUSIONS: Extracellular added copper decreased homocysteine-induced MMP-2 secretion. Homocysteine 139-151 matrix metallopeptidase 2 Rattus norvegicus 160-165 15860571-2 2005 In the present study, we investigated whether 6-ethyl chenodeoxycholic acid (6-ECDCA or INT-747), a semisynthetic derivative of chenodeoxycholic acid (CDCA), modulates tissue metalloproteinase inhibitor (TIMP)-1 and matrix metalloprotease (MMP)-2 expression/activity in HSCs and in the liver of rats rendered cirrhotic by 4-week administration of CCl(4). Chenodeoxycholic Acid 54-75 matrix metallopeptidase 2 Rattus norvegicus 216-246 16027249-9 2005 MMP-2 was found to cleave myosin light chain 1 between tyrosine 189 and glutamine 190 at the C terminus. Tyrosine 55-63 matrix metallopeptidase 2 Rattus norvegicus 0-5 16027249-9 2005 MMP-2 was found to cleave myosin light chain 1 between tyrosine 189 and glutamine 190 at the C terminus. Glutamine 72-81 matrix metallopeptidase 2 Rattus norvegicus 0-5 15823620-3 2005 The present work evaluates placental and fetal MMPs and NO levels during midpregnancy in neonatal streptozotocin-induced diabetic rats. Streptozocin 98-112 matrix metallopeptidase 2 Rattus norvegicus 47-51 15728709-3 2005 beta-AR stimulation (isoproterenol, 24 h) increased mRNA levels of MMP-2 and TIMP-1 while it decreased TIMP-2 mRNA levels as analyzed by real-time PCR. Isoproterenol 21-34 matrix metallopeptidase 2 Rattus norvegicus 67-72 15728709-5 2005 Inhibition of MMPs using GM-6001 (a broad-spectrum inhibitor of MMPs), SB3CT (inhibitor of MMP-2), and purified TIMP-2 inhibited beta-AR-stimulated apoptosis as determined by TdT-mediated dUTP nick end labeling staining. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 25-32 matrix metallopeptidase 2 Rattus norvegicus 14-18 15728709-5 2005 Inhibition of MMPs using GM-6001 (a broad-spectrum inhibitor of MMPs), SB3CT (inhibitor of MMP-2), and purified TIMP-2 inhibited beta-AR-stimulated apoptosis as determined by TdT-mediated dUTP nick end labeling staining. deoxyuridine triphosphate 188-192 matrix metallopeptidase 2 Rattus norvegicus 14-18 15728709-7 2005 This increase in MMP-2-mediated apoptosis was inhibited by GM-6001 and SB3CT pretreatment. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 59-66 matrix metallopeptidase 2 Rattus norvegicus 17-22 15728709-7 2005 This increase in MMP-2-mediated apoptosis was inhibited by GM-6001 and SB3CT pretreatment. SB 3CT compound 71-76 matrix metallopeptidase 2 Rattus norvegicus 17-22 15863246-0 2005 Repeated cadmium nebulizations induce pulmonary MMP-2 and MMP-9 production and emphysema in rats. Cadmium 9-16 matrix metallopeptidase 2 Rattus norvegicus 48-53 15863246-1 2005 This study describes induction of pulmonary inflammation, production of matrix metalloprotease of type 2 (MMP-2) and type 9 (MMP-9), and emphysema in cadmium (Cd)-exposed rats. Cadmium 150-157 matrix metallopeptidase 2 Rattus norvegicus 72-104 15863246-1 2005 This study describes induction of pulmonary inflammation, production of matrix metalloprotease of type 2 (MMP-2) and type 9 (MMP-9), and emphysema in cadmium (Cd)-exposed rats. Cadmium 150-157 matrix metallopeptidase 2 Rattus norvegicus 106-111 15863246-1 2005 This study describes induction of pulmonary inflammation, production of matrix metalloprotease of type 2 (MMP-2) and type 9 (MMP-9), and emphysema in cadmium (Cd)-exposed rats. Cadmium 159-161 matrix metallopeptidase 2 Rattus norvegicus 72-104 15863246-1 2005 This study describes induction of pulmonary inflammation, production of matrix metalloprotease of type 2 (MMP-2) and type 9 (MMP-9), and emphysema in cadmium (Cd)-exposed rats. Cadmium 159-161 matrix metallopeptidase 2 Rattus norvegicus 106-111 16042886-11 2005 RESULTS: In the model group the hepatic MMP-2 mRNA expression started to increase 10 days after DMN administration and remained at a much higher level than in the normal group throughout the study period, while TIMP-2 mRNA expression started to be lower than in the normal group 17 days after DMN administration and reached the lowest level on the 28th day. Dimethylnitrosamine 96-99 matrix metallopeptidase 2 Rattus norvegicus 40-45 16042886-11 2005 RESULTS: In the model group the hepatic MMP-2 mRNA expression started to increase 10 days after DMN administration and remained at a much higher level than in the normal group throughout the study period, while TIMP-2 mRNA expression started to be lower than in the normal group 17 days after DMN administration and reached the lowest level on the 28th day. Dimethylnitrosamine 293-296 matrix metallopeptidase 2 Rattus norvegicus 40-45 16042886-13 2005 TIMP-2/MMP-2 began to be lower by several days than that of the normal group after DMN administration through the remaining study period. Dimethylnitrosamine 83-86 matrix metallopeptidase 2 Rattus norvegicus 7-12 16042900-0 2005 [Effects of hyperbaric oxygen with free-radical antagonists on the expression and activity of matrix metalloproteinase-2 in rat livers]. Oxygen 23-29 matrix metallopeptidase 2 Rattus norvegicus 94-120 16042900-0 2005 [Effects of hyperbaric oxygen with free-radical antagonists on the expression and activity of matrix metalloproteinase-2 in rat livers]. Free Radicals 35-47 matrix metallopeptidase 2 Rattus norvegicus 94-120 16037621-0 2005 Effect of erythromycin on homocysteine-induced extracellular matrix metalloproteinase-2 production in cultured rat vascular smooth muscle cells. Erythromycin 10-22 matrix metallopeptidase 2 Rattus norvegicus 61-87 16037621-0 2005 Effect of erythromycin on homocysteine-induced extracellular matrix metalloproteinase-2 production in cultured rat vascular smooth muscle cells. Homocysteine 26-38 matrix metallopeptidase 2 Rattus norvegicus 61-87 16037621-3 2005 In the present study we investigated the effects of erythromycin on the production of homocysteineinduced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells (VSMCs). Erythromycin 52-64 matrix metallopeptidase 2 Rattus norvegicus 120-146 16037621-3 2005 In the present study we investigated the effects of erythromycin on the production of homocysteineinduced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells (VSMCs). Erythromycin 52-64 matrix metallopeptidase 2 Rattus norvegicus 148-153 16037621-4 2005 METHODS: Effects of different concentration of homocysteine (Hcy) (0-5000 micromol/l) on MMP-2 production, and the effects of different erythromycin concentrations (0-10 mmol/l) on homocysteine-induced MMP-2 production in cultured rat VSMCs were studied using gelatin zymography and Western blotting. Homocysteine 61-64 matrix metallopeptidase 2 Rattus norvegicus 89-94 16037621-6 2005 RESULTS: Homocysteine (50-1000 mu mol/l) increased the production of MMP-2 significantly in a dose-dependent manner and reduced the production of MMP-2 at a high level (5000 mu mol/l). Homocysteine 9-21 matrix metallopeptidase 2 Rattus norvegicus 69-74 16037621-6 2005 RESULTS: Homocysteine (50-1000 mu mol/l) increased the production of MMP-2 significantly in a dose-dependent manner and reduced the production of MMP-2 at a high level (5000 mu mol/l). Homocysteine 9-21 matrix metallopeptidase 2 Rattus norvegicus 146-151 16037621-7 2005 Increased production of MMP-2 induced by homocysteine was reduced by extracellularly added erythromycin in a dose-dependent manner. Homocysteine 41-53 matrix metallopeptidase 2 Rattus norvegicus 24-29 16037621-7 2005 Increased production of MMP-2 induced by homocysteine was reduced by extracellularly added erythromycin in a dose-dependent manner. Erythromycin 91-103 matrix metallopeptidase 2 Rattus norvegicus 24-29 16037621-8 2005 INTERPRETATION & CONCLUSION: Homocysteine increased the production of MMP-2 significantly in a dose-dependent manner. Adenosine Monophosphate 16-19 matrix metallopeptidase 2 Rattus norvegicus 74-79 16037621-8 2005 INTERPRETATION & CONCLUSION: Homocysteine increased the production of MMP-2 significantly in a dose-dependent manner. Homocysteine 33-45 matrix metallopeptidase 2 Rattus norvegicus 74-79 16037621-9 2005 Extracellularly added erythromycin decreased homocysteine-induced MMP-2 secretion. Erythromycin 22-34 matrix metallopeptidase 2 Rattus norvegicus 66-71 16037621-9 2005 Extracellularly added erythromycin decreased homocysteine-induced MMP-2 secretion. Homocysteine 45-57 matrix metallopeptidase 2 Rattus norvegicus 66-71 15978215-0 2005 Effects of irbesartan on the expression of matrix metalloproteinase-2/tissue inhibitor of metalloproteinase-2 in streptozotocin-induced diabetic rat kidney. Irbesartan 11-21 matrix metallopeptidase 2 Rattus norvegicus 43-109 15978215-0 2005 Effects of irbesartan on the expression of matrix metalloproteinase-2/tissue inhibitor of metalloproteinase-2 in streptozotocin-induced diabetic rat kidney. Streptozocin 113-127 matrix metallopeptidase 2 Rattus norvegicus 43-109 16037621-10 2005 The findings of the present study suggested that the beneficial effect of erythromycin on vascular disease processes might be due to its inhibitory effect on the Hcyinduced production of MMP-2 in VSMCs. Erythromycin 74-86 matrix metallopeptidase 2 Rattus norvegicus 187-192 15893960-15 2005 These results suggest that treatment with sodium alginate as a new immunosuppressive agent can reduce proteinuria, inhibit MMP-2 activity and suppress the antibody production as well as the development of glomerular lesions in a rat model of immune complex glomerulonephritis. Alginates 42-57 matrix metallopeptidase 2 Rattus norvegicus 123-128 15932706-11 2005 The levels of TNF-alpha mRNA in AMI rats treated with fosinopril, pravastatin and their combination reduced 29%, 26% and 33%, respectively (P < 0.01); MMP-2 activity reduced 25%, 30% and 35%, respectively (P < 0.01); MMP-9 activity reduced 20%, 18% and 24%, respectively (P < 0.01). Fosinopril 54-64 matrix metallopeptidase 2 Rattus norvegicus 154-159 15576828-0 2005 Differential effects of estrogen and raloxifene on messenger RNA and matrix metalloproteinase 2 activity in the rat uterus. Raloxifene Hydrochloride 37-47 matrix metallopeptidase 2 Rattus norvegicus 69-95 15576828-6 2005 Both E and lasofoxifene stimulated uterine MMP2 activity to a level twofold that of Ral, whereas levormeloxifene elevated MMP2 activity to a level 12-fold that of Ral. Lasofoxifene 11-23 matrix metallopeptidase 2 Rattus norvegicus 43-47 15576828-6 2005 Both E and lasofoxifene stimulated uterine MMP2 activity to a level twofold that of Ral, whereas levormeloxifene elevated MMP2 activity to a level 12-fold that of Ral. levormeloxifene 97-112 matrix metallopeptidase 2 Rattus norvegicus 122-126 15963646-10 2005 Paralleling these effects on cerebral ischemia, olmesartan treatment also reduced the reactive upregulation in brain angiotensin II, matrix metalloproteinase-2, matrix metalloproteinase-9, and membrane type 1-matrix metalloproteinase in the ischemic area. olmesartan 48-58 matrix metallopeptidase 2 Rattus norvegicus 133-187 15848549-9 2005 Of the dose combinations, CSA 7.5 mg/d + RAPA 0.5 mg/d produced the lowest serum creatinine for all time points, and inhibited profibrotic TIMP-1 (P = .017), while increasing antifibrotic MMP-2 (P = .009) mRNA expression, compared to CSA treatment alone. Cyclosporine 26-29 matrix metallopeptidase 2 Rattus norvegicus 188-193 15353401-1 2005 Tetracyclines exhibit significant anti-inflammatory properties, inhibit matrix metalloproteinases (MMPs), and are protective in models of ischemia-reperfusion injury (IRI). Tetracyclines 0-13 matrix metallopeptidase 2 Rattus norvegicus 99-103 15353401-7 2005 Minocycline diminished the perivascular increase in MMP-2 and MMP-9, as well as the increase in MMP-2 activity 24 h after ischemia. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 52-57 15353401-7 2005 Minocycline diminished the perivascular increase in MMP-2 and MMP-9, as well as the increase in MMP-2 activity 24 h after ischemia. Minocycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 96-101 15353401-8 2005 ABT-518, a specific inhibitor of MMP-2 and MMP-9, also significantly reduced the extent of dextran (500 kDa) leakage from the renal microvasculature 24 h after ischemia. N-(1-(2,2-dimethyl-1,3-dioxol-4-yl)-2-((4,4-(trifluoromethoxyphenoxy)phenyl)sulfonyl)ethyl)-N-hydroxyformamide 0-7 matrix metallopeptidase 2 Rattus norvegicus 33-38 15353401-8 2005 ABT-518, a specific inhibitor of MMP-2 and MMP-9, also significantly reduced the extent of dextran (500 kDa) leakage from the renal microvasculature 24 h after ischemia. Dextrans 91-98 matrix metallopeptidase 2 Rattus norvegicus 33-38 15853913-7 2005 Moreover, in vitro examinations revealed that treatment with LVA could diminish MMP-2 activity. mevinolinic acid 61-64 matrix metallopeptidase 2 Rattus norvegicus 80-85 15853913-9 2005 Some of the action of LVA may be associated with its inhibitory effects on cytokine and eicosanoid production and MMP-2 activity. mevinolinic acid 22-25 matrix metallopeptidase 2 Rattus norvegicus 114-119 15615723-2 2005 However, the role of MMPs in indomethacin-induced gastric ulcer and its healing process are not clearly understood. Indomethacin 29-41 matrix metallopeptidase 2 Rattus norvegicus 21-25 15615723-4 2005 Indomethacin-ulcerated stomach extracts exhibit significant up-regulation of pro-MMP-9 (92 kDa) activity and moderate reduction of MMP-2 activity, which strongly correlate with indomethacin dose and severity of ulcer. Indomethacin 0-12 matrix metallopeptidase 2 Rattus norvegicus 131-136 15615723-4 2005 Indomethacin-ulcerated stomach extracts exhibit significant up-regulation of pro-MMP-9 (92 kDa) activity and moderate reduction of MMP-2 activity, which strongly correlate with indomethacin dose and severity of ulcer. Indomethacin 177-189 matrix metallopeptidase 2 Rattus norvegicus 131-136 15615723-5 2005 The anti-inflammatory and antioxidant properties of curcumin, an active component of turmeric, suggest that curcumin may exert antiulcer activity through scavenging reactive oxygen species, by regulating MMP activity, or both. Curcumin 52-60 matrix metallopeptidase 2 Rattus norvegicus 204-207 15615723-5 2005 The anti-inflammatory and antioxidant properties of curcumin, an active component of turmeric, suggest that curcumin may exert antiulcer activity through scavenging reactive oxygen species, by regulating MMP activity, or both. Curcumin 108-116 matrix metallopeptidase 2 Rattus norvegicus 204-207 15633128-6 2005 A single in vivo administration of sulfasalazine promoted accelerated recovery from fibrosis as assessed by improved fibrosis score, selective clearance of smooth muscle alpha-actin-positive myofibroblasts, reduced hepatic procollagen I and tissue inhibitor of metalloproteinase 1 messenger RNA expression, and increased matrix metalloproteinase 2 activity. Sulfasalazine 35-48 matrix metallopeptidase 2 Rattus norvegicus 321-347 16178123-2 2005 Genomic analysis of olfactory mucosa from rats given alachlor (126 mg/kg/d) for from 1 day to 18 mo suggested that matrix metalloproteinases MMP-2 and MMP-9 were upregulated in the month following initiation of treatment. alachlor 53-61 matrix metallopeptidase 2 Rattus norvegicus 141-146 15808571-9 2005 Matrix metalloproteinase-2 expression was decreased by cyclosporine; all doses of pirfenidone significantly reversed this effect. Cyclosporine 55-67 matrix metallopeptidase 2 Rattus norvegicus 0-26 16178123-4 2005 Zymographic analysis of olfactory mucosal extracts confirmed that MMP-2 activity is higher in the olfactory mucosa of alachlor-treated rats. alachlor 118-126 matrix metallopeptidase 2 Rattus norvegicus 66-71 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 91-99 matrix metallopeptidase 2 Rattus norvegicus 42-47 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 91-99 matrix metallopeptidase 2 Rattus norvegicus 144-151 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 91-99 matrix metallopeptidase 2 Rattus norvegicus 144-149 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 42-47 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 144-151 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 144-149 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 42-47 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 144-151 16178123-8 2005 These data confirm that olfactory mucosal MMP-2 activity is increased following short-term alachlor exposure and show that administration of an MMP-2/9 inhibitor reduced the incidence of olfactory neoplasms in alachlor-treated rats, thereby implicating MMP-2 activity as a mediator of alachlor-induced carcinogenicity. alachlor 210-218 matrix metallopeptidase 2 Rattus norvegicus 144-149 15231495-5 2004 Additionally, pretreatment with the mast cell stabilizer nedocromil prevented ET-1-induced changes in MMP-2 activity, myocardial water content, collagen volume fraction, and end-diastolic volume. Nedocromil 57-67 matrix metallopeptidase 2 Rattus norvegicus 102-107 15642321-4 2004 The objective of this study was to assess the expression of MMPs and their regulators in an oxidative stress model of cataract, where epithelial cell death and cortical fibre cell swelling occurs in rat lenses after exposure to riboflavin, oxygen, and light. Riboflavin 228-238 matrix metallopeptidase 2 Rattus norvegicus 60-64 15642321-4 2004 The objective of this study was to assess the expression of MMPs and their regulators in an oxidative stress model of cataract, where epithelial cell death and cortical fibre cell swelling occurs in rat lenses after exposure to riboflavin, oxygen, and light. Oxygen 240-246 matrix metallopeptidase 2 Rattus norvegicus 60-64 15531084-6 2004 The brain damage, in terms of brain edema (4 +/- 1%) and overexpression of MMPs, was significantly (p < 0.05) ameliorated as a result of saline flushing into the ischemic territory prior to reperfusion. Sodium Chloride 140-146 matrix metallopeptidase 2 Rattus norvegicus 75-79 15525463-1 2004 AIM: To explore whether the angiotensin II (Ang II) receptor 1 (AT1) antagonist, losartan could reduce activity and expression of matrix metalloproteinases (MMPs) in rat atherosclerotic plaques. Losartan 81-89 matrix metallopeptidase 2 Rattus norvegicus 157-161 15534918-1 2004 AIM: To determine the dynamic changes in the expression of matrix metalloproteinases (MMPs) and the endogenous tissue inhibitors of MMPs inhibitors (TIMPs) during hepatic fibrosis induced by alcohol. Alcohols 191-198 matrix metallopeptidase 2 Rattus norvegicus 86-90 15534918-1 2004 AIM: To determine the dynamic changes in the expression of matrix metalloproteinases (MMPs) and the endogenous tissue inhibitors of MMPs inhibitors (TIMPs) during hepatic fibrosis induced by alcohol. Alcohols 191-198 matrix metallopeptidase 2 Rattus norvegicus 132-136 15522203-6 2004 Furthermore, 8-bromo-cAMP, an analogue of cAMP, mimicked the effect of AM, and H-89, an inhibitor for protein kinase A (PKA), significantly decreased the basal and AM-induced MMP-2 activity. 8-Bromo Cyclic Adenosine Monophosphate 13-25 matrix metallopeptidase 2 Rattus norvegicus 175-180 15522203-6 2004 Furthermore, 8-bromo-cAMP, an analogue of cAMP, mimicked the effect of AM, and H-89, an inhibitor for protein kinase A (PKA), significantly decreased the basal and AM-induced MMP-2 activity. Cyclic AMP 21-25 matrix metallopeptidase 2 Rattus norvegicus 175-180 15522203-6 2004 Furthermore, 8-bromo-cAMP, an analogue of cAMP, mimicked the effect of AM, and H-89, an inhibitor for protein kinase A (PKA), significantly decreased the basal and AM-induced MMP-2 activity. N-(2-(4-bromocinnamylamino)ethyl)-5-isoquinolinesulfonamide 79-83 matrix metallopeptidase 2 Rattus norvegicus 175-180 15522203-7 2004 CONCLUSION: This study provides a new insight into the biological action of AM and its intracellular signaling system of cAMP/PKA stimulating the matrix degrading enzyme MMP-2, suggesting an important role for this molecule in modulating ECM deposition in the adventitial layer. Cyclic AMP 121-125 matrix metallopeptidase 2 Rattus norvegicus 170-175 22900357-2 2004 Regulation of the MMPs produced by liver cells is important in maintaining cell-matrix ratio in liver, which is a major target site for hormones that mediate their intracellular effects through cAMP. Cyclic AMP 194-198 matrix metallopeptidase 2 Rattus norvegicus 18-22 22900357-3 2004 The possibility of cAMP affecting the activity of MMPs and their endogenous inhibitors, tissue inhibitor of MMPs (TIMPs) was studied using isolated rat hepatocytes in culture. Cyclic AMP 19-23 matrix metallopeptidase 2 Rattus norvegicus 50-54 22900357-8 2004 Kinetic analysis of production of MMPs and TIMPs showed that the response to Bt2 cAMP was a delayed one, indicating its effect on de novo protein synthesis. Bucladesine 77-85 matrix metallopeptidase 2 Rattus norvegicus 34-38 15525463-4 2004 In vitro, the effect of losartan 0.1-10 micromol/L on the expression of MMP-2 and MMP-9 was investigated in Ang II-stimulated rat peritoneal macrophages. Losartan 24-32 matrix metallopeptidase 2 Rattus norvegicus 72-77 15525463-5 2004 The expression and activity of MMP-2 and MMP-9 were monitored by Western blot, RT-PCR, and SDS-PAGE zymography analysis. Sodium Dodecyl Sulfate 91-94 matrix metallopeptidase 2 Rattus norvegicus 31-36 15525463-7 2004 Losartan significantly reduced the activity and expression of MMP-2 and MMP-9 compared with the placebo group (MMP-2, 5861+/-539 vs 8991+/-965, P<0.05; MMP-9,10527+/-1002 vs 14623+/-2462, P<0.01). Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 62-67 15525463-7 2004 Losartan significantly reduced the activity and expression of MMP-2 and MMP-9 compared with the placebo group (MMP-2, 5861+/-539 vs 8991+/-965, P<0.05; MMP-9,10527+/-1002 vs 14623+/-2462, P<0.01). Losartan 0-8 matrix metallopeptidase 2 Rattus norvegicus 111-116 15525463-8 2004 In cultured rat peritoneal macrophages, Ang II 0.1 micromol/L elicited an increase in MMP-2 and MMP-9 activity and expression that were prevented by losartan in a dose-dependent manner (P<0.01). Losartan 149-157 matrix metallopeptidase 2 Rattus norvegicus 86-91 15525463-10 2004 CONCLUSION: Losartan reduced the expression and activity of MMP-2 and MMP-9 in rat atherosclerotic lesions. Losartan 12-20 matrix metallopeptidase 2 Rattus norvegicus 60-65 15571005-0 2004 The anti-fibrotic effect of pirfenidone in rat liver fibrosis is mediated by downregulation of procollagen alpha1(I), TIMP-1 and MMP-2. pirfenidone 28-39 matrix metallopeptidase 2 Rattus norvegicus 129-134 15571005-6 2004 Treatment with dimethylnitrosamine increased transcripts levels for transforming growth factorbeta1, procollagen alpha1(I), tissue inhibitors of metalloproteinase-1 and matrix metalloproteinase-2 by 7-, 7-, 4- and 15-fold, respectively. Dimethylnitrosamine 15-34 matrix metallopeptidase 2 Rattus norvegicus 145-195 15571005-8 2004 CONCLUSIONS: (1) Pirfenidone is effective also if administered after the induction of the hepatic damage; (2) the anti-fibrotic effect of pirfenidone is mainly due to the reduced expression of profibrogenic procollagen alpha1(I) and TIMP-1, most likely through the downregulation of transforming growth factorbeta1 mRNA, and of matrix metalloproteinase-2, which is mainly implicated in the degradation of the normal extracellular matrix. pirfenidone 138-149 matrix metallopeptidase 2 Rattus norvegicus 328-354 15221343-6 2004 The results of this study indicated that the beneficial effect of magnesium supplementation on the cardiac disease may be due, at least in part, to the inhibitory effect of magnesium on production of MMPs in cardiac fibroblasts, which appears to be mediated by a protein tyrosine phosphorylation related signal transduction pathway. Tyrosine 271-279 matrix metallopeptidase 2 Rattus norvegicus 200-204 15557917-6 2004 RESULTS: In normal Krebs solution (2.5 mmol/L Ca2+ ) phenylephrine (10-5 mol/L) caused contraction of the aortic strips, which was significantly inhibited (P < .05) by MMP-2 (maximum, 48.9% +/- 5.0%) and to a greater extent by MMP-9 (maximum, 69.8% +/- 6.2%). Phenylephrine 53-66 matrix metallopeptidase 2 Rattus norvegicus 171-176 15557917-8 2004 The inhibitory effects of MMPs on phenylephrine contraction were reversible. Phenylephrine 34-47 matrix metallopeptidase 2 Rattus norvegicus 26-30 15557917-9 2004 In Ca2+ -free (2 mmol/L ethylene glycol bis[beta-aminoethyl ether]-N,N,N",N"-tetraacetic acid) Krebs solution phenylephrine caused a small contraction that was not inhibited by MMP-2 or MMP-9, which suggests that MMPs do not inhibit Ca2+ release from the intracellular stores. Phenylephrine 110-123 matrix metallopeptidase 2 Rattus norvegicus 177-182 15557917-9 2004 In Ca2+ -free (2 mmol/L ethylene glycol bis[beta-aminoethyl ether]-N,N,N",N"-tetraacetic acid) Krebs solution phenylephrine caused a small contraction that was not inhibited by MMP-2 or MMP-9, which suggests that MMPs do not inhibit Ca2+ release from the intracellular stores. Phenylephrine 110-123 matrix metallopeptidase 2 Rattus norvegicus 213-217 15557917-10 2004 Membrane depolarization with 96 mmol/L of potassium chloride, which stimulates Ca2+ entry from the extracellular space, caused a time-dependent and reversible contraction, which was inhibited by MMP-2 and MMP-9. Potassium Chloride 42-60 matrix metallopeptidase 2 Rattus norvegicus 195-200 15557917-12 2004 MMP-2 and MMP-9 also caused significant inhibition of 45Ca2+ influx induced by phenylephrine and potassium chloride. Phenylephrine 79-92 matrix metallopeptidase 2 Rattus norvegicus 0-5 15557917-12 2004 MMP-2 and MMP-9 also caused significant inhibition of 45Ca2+ influx induced by phenylephrine and potassium chloride. Potassium Chloride 97-115 matrix metallopeptidase 2 Rattus norvegicus 0-5 15477110-10 2004 The animals given ONO-4817 exhibited a significant decrease in the percentage of affected vessels, in the percentage of intimal proliferation, in the intima-to-media ratio, and in the expression of MMP-2 and TIMP-2. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 18-26 matrix metallopeptidase 2 Rattus norvegicus 198-203 15320878-12 2004 Moreover, GXM therapy could diminish MMP-2 activity, but it had no notable effect on apoptosis. glucuronoxylomannan 10-13 matrix metallopeptidase 2 Rattus norvegicus 37-42 15215045-5 2004 MMP activities were determined by SDS-gelatin-, casein-, and carboxymethyl transferrin-polyacrylamide gel zymography. Sodium Dodecyl Sulfate 34-37 matrix metallopeptidase 2 Rattus norvegicus 0-3 15215045-5 2004 MMP activities were determined by SDS-gelatin-, casein-, and carboxymethyl transferrin-polyacrylamide gel zymography. polyacrylamide 87-101 matrix metallopeptidase 2 Rattus norvegicus 0-3 15243304-9 2004 Data indicated that nifedipine might increase MMP-2 expression through a possible NO-dependent pathway. Nifedipine 20-30 matrix metallopeptidase 2 Rattus norvegicus 46-51 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Amlodipine 4-14 matrix metallopeptidase 2 Rattus norvegicus 35-40 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Amlodipine 4-14 matrix metallopeptidase 2 Rattus norvegicus 179-184 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Genistein 109-118 matrix metallopeptidase 2 Rattus norvegicus 35-40 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Genistein 109-118 matrix metallopeptidase 2 Rattus norvegicus 179-184 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. herbimycin 123-135 matrix metallopeptidase 2 Rattus norvegicus 35-40 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. herbimycin 123-135 matrix metallopeptidase 2 Rattus norvegicus 179-184 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Amlodipine 153-163 matrix metallopeptidase 2 Rattus norvegicus 35-40 15243304-11 2004 The amlodipine-induced decrease of MMP-2 expression was abolished by two protein tyrosine kinase inhibitors, genistein and herbimycin A, indicating that amlodipine might decrease MMP-2 expression through a possible protein tyrosine kinase pathway. Amlodipine 153-163 matrix metallopeptidase 2 Rattus norvegicus 179-184 15451797-7 2004 NAC treatment, which replenished cardiac glutathione, had no effect on hypertension but reduced LV remodeling and dysfunction, normalized serum TNF-alpha level, and limited activation of matrix metalloproteinases -2 and -9 and collagen deposition in LV tissues. Acetylcysteine 0-3 matrix metallopeptidase 2 Rattus norvegicus 187-222 15326086-11 2004 The expression of the mRNA of all TGF-beta isoforms of collagen type I and type III, and of the matrix metalloproteinase (MMP)-2 and its inhibitor TIMP-2 was reduced predominantly by alpha-adrenoceptor blockade with prazosin. Prazosin 216-224 matrix metallopeptidase 2 Rattus norvegicus 96-128 15461845-13 2004 Dexamethasone could down-regulate the mRNA expressions of MMP-2 and MMP-9 in a concentration dependent manner. Dexamethasone 0-13 matrix metallopeptidase 2 Rattus norvegicus 58-63 15461845-15 2004 Decreasing ratios of MMP-2/TIMP-2 and MMP-9/TIMP-1 were found in correlation with increasing concentration of dexamethasone. Dexamethasone 110-123 matrix metallopeptidase 2 Rattus norvegicus 21-26 15269222-6 2004 Chelerythrine, an inhibitor of PKC, inhibited activation of ERK1/2 and JNKs and expression and activity of both MMPs. chelerythrine 0-13 matrix metallopeptidase 2 Rattus norvegicus 112-116 15350851-6 2004 By zymography, MMP-2 activity was increased by cyclical stretch that was significantly attenuated by losartan and AG-490. Losartan 101-109 matrix metallopeptidase 2 Rattus norvegicus 15-20 15350851-6 2004 By zymography, MMP-2 activity was increased by cyclical stretch that was significantly attenuated by losartan and AG-490. alpha-cyano-(3,4-dihydroxy)-N-benzylcinnamide 114-120 matrix metallopeptidase 2 Rattus norvegicus 15-20 15243304-4 2004 Using gelatin zymography, Western blotting, Griess reagent, and a calcium kit-fluo 3, we investigated the effects of nifedipine, verapamil, diltiazem, and amlodipine on MMP-2 expression and further elucidate the mechanisms in cultured rat cardiac fibroblasts. Amlodipine 155-165 matrix metallopeptidase 2 Rattus norvegicus 169-174 15243304-5 2004 Nifedipine increased and amlodipine decreased the expression of MMP-2; however, neither verapamil nor diltiazem altered MMP-2 expression. Amlodipine 25-35 matrix metallopeptidase 2 Rattus norvegicus 64-69 15243304-7 2004 Nifedipine-induced MMP-2 expression was also blunted by L-NAME. Nifedipine 0-10 matrix metallopeptidase 2 Rattus norvegicus 19-24 15243304-7 2004 Nifedipine-induced MMP-2 expression was also blunted by L-NAME. NG-Nitroarginine Methyl Ester 56-62 matrix metallopeptidase 2 Rattus norvegicus 19-24 15288472-9 2004 Following FTS treatment, the MMP-2 and MMP-9-induced collagenolytic activity and TIMP-2 expression, were increased in FTS-compared to PBS-treated rats. Lead 134-137 matrix metallopeptidase 2 Rattus norvegicus 29-34 15221343-0 2004 Effects of magnesium on matrix metalloproteinase-2 production in cultured rat cardiac fibroblasts. Magnesium 11-20 matrix metallopeptidase 2 Rattus norvegicus 24-50 15221343-5 2004 Using gelatin zymography and western blotting, we found that magnesium reduced MMP-2 production dose-dependently, and this effect was inhibited by the tyrosine kinase inhibitors, genistein or herbimycin A. Magnesium 61-70 matrix metallopeptidase 2 Rattus norvegicus 79-84 15221343-5 2004 Using gelatin zymography and western blotting, we found that magnesium reduced MMP-2 production dose-dependently, and this effect was inhibited by the tyrosine kinase inhibitors, genistein or herbimycin A. Genistein 179-188 matrix metallopeptidase 2 Rattus norvegicus 79-84 15221343-5 2004 Using gelatin zymography and western blotting, we found that magnesium reduced MMP-2 production dose-dependently, and this effect was inhibited by the tyrosine kinase inhibitors, genistein or herbimycin A. herbimycin 192-204 matrix metallopeptidase 2 Rattus norvegicus 79-84 15221343-6 2004 The results of this study indicated that the beneficial effect of magnesium supplementation on the cardiac disease may be due, at least in part, to the inhibitory effect of magnesium on production of MMPs in cardiac fibroblasts, which appears to be mediated by a protein tyrosine phosphorylation related signal transduction pathway. Magnesium 66-75 matrix metallopeptidase 2 Rattus norvegicus 200-204 15221343-6 2004 The results of this study indicated that the beneficial effect of magnesium supplementation on the cardiac disease may be due, at least in part, to the inhibitory effect of magnesium on production of MMPs in cardiac fibroblasts, which appears to be mediated by a protein tyrosine phosphorylation related signal transduction pathway. Magnesium 173-182 matrix metallopeptidase 2 Rattus norvegicus 200-204 15265379-0 2004 Effects of pioglitazone on expressions of matrix metalloproteinases 2 and 9 in kidneys of diabetic rats. Pioglitazone 11-23 matrix metallopeptidase 2 Rattus norvegicus 42-75 15265379-10 2004 All diabetes-associated changes in MMP-2 expression were attenuated by pioglitazone treatment in association with reduced C-IV accumulation. Pioglitazone 71-83 matrix metallopeptidase 2 Rattus norvegicus 35-40 15265379-12 2004 Pioglitazone treatment, which can attenuate the decrease of glomerular MMP-2 and the increase of C-IV degradation, has curative effects on diabetic nephropathy. Pioglitazone 0-12 matrix metallopeptidase 2 Rattus norvegicus 71-76 15128883-2 2004 Although we have shown previously that matrix metalloproteinase-2 (MMP-2) is increased in peritoneal injury leading to SP/EPS, most of the MMP-2 in the dialysate drained from the peritoneal cavity was the latent form that was lacking activity. sp 119-121 matrix metallopeptidase 2 Rattus norvegicus 67-72 15296945-7 2004 In protein-protein binding assays, 2% DMSO disrupted gelatin interactions of both rCBD and rMMP-2. Dimethyl Sulfoxide 38-42 matrix metallopeptidase 2 Rattus norvegicus 91-97 15128883-2 2004 Although we have shown previously that matrix metalloproteinase-2 (MMP-2) is increased in peritoneal injury leading to SP/EPS, most of the MMP-2 in the dialysate drained from the peritoneal cavity was the latent form that was lacking activity. sp 119-121 matrix metallopeptidase 2 Rattus norvegicus 39-65 15493832-1 2004 AIM: To investigate the effect of puerarin on expressions of MMP-2 and TIMP-2 in the kidney of diabetic rats. puerarin 34-42 matrix metallopeptidase 2 Rattus norvegicus 61-66 15493832-7 2004 CONCLUSION: Puerarin showed some renal protective effect on diabetic nephropathy, partly through inhibition of excessive deposition of glomeruli extracellular matrix by up-regulating MMP-2 and down-regulating TIMP-2 expressions besides reducing the blood glucose. puerarin 12-20 matrix metallopeptidase 2 Rattus norvegicus 183-188 15130778-1 2004 Reactive oxygen species (ROS) have been implicated in the regulation of matrix metalloproteinases (MMPs). Reactive Oxygen Species 0-23 matrix metallopeptidase 2 Rattus norvegicus 99-103 15130778-1 2004 Reactive oxygen species (ROS) have been implicated in the regulation of matrix metalloproteinases (MMPs). Reactive Oxygen Species 25-28 matrix metallopeptidase 2 Rattus norvegicus 99-103 15130778-14 2004 The results also suggest that caution needs to be taken when interpreting the reported results on activation of MMPs where X/XO had been used as an "authentic" source of superoxide anion. Superoxides 170-186 matrix metallopeptidase 2 Rattus norvegicus 112-116 15279727-1 2004 PURPOSE: AG3340 (prinomastat) is a nonpeptidic, small-molecular-weight, synthetic matrix metalloproteinase inhibitor (MMPI) with selective inhibitory action of MMP-2, MMP-9, MMP-3, and MT-MMP1. prinomastat 9-15 matrix metallopeptidase 2 Rattus norvegicus 160-165 15081471-10 2004 Noncalcified, explanted aluminum-pretreated elastin exhibited reduced activities of MMPs. Aluminum 24-32 matrix metallopeptidase 2 Rattus norvegicus 84-88 15161499-1 2004 OBJECTIVE: To study the role of changes of matrix metalloproteinase-2, 9 (MMP-2, 9) activity in the development of dimethylnitrosamine (DMN)-induced liver fibrosis in rats. Dimethylnitrosamine 136-139 matrix metallopeptidase 2 Rattus norvegicus 74-79 15095483-8 2004 Thioacetamide-induced liver fibrosis was associated with increased levels of MMP-9 and MMP-2, correlating with the severity of the disease. Thioacetamide 0-13 matrix metallopeptidase 2 Rattus norvegicus 87-92 15161499-8 2004 RESULTS: The MMP-2, 9 activity (gray value) significantly increased in the 2d and 3d DMN model rats (2d: normal/model group, MMP-2: 54.72+/-4.56/70.76+/-7.63; F = 16.27, P < 0.05; MMP-9: 25.72+/-4.29/51.76+/-15.33, F=13.38, P < 0.05). Dimethylnitrosamine 85-88 matrix metallopeptidase 2 Rattus norvegicus 13-18 15161499-1 2004 OBJECTIVE: To study the role of changes of matrix metalloproteinase-2, 9 (MMP-2, 9) activity in the development of dimethylnitrosamine (DMN)-induced liver fibrosis in rats. Dimethylnitrosamine 115-134 matrix metallopeptidase 2 Rattus norvegicus 43-72 15161499-8 2004 RESULTS: The MMP-2, 9 activity (gray value) significantly increased in the 2d and 3d DMN model rats (2d: normal/model group, MMP-2: 54.72+/-4.56/70.76+/-7.63; F = 16.27, P < 0.05; MMP-9: 25.72+/-4.29/51.76+/-15.33, F=13.38, P < 0.05). Dimethylnitrosamine 85-88 matrix metallopeptidase 2 Rattus norvegicus 125-130 15161499-1 2004 OBJECTIVE: To study the role of changes of matrix metalloproteinase-2, 9 (MMP-2, 9) activity in the development of dimethylnitrosamine (DMN)-induced liver fibrosis in rats. Dimethylnitrosamine 115-134 matrix metallopeptidase 2 Rattus norvegicus 74-79 14761280-9 2004 Perindopril treatment significantly reduced mean fibrosis score, messenger RNA and protein levels of AT1 receptor, protein levels of TGF-beta1 and PDGF-BB, Serum levels of HA and LN, and MMP-2 activity. Perindopril 0-11 matrix metallopeptidase 2 Rattus norvegicus 187-192 15161499-1 2004 OBJECTIVE: To study the role of changes of matrix metalloproteinase-2, 9 (MMP-2, 9) activity in the development of dimethylnitrosamine (DMN)-induced liver fibrosis in rats. Dimethylnitrosamine 136-139 matrix metallopeptidase 2 Rattus norvegicus 43-72 14645107-8 2004 Using an in vivo model to study AJ dynamics where adult rats were treated with 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide (AF-2364) to disrupt Sertoli-germ cell adhesive function, an induction of active MMP-2, active MT1-MMP and TIMP-2 but not active MMP-9 was detected between 0.5 and 8 h after AF-2364 treatment. 1-(2,4-dichlorobenzyl)indazole-3-carbohydrazide 79-127 matrix metallopeptidase 2 Rattus norvegicus 209-214 14645107-10 2004 Perhaps the most important of all, the use of a specific MMP-2 and MMP-9 inhibitor, (2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid, could effectively delay the AF-2364-induced elongating/elongate spermatid loss from the epithelium, demonstrating the pivotal role of MMP-2 activation in ES disassembly. mmp-2/mmp-9 inhibitor i 84-143 matrix metallopeptidase 2 Rattus norvegicus 57-62 14645107-10 2004 Perhaps the most important of all, the use of a specific MMP-2 and MMP-9 inhibitor, (2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid, could effectively delay the AF-2364-induced elongating/elongate spermatid loss from the epithelium, demonstrating the pivotal role of MMP-2 activation in ES disassembly. mmp-2/mmp-9 inhibitor i 84-143 matrix metallopeptidase 2 Rattus norvegicus 279-284 14645107-10 2004 Perhaps the most important of all, the use of a specific MMP-2 and MMP-9 inhibitor, (2R)-2-[(4-biphenylylsulfonyl)amino]-3-phenylpropionic acid, could effectively delay the AF-2364-induced elongating/elongate spermatid loss from the epithelium, demonstrating the pivotal role of MMP-2 activation in ES disassembly. 1-(2,4-dichlorobenzyl)indazole-3-carbohydrazide 173-180 matrix metallopeptidase 2 Rattus norvegicus 57-62 14960172-5 2004 Active form of MMP-2 was detected by gelatin zymography in the conditioned medium of HSCs cultured on type I collagen gel, whereas it was not detected when HSCs were cultured on polystyrene, type I collagen-coated surface, or Matrigel. Polystyrenes 178-189 matrix metallopeptidase 2 Rattus norvegicus 15-20 15038770-4 2004 Studies using the transcription inhibitor actinomycin D (ActD) added 24 h after irradiation revealed the t(1/2) of Mmp2 mRNA to be approximately 8 h in control cells. Dactinomycin 42-55 matrix metallopeptidase 2 Rattus norvegicus 115-119 15038770-5 2004 In contrast, the increase in Mmp2 mRNA levels in irradiated cells was essentially unchanged after incubation with ActD for up to 12 h. Incubating cells with the antioxidants N-acetylcysteine or ebselen or the MEK pathway inhibitors PD98059 and U0126 prior to irradiation abolished the radiation-induced up-regulation of Mmp2. Acetylcysteine 174-190 matrix metallopeptidase 2 Rattus norvegicus 29-33 14987950-8 2004 SB203580 diminished the reduction of mRNA as well as the activity of TIMP-1 by TJ-9 and induction of mRNA as well as the activity of MMP-2. SB 203580 0-8 matrix metallopeptidase 2 Rattus norvegicus 133-138 15053235-5 2004 Osteoblasts from distal femoral head showed an increase in the pattern of MT1-MMP mRNA and protein production in sham-operated controls and 17beta-estradiol (E2)-treated rats, compared with the ovariectomized group; the synthesis of MMP-2 and TIMP-2 mRNA and protein was unaffected. Estradiol 140-156 matrix metallopeptidase 2 Rattus norvegicus 233-238 15026117-1 2004 The effect of treatment with a broad-spectrum inhibitor (BB1101) of the matrix metalloproteinases (MMPs) on nerve regeneration and functional recovery after nerve crush was examined. BB 1101 57-63 matrix metallopeptidase 2 Rattus norvegicus 99-103 15026117-7 2004 In situ zymography confirmed that the activity of MMPs in the nerve was increased following crush but that the activity was greatly reduced in rats treated with BB-1101. BB 1101 161-168 matrix metallopeptidase 2 Rattus norvegicus 50-54 15026117-8 2004 Thus despite the inhibition of MMPs by BB-1101, the drug did not appear to essentially affect nerve degeneration or regeneration following nerve crush but that it could be beneficial in promoting the more effective reinnervation of muscles possibly by actions at the level of the muscles. BB 1101 39-46 matrix metallopeptidase 2 Rattus norvegicus 31-35 14500723-6 2003 Inhibition of PKC using chelerythrine inhibited the activities of both MMP-2 and MMP-9. chelerythrine 24-37 matrix metallopeptidase 2 Rattus norvegicus 71-76 14593002-3 2003 Using chronically instrumented conscious rats, we demonstrated that a specific peptide inhibitor of the gelatinases MMP-2 and -9, cyclic CTTHWGFTLC (cyclic CTT), but not the control peptide, STTHWGFTLS (STT), completely reversed renal vasodilation and hyperfiltration in relaxin-treated rats. cyclo(Cys-Thr-Thr-His-Trp-Gly-Phe-Thr-Leu-Cys) 130-147 matrix metallopeptidase 2 Rattus norvegicus 116-128 14593002-4 2003 Comparable findings were observed with a structurally different and well-established, general antagonist of MMPs, GM6001. N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide 114-120 matrix metallopeptidase 2 Rattus norvegicus 108-112 14593002-7 2003 Moreover, a neutralizing antibody specific for MMP-2 completely abrogated the reduced myogenic reactivity of small renal arteries from relaxin-treated nonpregnant and midterm pregnant rats. Relaxin 135-142 matrix metallopeptidase 2 Rattus norvegicus 47-52 14593002-9 2003 Using gelatin zymography, we showed increased pro and active MMP-2 activity in small renal arteries from relaxin-treated nonpregnant and midterm pregnant rats relative to the control animals. Relaxin 105-112 matrix metallopeptidase 2 Rattus norvegicus 61-66 14586590-1 2003 BACKGROUND: N-Biphenyl sulfonyl-phenylalanine hydroxamic acid (BPHA), a synthetic, selective matrix metalloproteinase (MMP)-2, -9, -14 inhibitor, has been reported to show significant antiangiogenic activity without unpleasant adverse effects. N-biphenylsulfonylphenylalanine hydroxamic acid 12-61 matrix metallopeptidase 2 Rattus norvegicus 93-125 14586590-1 2003 BACKGROUND: N-Biphenyl sulfonyl-phenylalanine hydroxamic acid (BPHA), a synthetic, selective matrix metalloproteinase (MMP)-2, -9, -14 inhibitor, has been reported to show significant antiangiogenic activity without unpleasant adverse effects. N-biphenylsulfonylphenylalanine hydroxamic acid 63-67 matrix metallopeptidase 2 Rattus norvegicus 93-125 14507662-1 2003 Recent research has shown that the tetracycline antibiotics are pluripotent drugs that inhibit the activity of matrix metalloproteinases (MMPs) and affect many cellular functions including proliferation, migration, and matrix remodeling. Tetracycline 35-47 matrix metallopeptidase 2 Rattus norvegicus 138-142 14648529-11 2003 On days 6, 10, and 13, TCC-treated wounds contained significantly lower concentrations of TNF-alpha and MMP-2 and MMP-9 than control wounds. Triclocarban 23-26 matrix metallopeptidase 2 Rattus norvegicus 104-109 14529574-9 2003 RESULTS: MMP-1, MMP-2, MMP-8 and MMP-9 expression were detected at 48 hrs in undebrided corneal epithelium groups treated with the topical fluoroquinolones. Fluoroquinolones 139-155 matrix metallopeptidase 2 Rattus norvegicus 16-21 14529574-13 2003 CONCLUSIONS: Our study provides preliminary evidence that topical application of fluoroquinolone drugs can induce the expression of MMP-1, MMP-2, MMP-8 and MMP-9 in the undebrided corneal epithelium compared to artificial tear eye drops. Fluoroquinolones 81-96 matrix metallopeptidase 2 Rattus norvegicus 139-144 14577597-6 2003 Cromolyn induced a slight depression of the NE-induced elevation of the matrix metalloproteinase (MMP)-2. Cromolyn Sodium 0-8 matrix metallopeptidase 2 Rattus norvegicus 72-104 12949732-4 2003 RESULTS: In the monocrotaline-induced rat model of sinusoidal obstruction syndrome, there was an early increase of matrix metalloproteinase-9 and a later, lower-magnitude increase of matrix metalloproteinase-2 in the liver. Monocrotaline 16-29 matrix metallopeptidase 2 Rattus norvegicus 183-209 14619580-9 2003 MMP-2 and TIMP-1mRNA levels in asthmatic group (0.68 +/- 0.14, 0.56 +/- 0.10) and dexamethasone group (0.37 +/- 0.11, 0.31 +/- 0.10) were significantly higher than those in control group (0.14 +/- 0.03, 0.11 +/- 0.05). Dexamethasone 82-95 matrix metallopeptidase 2 Rattus norvegicus 0-5 14619580-12 2003 There was a significant positive correlation between MMP-2 and TIMP-1 mRNA in control group and dexamethasone group (r = 0.67, 0.58, P < 0.05), but not in asthmatic group (r = 0.24, P > 0.05). Dexamethasone 96-109 matrix metallopeptidase 2 Rattus norvegicus 53-58 14619580-13 2003 CONCLUSION: Dexamethasone could prevent airway remodeling by downregulating the expression of MMP-2 and TIMP-1 and restoring the balance between MMP-2 and TIMP-1. Dexamethasone 12-25 matrix metallopeptidase 2 Rattus norvegicus 94-99 14619580-13 2003 CONCLUSION: Dexamethasone could prevent airway remodeling by downregulating the expression of MMP-2 and TIMP-1 and restoring the balance between MMP-2 and TIMP-1. Dexamethasone 12-25 matrix metallopeptidase 2 Rattus norvegicus 145-150 12949732-8 2003 CONCLUSIONS: Monocrotaline causes depolymerization of F-actin in sinusoidal endothelial cells, which leads to increased expression of metalloproteinase-9 and matrix metalloproteinase-2 by sinusoidal endothelial cells. Monocrotaline 13-26 matrix metallopeptidase 2 Rattus norvegicus 134-184 14575305-2 2003 Since matrix metalloproteinases (MMPs) are activated in vitro by peroxynitrite, we hypothezised that MMPs may contribute to cardiac mechanical dysfunction in sepsis. Peroxynitrous Acid 65-78 matrix metallopeptidase 2 Rattus norvegicus 33-37 14575305-2 2003 Since matrix metalloproteinases (MMPs) are activated in vitro by peroxynitrite, we hypothezised that MMPs may contribute to cardiac mechanical dysfunction in sepsis. Peroxynitrous Acid 65-78 matrix metallopeptidase 2 Rattus norvegicus 101-105 14575305-12 2003 The MMP inhibitors significantly improved cardiac function of LPS-treated rats (Ro 31-9790: 38 +/- 3, doxycycline: 51 +/- 3 mmHg*mL*min(-1)), had no effect on the loss of MMP-2 activity, and significantly reduced the MMP-9 activity in the perfusate. 3, doxycycline 99-113 matrix metallopeptidase 2 Rattus norvegicus 4-7 12873732-0 2003 Analgesic effect of intrathecally administered matrix metalloproteinase 2 (MMP-2) in the rat formalin test. Formaldehyde 93-101 matrix metallopeptidase 2 Rattus norvegicus 47-73 12873732-0 2003 Analgesic effect of intrathecally administered matrix metalloproteinase 2 (MMP-2) in the rat formalin test. Formaldehyde 93-101 matrix metallopeptidase 2 Rattus norvegicus 75-80 12873732-2 2003 In the present study, the authors examined the effect of intrathecal injection of MMP-2 on the nociceptive transmission during the rat formalin test (a model of inflammatory pain). Formaldehyde 135-143 matrix metallopeptidase 2 Rattus norvegicus 82-87 12873732-4 2003 Intrathecal injection of 1 microg of MMP-2 depressed the phase 1 agitation behavior, but not the phase 2 agitation behavior, and this effect of MMP-2 was antagonized by ONO-4817, an MMP inhibitor. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 169-177 matrix metallopeptidase 2 Rattus norvegicus 37-42 12873732-4 2003 Intrathecal injection of 1 microg of MMP-2 depressed the phase 1 agitation behavior, but not the phase 2 agitation behavior, and this effect of MMP-2 was antagonized by ONO-4817, an MMP inhibitor. N-hydroxy-5-ethoxymethyloxy-2-methyl-4-(4-phenoxybenzoyl)aminopentanamide 169-177 matrix metallopeptidase 2 Rattus norvegicus 144-149 12873732-6 2003 These data suggest that exogenously applied MMP-2 to the spinal cord produces analgesic effects in the rat formalin test. Formaldehyde 107-115 matrix metallopeptidase 2 Rattus norvegicus 44-49 12930639-15 2003 Both of perindopril and losartan treatment significantly reduced mean fibrosis score, messenger RNA and protein levels of AT1 receptor, protein levels of TGF-beta1 and PDGF-BB, Serum levels of HA and LN, and MMP-2 activity. Perindopril 8-19 matrix metallopeptidase 2 Rattus norvegicus 208-213 12930639-15 2003 Both of perindopril and losartan treatment significantly reduced mean fibrosis score, messenger RNA and protein levels of AT1 receptor, protein levels of TGF-beta1 and PDGF-BB, Serum levels of HA and LN, and MMP-2 activity. Losartan 24-32 matrix metallopeptidase 2 Rattus norvegicus 208-213 12706262-6 2003 Activation experiments with amino phenyl mercuric acetate suggested that the 52-54 kDa gelatin-degrading activity was an activated form of MMP-2. amino phenyl mercuric acetate 28-57 matrix metallopeptidase 2 Rattus norvegicus 139-144 12791179-1 2003 AIM: To investigate the effects of high glucose on expression of matrix metalloproteinase-2 (MMP-2) in rat aortic smooth muscle cells and the influence of matrix remodeling on atherogenesis in diabetic patients. Glucose 40-47 matrix metallopeptidase 2 Rattus norvegicus 65-91 12791179-1 2003 AIM: To investigate the effects of high glucose on expression of matrix metalloproteinase-2 (MMP-2) in rat aortic smooth muscle cells and the influence of matrix remodeling on atherogenesis in diabetic patients. Glucose 40-47 matrix metallopeptidase 2 Rattus norvegicus 93-98 12746943-0 2003 Early postnatal dexamethasone influences matrix metalloproteinase-2 and -9, and their tissue inhibitors in the developing rat lung. Dexamethasone 16-29 matrix metallopeptidase 2 Rattus norvegicus 41-74 12746943-1 2003 In order to test the hypothesis that early postnatal exposure to dexamethasone (Dex) influences matrix metalloproteinases (MMP)-2 and -9, as well as their tissue inhibitors (TIMP-1 and -2) in the developing rat lung, newborn rats (3 litters/group) were treated with low Dex (0.1 mg/kg/day, IM), high Dex (0.5 mg/kg/day), or equivalent volumes of saline at 5 days postnatal age (P5), P6, and P7. Dexamethasone 65-78 matrix metallopeptidase 2 Rattus norvegicus 96-136 12746943-1 2003 In order to test the hypothesis that early postnatal exposure to dexamethasone (Dex) influences matrix metalloproteinases (MMP)-2 and -9, as well as their tissue inhibitors (TIMP-1 and -2) in the developing rat lung, newborn rats (3 litters/group) were treated with low Dex (0.1 mg/kg/day, IM), high Dex (0.5 mg/kg/day), or equivalent volumes of saline at 5 days postnatal age (P5), P6, and P7. Dexamethasone 80-83 matrix metallopeptidase 2 Rattus norvegicus 96-136 12746943-9 2003 These data provide evidence that early postnatal dexamethasone results in an imbalance between gelatinase-A and -B, and their tissue inhibitors in the developing rat lung. Dexamethasone 49-62 matrix metallopeptidase 2 Rattus norvegicus 95-114 12850461-2 2003 We hypothesized that COL-3, a chemically modified tetracycline known to inhibit MMP-2 and MMP-9, would reduce lung injury and improve survival in rats following cecal ligation and puncture (CLP). Tetracycline 50-62 matrix metallopeptidase 2 Rattus norvegicus 80-85 12535739-6 2003 Magnesium reduced MMP-2 production dose-dependently at basal and PDGF-stimulated conditions in VSMCs. Magnesium 0-9 matrix metallopeptidase 2 Rattus norvegicus 18-23 12934382-7 2003 The mRNA expression of MMP-2 and MMP-9 in the lymphocytes of the peripheral blood and spleen and the protein expression of MMP-2 and MMP-9 in the muscle tissues all increased significantly in the EAM group compared with those of the control group. molibresib 196-199 matrix metallopeptidase 2 Rattus norvegicus 23-28 12934382-7 2003 The mRNA expression of MMP-2 and MMP-9 in the lymphocytes of the peripheral blood and spleen and the protein expression of MMP-2 and MMP-9 in the muscle tissues all increased significantly in the EAM group compared with those of the control group. molibresib 196-199 matrix metallopeptidase 2 Rattus norvegicus 123-128 12934382-8 2003 However, the mRNA and protein expression of MMP-2 and MM-9 was suppressed significantly in contrast with that in the EAM group. molibresib 117-120 matrix metallopeptidase 2 Rattus norvegicus 44-49 12934382-13 2003 Methylprednisolone may reduce the pathological damages of EAM, and this protective mechanism may be due to the inhibited expression of MMP-2 and MMP-9 and promoted expression of TIMP-1. Methylprednisolone 0-18 matrix metallopeptidase 2 Rattus norvegicus 135-140 12639820-0 2003 Cyclosporine A up-regulates expression of matrix metalloproteinase 2 and vascular endothelial growth factor in rat heart. Cyclosporine 0-14 matrix metallopeptidase 2 Rattus norvegicus 42-68 12639820-3 2003 Since the immunosuppressive therapy induces myocardial toxicity, the aim of this study was to evaluate in the myocardium of CsA-treated rats the expression variations of vascular endothelial growth factor (VEGF) and matrix metalloproteinase 2 (MMP2), to verify if: VEGF increased, VEGF increase was associated with MMP2 increase and they could be considered as repair proteins. Cyclosporine 124-127 matrix metallopeptidase 2 Rattus norvegicus 216-242 12639820-3 2003 Since the immunosuppressive therapy induces myocardial toxicity, the aim of this study was to evaluate in the myocardium of CsA-treated rats the expression variations of vascular endothelial growth factor (VEGF) and matrix metalloproteinase 2 (MMP2), to verify if: VEGF increased, VEGF increase was associated with MMP2 increase and they could be considered as repair proteins. Cyclosporine 124-127 matrix metallopeptidase 2 Rattus norvegicus 244-248 12639820-3 2003 Since the immunosuppressive therapy induces myocardial toxicity, the aim of this study was to evaluate in the myocardium of CsA-treated rats the expression variations of vascular endothelial growth factor (VEGF) and matrix metalloproteinase 2 (MMP2), to verify if: VEGF increased, VEGF increase was associated with MMP2 increase and they could be considered as repair proteins. Cyclosporine 124-127 matrix metallopeptidase 2 Rattus norvegicus 315-319 12639820-7 2003 The group II animals (CsA-treated) showed structural degenerative changes with myocardial fibrosis and a clear increase both in MMP2 and VEGF. Cyclosporine 22-25 matrix metallopeptidase 2 Rattus norvegicus 128-132 12535739-8 2003 The effect of magnesium on the production of MMP-2 was inhibited by two tyrosine kinase inhibitors-genistein and herbimycin A. Magnesium 14-23 matrix metallopeptidase 2 Rattus norvegicus 45-50 12535739-8 2003 The effect of magnesium on the production of MMP-2 was inhibited by two tyrosine kinase inhibitors-genistein and herbimycin A. Genistein 99-108 matrix metallopeptidase 2 Rattus norvegicus 45-50 12535739-8 2003 The effect of magnesium on the production of MMP-2 was inhibited by two tyrosine kinase inhibitors-genistein and herbimycin A. herbimycin 113-125 matrix metallopeptidase 2 Rattus norvegicus 45-50 12535739-9 2003 The results of this study indicate that extracellularly added magnesium decreased MMPs secretion, which appears to be associated with protein tyrosine kinase. Magnesium 62-71 matrix metallopeptidase 2 Rattus norvegicus 82-86 12524413-11 2003 The effect of ethanol and acetaldehyde on MMP2 and TIMP2 secretion was also assessed by this method. Acetaldehyde 26-38 matrix metallopeptidase 2 Rattus norvegicus 42-46 12371906-3 2003 Culture of rat cardiac fibroblasts for 24 h in 1% oxygen enhanced MMP-2 synthesis by more than 5-fold and augmented the MMP-2 synthetic responses of these cells to endothelin-1, angiotensin II and interleukin 1beta. Oxygen 50-56 matrix metallopeptidase 2 Rattus norvegicus 66-71 12371906-3 2003 Culture of rat cardiac fibroblasts for 24 h in 1% oxygen enhanced MMP-2 synthesis by more than 5-fold and augmented the MMP-2 synthetic responses of these cells to endothelin-1, angiotensin II and interleukin 1beta. Oxygen 50-56 matrix metallopeptidase 2 Rattus norvegicus 120-125 12566110-6 2003 The activity of MMP-2 was increased both in the LV and RV after 3 days of NE infusion and reduced after concomitant doxycycline treatment which also caused inhibition when given alone. Doxycycline 116-127 matrix metallopeptidase 2 Rattus norvegicus 16-21 12524413-15 2003 Ethanol and acetaldehyde induced secretion of both MMP2 and TIMP2 by PSCs. Ethanol 0-7 matrix metallopeptidase 2 Rattus norvegicus 51-55 12524413-15 2003 Ethanol and acetaldehyde induced secretion of both MMP2 and TIMP2 by PSCs. Acetaldehyde 12-24 matrix metallopeptidase 2 Rattus norvegicus 51-55 12524413-18 2003 Both ethanol and its metabolite acetaldehyde increase MMP2 as well as TIMP2 secretion by PSCs. Ethanol 5-12 matrix metallopeptidase 2 Rattus norvegicus 54-58 12524413-18 2003 Both ethanol and its metabolite acetaldehyde increase MMP2 as well as TIMP2 secretion by PSCs. Acetaldehyde 32-44 matrix metallopeptidase 2 Rattus norvegicus 54-58 12044662-12 2002 SDS-PAGE zymography differentiated between a high level of activated MMPs in the ischemic area and a low level in the non-ischemic basal ganglia. Sodium Dodecyl Sulfate 0-3 matrix metallopeptidase 2 Rattus norvegicus 69-73 12419858-3 2002 Acute alachlor exposure caused upregulation of matrix metalloproteinases (MMP)-2 and -9, tissue inhibitor of metalloproteinase-1, carboxypeptidase Z, and other genes related to extracellular matrix homeostasis. alachlor 6-14 matrix metallopeptidase 2 Rattus norvegicus 47-87 12477525-0 2002 Nitric oxide induces gelatinase A (matrix metalloproteinase 2) during rat embryo implantation. Nitric Oxide 0-12 matrix metallopeptidase 2 Rattus norvegicus 21-33 12477525-0 2002 Nitric oxide induces gelatinase A (matrix metalloproteinase 2) during rat embryo implantation. Nitric Oxide 0-12 matrix metallopeptidase 2 Rattus norvegicus 35-61 12477525-1 2002 OBJECTIVE: To evaluate a reciprocal signaling interaction initiated by embryo-derived nitric oxide (NO) to facilitate implantation by increased production of gelatinase A (matrix metalloproteinase 2, MMP2) in uterine stroma. Nitric Oxide 86-98 matrix metallopeptidase 2 Rattus norvegicus 158-170 12477525-1 2002 OBJECTIVE: To evaluate a reciprocal signaling interaction initiated by embryo-derived nitric oxide (NO) to facilitate implantation by increased production of gelatinase A (matrix metalloproteinase 2, MMP2) in uterine stroma. Nitric Oxide 86-98 matrix metallopeptidase 2 Rattus norvegicus 172-198 12477525-1 2002 OBJECTIVE: To evaluate a reciprocal signaling interaction initiated by embryo-derived nitric oxide (NO) to facilitate implantation by increased production of gelatinase A (matrix metalloproteinase 2, MMP2) in uterine stroma. Nitric Oxide 86-98 matrix metallopeptidase 2 Rattus norvegicus 200-204 12553043-3 2002 ATRA significantly and dose-dependently inhibited matrigel membrane invasion of the cells by 53%, inhibited MMP-2 activity by 71%, MMP-9(80%), alpha-(59%) and beta-(65%) catenin expression at 10 microM (p < 0.01). Tretinoin 0-4 matrix metallopeptidase 2 Rattus norvegicus 108-113 12470508-16 2002 The zymographic analysis revealed a temporal increase in MMP-2 activity from 4 to 8 weeks post homocysteine administration. Homocysteine 95-107 matrix metallopeptidase 2 Rattus norvegicus 57-62 12470508-20 2002 The results suggest that in the absence of endothelial NO, and in an attempt to reduce LV load, MMP-2 is activated and CIMP is inactivated, by increasing nitrotyrosine. 3-nitrotyrosine 154-167 matrix metallopeptidase 2 Rattus norvegicus 96-101 12114911-1 2002 OBJECTIVE: Our purpose was to examine whether the type IV collagenases (metalloproteinase [MMP]-2 and MMP-9) and their inhibitors (TIMP-1 and TIMP-2) are regulated by a prostaglandin E(2) (PGE(2))-cyclic adenosine monophosphate (cAMP) mechanism in nonpregnant virgin, preterm and term pregnant and postpartum rats. Dinoprostone 169-187 matrix metallopeptidase 2 Rattus norvegicus 91-97 12114911-1 2002 OBJECTIVE: Our purpose was to examine whether the type IV collagenases (metalloproteinase [MMP]-2 and MMP-9) and their inhibitors (TIMP-1 and TIMP-2) are regulated by a prostaglandin E(2) (PGE(2))-cyclic adenosine monophosphate (cAMP) mechanism in nonpregnant virgin, preterm and term pregnant and postpartum rats. Dinoprostone 189-196 matrix metallopeptidase 2 Rattus norvegicus 91-97 12114911-1 2002 OBJECTIVE: Our purpose was to examine whether the type IV collagenases (metalloproteinase [MMP]-2 and MMP-9) and their inhibitors (TIMP-1 and TIMP-2) are regulated by a prostaglandin E(2) (PGE(2))-cyclic adenosine monophosphate (cAMP) mechanism in nonpregnant virgin, preterm and term pregnant and postpartum rats. Cyclic AMP 197-227 matrix metallopeptidase 2 Rattus norvegicus 91-97 12114911-1 2002 OBJECTIVE: Our purpose was to examine whether the type IV collagenases (metalloproteinase [MMP]-2 and MMP-9) and their inhibitors (TIMP-1 and TIMP-2) are regulated by a prostaglandin E(2) (PGE(2))-cyclic adenosine monophosphate (cAMP) mechanism in nonpregnant virgin, preterm and term pregnant and postpartum rats. Cyclic AMP 229-233 matrix metallopeptidase 2 Rattus norvegicus 91-97 12114911-4 2002 RESULTS: PGE(2) evoked elevations in plasma and tissue levels of cAMP and MMP-2 in the preterm and term pregnant rats. Prostaglandins E 9-12 matrix metallopeptidase 2 Rattus norvegicus 74-79 12146531-9 2002 Immunohistochemistry was positive for TNF, IL-1, and IL-6 in the inflammatory cells from untreated endotoxin rat tissues, whereas treatment with CMTs decreased the number of immuno-positive stained cells for cytokines and MMPs. cmts 145-149 matrix metallopeptidase 2 Rattus norvegicus 222-226 12042738-9 2002 Rat aortic smooth muscle cell MMP-2 activity is inhibited with dexamethasone in a dose-dependent fashion, and human aortic smooth muscle cell MMP-2 activity is unchanged with dexamethasone. Dexamethasone 63-76 matrix metallopeptidase 2 Rattus norvegicus 30-35 12042738-10 2002 MMP-2 secretion is inhibited with dexamethasone in rat aortic smooth muscle cells but remains unaltered in human aortic smooth muscle cells. Dexamethasone 34-47 matrix metallopeptidase 2 Rattus norvegicus 0-5 12042738-12 2002 CONCLUSION: Dexamethasone inhibits rat aortic smooth muscle cell migration, MMP-2 activity, and MMP-2 secretion and increases TIMP-2 secretion. Dexamethasone 12-25 matrix metallopeptidase 2 Rattus norvegicus 76-81 12042738-12 2002 CONCLUSION: Dexamethasone inhibits rat aortic smooth muscle cell migration, MMP-2 activity, and MMP-2 secretion and increases TIMP-2 secretion. Dexamethasone 12-25 matrix metallopeptidase 2 Rattus norvegicus 96-101 12042638-8 2002 RESULTS: Intrarenal expression of TGF-beta, collagen, fibronectin, MMP-2, MMP-9, and tissue inhibitor of MMP-2 was significantly increased in rats treated with CsA for 180 days compared with untreated rats and those treated for 30 days. Cyclosporine 160-163 matrix metallopeptidase 2 Rattus norvegicus 67-72 12042638-8 2002 RESULTS: Intrarenal expression of TGF-beta, collagen, fibronectin, MMP-2, MMP-9, and tissue inhibitor of MMP-2 was significantly increased in rats treated with CsA for 180 days compared with untreated rats and those treated for 30 days. Cyclosporine 160-163 matrix metallopeptidase 2 Rattus norvegicus 105-110 12107433-2 2002 The major objective of this communication is to construct a phenotypic signature for cells of the nucleus pulposus that is based on the hypothesis that in response to restriction on oxygen and nutrient flux, there is expression of HIF-1, GLUT-1 and MMP-2. Oxygen 182-188 matrix metallopeptidase 2 Rattus norvegicus 249-254 11984824-6 2002 Furthermore, the 67 kDa MMP-2 can be converted to 64 kDa forms by incubation with p-aminophenylmercuric acetate (APMA) and trypsin in vitro. 4-aminophenylmercuriacetate 82-111 matrix metallopeptidase 2 Rattus norvegicus 24-29 11984824-6 2002 Furthermore, the 67 kDa MMP-2 can be converted to 64 kDa forms by incubation with p-aminophenylmercuric acetate (APMA) and trypsin in vitro. 4-aminophenylmercuriacetate 113-117 matrix metallopeptidase 2 Rattus norvegicus 24-29 12133319-13 2002 (3) MMP-2 and TIMP-1 mRNA levels in the L-arginine group and the asthmatic group were significantly higher than that in the control group [L-arginine group (0.82 +/- 0.11), (0.51 +/- 0.12); asthmatic group (0.68 +/- 0.14), (0.56 +/- 0.10); control group (0.14 +/- 0.03), (0.11 +/- 0.05), respectively]. Arginine 40-50 matrix metallopeptidase 2 Rattus norvegicus 4-9 12032490-12 2002 During weeks 1 and 2 and compared with untreated controls, doxycycline-treated rats had attenuated pouch tissue weight, collagen concentration, MMP2 lytic activity and vascularity, and reduced exudate volume and mononuclear cells. Doxycycline 59-70 matrix metallopeptidase 2 Rattus norvegicus 144-148 12032490-16 2002 As repair proceeds in subsequent weeks, doxycycline retards collagen degradation and pouch resorption by inhibiting MMPs. Doxycycline 40-51 matrix metallopeptidase 2 Rattus norvegicus 116-120 11961487-0 2002 Long-term overexpression of membrane type-1 matrix metalloproteinase and matrix metalloproteinase-2 in oleic acid-induced pancreatitis in rats. Oleic Acid 103-113 matrix metallopeptidase 2 Rattus norvegicus 73-99 11961487-4 2002 RESULTS: Gelatinolytic activity of pro-and active MMP-2 and concentrations of MT1-MMP protein, as determined by zymography and Western blot analysis, respectively, increased significantly from 6 hours to day 42 after intraductal infusion of oleic acid. Oleic Acid 241-251 matrix metallopeptidase 2 Rattus norvegicus 50-55 11961487-7 2002 CONCLUSION: Our findings indicate that long-term increases of gelatinolytic activity of active MMP-2 cause continuous disorganization of type IV collagen in basement membranes during progressive atrophy of pancreatic gland in oleic acid-induced pancreatitis, and that MT1-MMP and TIMP-2 work as activating factors during proMMP-2 activation. Oleic Acid 226-236 matrix metallopeptidase 2 Rattus norvegicus 95-100 11971672-1 2002 OBJECTIVE: Nitric oxide (NO) may mediate vessel wall remodeling by regulating expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Nitric Oxide 11-23 matrix metallopeptidase 2 Rattus norvegicus 119-123 12133319-14 2002 The difference in the MMP-2 mRNA levels was significant between the L-arginine group and the asthmatic group (P < 0.05), but the difference in the TIMP-1 mRNA levels between the two groups was not statistically significant. Arginine 68-78 matrix metallopeptidase 2 Rattus norvegicus 22-27 12133319-16 2002 (4) A significant positive correlation was found between the MMP-2 mRNA levels and nitrites/nitrates levels in L-arginine group and asthmatic group (r(s) = 0.65, 0.68, P < 0.05), but there was no significant correlation between the nitrites/nitrates levels and the TIMP-1 mRNA levels in the two groups (r(s) = 0.23, 0.18, P > 0.05). Nitrites 83-91 matrix metallopeptidase 2 Rattus norvegicus 61-66 12133319-16 2002 (4) A significant positive correlation was found between the MMP-2 mRNA levels and nitrites/nitrates levels in L-arginine group and asthmatic group (r(s) = 0.65, 0.68, P < 0.05), but there was no significant correlation between the nitrites/nitrates levels and the TIMP-1 mRNA levels in the two groups (r(s) = 0.23, 0.18, P > 0.05). Nitrates 92-100 matrix metallopeptidase 2 Rattus norvegicus 61-66 12133319-16 2002 (4) A significant positive correlation was found between the MMP-2 mRNA levels and nitrites/nitrates levels in L-arginine group and asthmatic group (r(s) = 0.65, 0.68, P < 0.05), but there was no significant correlation between the nitrites/nitrates levels and the TIMP-1 mRNA levels in the two groups (r(s) = 0.23, 0.18, P > 0.05). Arginine 111-121 matrix metallopeptidase 2 Rattus norvegicus 61-66 12133319-16 2002 (4) A significant positive correlation was found between the MMP-2 mRNA levels and nitrites/nitrates levels in L-arginine group and asthmatic group (r(s) = 0.65, 0.68, P < 0.05), but there was no significant correlation between the nitrites/nitrates levels and the TIMP-1 mRNA levels in the two groups (r(s) = 0.23, 0.18, P > 0.05). Nitrites 235-243 matrix metallopeptidase 2 Rattus norvegicus 61-66 12133319-16 2002 (4) A significant positive correlation was found between the MMP-2 mRNA levels and nitrites/nitrates levels in L-arginine group and asthmatic group (r(s) = 0.65, 0.68, P < 0.05), but there was no significant correlation between the nitrites/nitrates levels and the TIMP-1 mRNA levels in the two groups (r(s) = 0.23, 0.18, P > 0.05). Nitrates 244-252 matrix metallopeptidase 2 Rattus norvegicus 61-66 11960381-2 2002 A novel inhibitor, Ro 28-2653, with high selectivity for MMP2, MMP9 and membrane type 1-MMP was evaluated in an orthotopic prostate cancer rat model. Ro 28-2653 19-29 matrix metallopeptidase 2 Rattus norvegicus 57-61 11955860-3 2002 METHODS: In Dahl salt-sensitive rats with hypertension, in which a stage of concentric, compensated left ventricular hypertrophy (LVH) at 11 weeks is followed by a distinct stage of congestive heart failure (CHF) with LV enlargement and dysfunction at 17 weeks, we determined protein and messenger ribonucleic acid (mRNA) levels of LV myocardial TIMP-2 and -4 and MMP-2, as well as their concomitant activities. Salts 17-21 matrix metallopeptidase 2 Rattus norvegicus 364-369 11995922-6 2002 Furthermore, dexamethasone (a down-regulator of MMP and PA) and TNP-470 (an endothelial cell growth inhibitor) induced another capillary morphology. Dexamethasone 13-26 matrix metallopeptidase 2 Rattus norvegicus 48-51 12039062-6 2002 Interestingly, TNFalpha reversed FSH- and cytochalasin D-induced effects both on cell shape and on MMP-2 and TIMP-2. Cytochalasin D 42-56 matrix metallopeptidase 2 Rattus norvegicus 99-104 11935159-11 2002 Activation of latent MMPs with amino-phenylmercuric acetate increased matrix degradation by two-fold. amino-phenylmercuric acetate 31-59 matrix metallopeptidase 2 Rattus norvegicus 21-25 11891205-4 2002 Doxycycline reduced the activity of matrix metalloproteinase (MMP)-2 and MMP-9 in the arterial wall, and inhibited smooth muscle cell migration from media to intima by 77% at 4 days after balloon injury. Doxycycline 0-11 matrix metallopeptidase 2 Rattus norvegicus 36-68 11914010-10 2002 CONCLUSION: pirfenidone reduces expression of MMPs governing smooth muscle cell proliferation and migration (MMP-2 and 9), and genes favouring ECM accumulation (TIMP-1 and collagen III). pirfenidone 12-23 matrix metallopeptidase 2 Rattus norvegicus 46-50 11914010-10 2002 CONCLUSION: pirfenidone reduces expression of MMPs governing smooth muscle cell proliferation and migration (MMP-2 and 9), and genes favouring ECM accumulation (TIMP-1 and collagen III). pirfenidone 12-23 matrix metallopeptidase 2 Rattus norvegicus 109-120 11914015-0 2002 Up-regulation of MMP-2 and MMP-9 leads to degradation of type IV collagen during skeletal muscle reperfusion injury; protection by the MMP inhibitor, doxycycline. Doxycycline 150-161 matrix metallopeptidase 2 Rattus norvegicus 17-22 11914015-1 2002 OBJECTIVES: to determine the role of matrix metalloproteinases, MMP-2 and MMP-9, in reperfusion injury following skeletal muscle ischaemia and whether inhibition of MMPs by doxycycline protects against tissue damage. Doxycycline 173-184 matrix metallopeptidase 2 Rattus norvegicus 165-169 11939349-9 2002 The data provided in this study may be useful in designing selective therapy for painful neuropathy using synthetic hydroxamate MMP inhibitors. hydroxamate 116-127 matrix metallopeptidase 2 Rattus norvegicus 128-131 12617792-8 2002 In conclusion, the results show that the uterine MMP2 activity, which is higher in diabetic animals than in control animals, is modulated positively by NO and ROS during embryo implantation in a model of streptozotocin-induced diabetic rats. Reactive Oxygen Species 159-162 matrix metallopeptidase 2 Rattus norvegicus 49-53 11744025-0 2002 Peroxynitrite-induced myocardial injury is mediated through matrix metalloproteinase-2. Peroxynitrous Acid 0-13 matrix metallopeptidase 2 Rattus norvegicus 60-86 11744025-10 2002 The MMPs inhibitor PD-166793 prevented the ONOO(-)-induced loss in myocardial mechanical function. (R)-2-(4'-bromo-biphenyl-4-sulfonyl-amino)-3-methyl-butyric acid 19-28 matrix metallopeptidase 2 Rattus norvegicus 4-8 11744025-10 2002 The MMPs inhibitor PD-166793 prevented the ONOO(-)-induced loss in myocardial mechanical function. onoo(-) 43-50 matrix metallopeptidase 2 Rattus norvegicus 4-8 11744025-12 2002 CONCLUSIONS: Acute cardiac toxicity induced by ONOO(-) is mediated by MMP-2. onoo(-) 47-54 matrix metallopeptidase 2 Rattus norvegicus 70-75 11851355-7 2002 Ramipril reduced MMP-2 expression (active form), collagen type I mRNA expression and content and increased TIMP-4 levels associated with decreased left ventricular end diastolic pressure (LVEDP), mortality rate and increased LV pressure (LVP). Ramipril 0-8 matrix metallopeptidase 2 Rattus norvegicus 17-22 11851355-8 2002 Combination therapy with furosemide is less efficient with regard to collagen content and MMP-2 (active form) reduction but did not worsen beneficial effects of ramipril on LV function and mortality rate. Furosemide 25-35 matrix metallopeptidase 2 Rattus norvegicus 90-95 11795999-9 2002 Zymography showed that DEX inhibits MMP-2 activity in a dose-dependent manner. Dexamethasone 23-26 matrix metallopeptidase 2 Rattus norvegicus 36-41 11795999-11 2002 CONCLUSIONS: DEX inhibits platelet-derived growth factor-induced migration of RASMCs and MMP-2 activity in vitro. Dexamethasone 13-16 matrix metallopeptidase 2 Rattus norvegicus 89-94 12238810-3 2002 Three major bands with gelatinolytic activity were detected at all periods and characterized as the latent and active forms of MMP-2 using their molecular weight and activity dependent on Zn++ and Ca++ ions as criteria. Zinc 188-192 matrix metallopeptidase 2 Rattus norvegicus 127-132 12617792-8 2002 In conclusion, the results show that the uterine MMP2 activity, which is higher in diabetic animals than in control animals, is modulated positively by NO and ROS during embryo implantation in a model of streptozotocin-induced diabetic rats. Streptozocin 204-218 matrix metallopeptidase 2 Rattus norvegicus 49-53 11983005-0 2002 Chemically modified tetracycline (CMT-8) and estrogen promote wound healing in ovariectomized rats: effects on matrix metalloproteinase-2, membrane type 1 matrix metalloproteinase, and laminin-5 gamma2-chain. cmt 34-37 matrix metallopeptidase 2 Rattus norvegicus 111-179 11733347-4 2001 Subdermal implantation of AlCl(3)-pretreated elastin showed significantly lower MMP-9 and MMP-2 activity surrounding the implant as compared to the control implants. Aluminum Chloride 26-33 matrix metallopeptidase 2 Rattus norvegicus 90-95 11866990-2 2001 METHODS: (1) Dynamic changes of MMP(2) expression were observed in bleomycin-induced rat pulmonary fibrosis by use of immunohistochemical technique. Bleomycin 67-76 matrix metallopeptidase 2 Rattus norvegicus 32-38 11866990-5 2001 RESULTS: (1) On day 1-7th after receiving bleomycin, the infiltrated pulmonary macrophages and septa mesenchymal cells showed positive reaction with anti-MMP(2) and an increase in number. Bleomycin 42-51 matrix metallopeptidase 2 Rattus norvegicus 154-160 11866990-7 2001 (2) The gene expression of MMP(2) mRNA of PFbs were enhanced after bleomycin treatment from the Day 1 and decreased by Day 28. Bleomycin 67-76 matrix metallopeptidase 2 Rattus norvegicus 27-33 11684074-1 2001 OBJECTIVE: In this study we have tested the hypothesis that degradation of collagen by matrix metalloproteinase 2 (MMP-2) precedes the deposition of extracellular matrix (ECM) after long term norepinephrine (NE) treatment. Norepinephrine 192-206 matrix metallopeptidase 2 Rattus norvegicus 87-113 11684074-1 2001 OBJECTIVE: In this study we have tested the hypothesis that degradation of collagen by matrix metalloproteinase 2 (MMP-2) precedes the deposition of extracellular matrix (ECM) after long term norepinephrine (NE) treatment. Norepinephrine 192-206 matrix metallopeptidase 2 Rattus norvegicus 115-120 11549451-1 2001 This letter describes SAR exploration and rat PK optimization of a series of novel, MMP-1 sparing aryl hydroxamate sulfonamides with activity against MMP-2 and MMP-13. aryl hydroxamate sulfonamides 98-127 matrix metallopeptidase 2 Rattus norvegicus 150-155 11819847-5 2001 Compared the varied duration of hypoxia, the changes of expressions including mRNA and protein level as well as activity of MMP-2 were most notable in 6h group. 6H 151-153 matrix metallopeptidase 2 Rattus norvegicus 124-129 11819847-7 2001 In the situation of hyperoxia for 12h, the contents (A(450)) of MMP-2 and TIMP-2 in supernatant were both higher than those in the control, especially the TIMP-2 (hyperoxia group: 0.0499 +/- 0.0144, n = 16; control: 0.0219 +/- 0.0098, n = 14; P < 0.01), and so was the activity of MMP-2 (hyperoxia group: 5.252 +/- 0.771, n = 14; control: 4.304 +/- 1.083, n = 12; P < 0.05), and the expression of MT1-MMP was increased. 12-hydroxydodecanoic acid 34-37 matrix metallopeptidase 2 Rattus norvegicus 64-69 11819847-8 2001 CONCLUSION: HSC is sensitive to the oxygen, hypoxia enhances the expression of MMP-2 and the effect is more marked at the early stage; hyperoxia mainly raises the activity of MMP-2. Oxygen 36-42 matrix metallopeptidase 2 Rattus norvegicus 79-84 11819847-8 2001 CONCLUSION: HSC is sensitive to the oxygen, hypoxia enhances the expression of MMP-2 and the effect is more marked at the early stage; hyperoxia mainly raises the activity of MMP-2. Oxygen 36-42 matrix metallopeptidase 2 Rattus norvegicus 175-180 11757635-6 2001 Increased MMP-2 activity was also found 30 days postmonocrotaline. postmonocrotaline 48-65 matrix metallopeptidase 2 Rattus norvegicus 10-15 15348357-7 2001 Metalloproteinase (MMP-2) activity was detected in all the samples analyzed but a higher expression of MMP-9 was detected in those implants treated with chloroform/methanol and ethanol. Chloroform 153-163 matrix metallopeptidase 2 Rattus norvegicus 19-24 15348357-7 2001 Metalloproteinase (MMP-2) activity was detected in all the samples analyzed but a higher expression of MMP-9 was detected in those implants treated with chloroform/methanol and ethanol. Methanol 164-172 matrix metallopeptidase 2 Rattus norvegicus 19-24 15348357-7 2001 Metalloproteinase (MMP-2) activity was detected in all the samples analyzed but a higher expression of MMP-9 was detected in those implants treated with chloroform/methanol and ethanol. Ethanol 165-172 matrix metallopeptidase 2 Rattus norvegicus 19-24 11507770-5 2001 Investigation of this layer in every resorption area by gelatin histozymography and TIMP-2 histochemistry demonstrates the presence of an MMP whose histozymographic activity is inhibited by such a low dose of the inhibitor CT1746 as to identify it as gelatinase A or B. CT 1746 223-229 matrix metallopeptidase 2 Rattus norvegicus 138-141 11550211-6 2001 Positive immunolabeling of matrix metalloproteinases 2 (MMP-2) and 9 (MMP-9) was detected in the fibromuscular layer surrounding the adenoma and adenocarcinoma induced in LP and VP after treatments with steroids for over 9-12 months. Steroids 203-211 matrix metallopeptidase 2 Rattus norvegicus 56-68 11420061-4 2001 Here, using a rat molar model, it is demonstrated that CyA immunosuppression inhibits the activity of matrix metalloproteinases 2 and 9 in the early phase of granulation tissue in the healing dental socket. Cyclosporine 55-58 matrix metallopeptidase 2 Rattus norvegicus 102-135 11532435-6 2001 SDS-PAGE zymography was used to measure MMP2 and MMP9 activities. Sodium Dodecyl Sulfate 0-3 matrix metallopeptidase 2 Rattus norvegicus 40-44 11507770-5 2001 Investigation of this layer in every resorption area by gelatin histozymography and TIMP-2 histochemistry demonstrates the presence of an MMP whose histozymographic activity is inhibited by such a low dose of the inhibitor CT1746 as to identify it as gelatinase A or B. CT 1746 223-229 matrix metallopeptidase 2 Rattus norvegicus 251-263 11565871-6 2001 Finally, using semiquantitative reverse transcriptase-polymerase chain reaction, the authors demonstrated that LY294002 decreased messenger (m)RNA levels for both MMPs. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 111-119 matrix metallopeptidase 2 Rattus norvegicus 163-167 11520947-3 2001 Since the RH protocol consists of 2-acetylaminofluorene (2-AAF) followed by a PH, we reasoned that MMP-2 and -9 might be critical for the growth of lesions. 2-Acetylaminofluorene 34-55 matrix metallopeptidase 2 Rattus norvegicus 99-111 11520947-3 2001 Since the RH protocol consists of 2-acetylaminofluorene (2-AAF) followed by a PH, we reasoned that MMP-2 and -9 might be critical for the growth of lesions. 2-Acetylaminofluorene 57-62 matrix metallopeptidase 2 Rattus norvegicus 99-111 11520947-9 2001 They then received either the MMP inhibitor batimastat (30 mg/kg, intraperitoneally) or vehicle alone daily from Day 3 to 20 post-PH and were sacrificed on Day 21. batimastat 44-54 matrix metallopeptidase 2 Rattus norvegicus 30-33 11435213-8 2001 Lungs from copper-deficient rats had much higher levels of matrix metalloproteinase (MMP)-2 and MMP-9 than did copper-adequate control animals. Copper 11-17 matrix metallopeptidase 2 Rattus norvegicus 59-91 11758165-6 2001 RESULTS: (1) The MMP-2 gene expression of fibroblasts increased 2.05 times(t = 10.667, P < 0.01) higher than that of control in 24 hours after bleomycin instillation and remained at the high level until the 28th day after exposure. Bleomycin 146-155 matrix metallopeptidase 2 Rattus norvegicus 17-22 11410620-2 2001 Using a standard ISH protocol, we hybridized serial sections of paraffin blocks stored for different periods of time with (33)P-labeled riboprobes specific for rat Type III collagen and matrix metalloproteinase-2 (MMP-2). Phosphorus-33 122-127 matrix metallopeptidase 2 Rattus norvegicus 214-219 11438504-7 2001 RESULTS: Captopril treatment significantly reduced hepatic hydroxyproline levels, mean fibrosis score, steady state messenger RNA levels of TGF-beta1 and procollagen alpha1(I), and matrix metalloproteinase 2 and 9 activity. Captopril 9-18 matrix metallopeptidase 2 Rattus norvegicus 181-207 11382924-7 2001 Secretion of one or both MMPs was inhibited by EGF, TGFalpha, prolactin, and hydrocortisone and stimulated by progesterone. Hydrocortisone 77-91 matrix metallopeptidase 2 Rattus norvegicus 25-29 11382924-7 2001 Secretion of one or both MMPs was inhibited by EGF, TGFalpha, prolactin, and hydrocortisone and stimulated by progesterone. Progesterone 110-122 matrix metallopeptidase 2 Rattus norvegicus 25-29 11382924-8 2001 Furthermore, the functional significance of MMPs was demonstrated since three MMP inhibitors blocked branching morphogenesis elicited by the absence of hydrocortisone. Hydrocortisone 152-166 matrix metallopeptidase 2 Rattus norvegicus 44-48 11435218-8 2001 Inhibition of MMPs with doxycycline reduced the migration of AEC from hyperoxic rats to the level of control adult AEC. Doxycycline 24-35 matrix metallopeptidase 2 Rattus norvegicus 14-18 11487304-9 2001 Serum MMP-9 and active MMP-2 were suppressed (P<0.05) by addition of either CLA or DHA. Linoleic Acids, Conjugated 79-82 matrix metallopeptidase 2 Rattus norvegicus 23-28 11487304-9 2001 Serum MMP-9 and active MMP-2 were suppressed (P<0.05) by addition of either CLA or DHA. Docosahexaenoic Acids 86-89 matrix metallopeptidase 2 Rattus norvegicus 23-28 11222998-16 2001 The hydroxymate-type, MMP inhibitor, BB-1101, blocked the activation of MMP-2 and MMP-9 by LPS in mixed glial cultures. hydroxymate 4-15 matrix metallopeptidase 2 Rattus norvegicus 72-77 11249854-2 2001 Addition of the ET(A) receptor antagonists or neutralizing anti-endothelin antibody into MC cultures markedly augmented the secretion and activation of MMP-2. Methylcholanthrene 89-91 matrix metallopeptidase 2 Rattus norvegicus 152-157 11249854-3 2001 On the contrary, addition of the exogenous ET-1 into MC culture significantly inhibited the synthesis of MMP-2 in both basal and cytokines (tumor necrosis factor-alpha and interferon-gamma) plus lipopolysaccharide-stimulated conditions. Methylcholanthrene 53-55 matrix metallopeptidase 2 Rattus norvegicus 105-110 11249854-4 2001 Furthermore, pretreatment of cells with exogenous ET-1 obviously prevented cytochalasin D-elicited activation of MMP-2, an effect that was completely abolished by ET(A) receptor antagonist, FR139317. Cytochalasin D 75-89 matrix metallopeptidase 2 Rattus norvegicus 113-118 11249854-4 2001 Furthermore, pretreatment of cells with exogenous ET-1 obviously prevented cytochalasin D-elicited activation of MMP-2, an effect that was completely abolished by ET(A) receptor antagonist, FR139317. FR 139317 190-198 matrix metallopeptidase 2 Rattus norvegicus 113-118 11249854-6 2001 The addition of recombinant TIMP-2 into the culture abrogated dose-dependently the cytochalasin D-elicited activation of MMP-2. Cytochalasin D 83-97 matrix metallopeptidase 2 Rattus norvegicus 121-126 11283850-4 2001 Addition to the cell cultures of PGE(2) promoted the release of MMPs through a mechanism that involved the expression of COX-2 and the synthesis of additional PGs. Dinoprostone 33-39 matrix metallopeptidase 2 Rattus norvegicus 64-68 11283850-4 2001 Addition to the cell cultures of PGE(2) promoted the release of MMPs through a mechanism that involved the expression of COX-2 and the synthesis of additional PGs. Prostaglandins 159-162 matrix metallopeptidase 2 Rattus norvegicus 64-68 11283850-5 2001 Kinetic analysis of the secretion of MMPs in response to LPS and PGE(2) showed a similar time course, with a lag period of 6 hours, which suggests that PGE(2) does not act directly on the mechanism of MMP processing and release. Prostaglandins E 65-68 matrix metallopeptidase 2 Rattus norvegicus 37-41 11283850-5 2001 Kinetic analysis of the secretion of MMPs in response to LPS and PGE(2) showed a similar time course, with a lag period of 6 hours, which suggests that PGE(2) does not act directly on the mechanism of MMP processing and release. Prostaglandins E 65-68 matrix metallopeptidase 2 Rattus norvegicus 37-40 11283850-5 2001 Kinetic analysis of the secretion of MMPs in response to LPS and PGE(2) showed a similar time course, with a lag period of 6 hours, which suggests that PGE(2) does not act directly on the mechanism of MMP processing and release. Prostaglandins E 152-155 matrix metallopeptidase 2 Rattus norvegicus 37-41 11283850-5 2001 Kinetic analysis of the secretion of MMPs in response to LPS and PGE(2) showed a similar time course, with a lag period of 6 hours, which suggests that PGE(2) does not act directly on the mechanism of MMP processing and release. Prostaglandins E 152-155 matrix metallopeptidase 2 Rattus norvegicus 37-40 11283850-6 2001 Inhibitors of protein kinase A, p38 MAP kinase, phosphatidylinositol-3-kinase, and nuclear factor kappaB (NF-kappaB) activation impaired the release of MMPs in response to PGE(2) challenge, indicating the involvement of multiple steps in the process. Prostaglandins E 172-175 matrix metallopeptidase 2 Rattus norvegicus 152-156 11416886-10 2001 Enzymatic activity of both human and rat matrix metalloproteinase-2 was strongly inhibited in a dose-dependent fashion when incubated with cyanate. Cyanates 139-146 matrix metallopeptidase 2 Rattus norvegicus 41-67 11222998-16 2001 The hydroxymate-type, MMP inhibitor, BB-1101, blocked the activation of MMP-2 and MMP-9 by LPS in mixed glial cultures. BB 1101 37-44 matrix metallopeptidase 2 Rattus norvegicus 72-77 11179039-6 2001 In LV myocardium remote from the infarct, the activities of MMP-1, MMP-2, and MMP-9 were increased in the post-MI group, and the increases were prevented by sitaxsentan treatment. sitaxsentan 157-168 matrix metallopeptidase 2 Rattus norvegicus 67-72 11121376-8 2001 DDC and DHEA decreased collagen synthesis and increased MMP activity, and both effects were inhibited by an SOD/catalase mimetic. Ditiocarb 0-3 matrix metallopeptidase 2 Rattus norvegicus 56-59 11230740-4 2001 In this report we extended our studies and showed that turpentine induced, in a time-dependent manner, expression of alpha1(I) and alpha1(IV) collagens, TIMP-1, and matrix-metalloproteinase 2 (MMP-2) mRNAs. Turpentine 55-65 matrix metallopeptidase 2 Rattus norvegicus 165-191 11230740-4 2001 In this report we extended our studies and showed that turpentine induced, in a time-dependent manner, expression of alpha1(I) and alpha1(IV) collagens, TIMP-1, and matrix-metalloproteinase 2 (MMP-2) mRNAs. Turpentine 55-65 matrix metallopeptidase 2 Rattus norvegicus 193-198 11168932-11 2001 CsA-treated rats also had significantly increased TIMP-1 (7.4-fold, P < 0.001), MMP-2, and PAI-1 (all approximately 2-fold, P < 0.02) and decreased MMP-9 (85% reduction, P < 0.001) as compared with controls. Cyclosporine 0-3 matrix metallopeptidase 2 Rattus norvegicus 83-88 11121376-8 2001 DDC and DHEA decreased collagen synthesis and increased MMP activity, and both effects were inhibited by an SOD/catalase mimetic. dehydroepiandrosterone acetate 8-12 matrix metallopeptidase 2 Rattus norvegicus 56-59 11133670-0 2001 Lysyl oxidase and MMP-2 expression in dehydroepiandrosterone-induced polycystic ovary in rats. Dehydroepiandrosterone 38-60 matrix metallopeptidase 2 Rattus norvegicus 18-23 11133670-5 2001 MMP-2 mRNA expression in control rats was threefold greater than that in the DHEA-induced group (P: < 0.05). Dehydroepiandrosterone 77-81 matrix metallopeptidase 2 Rattus norvegicus 0-5 11133670-6 2001 Expression of both latent and active forms of MMP-2 in controls was more than twice that in the DHEA-induced group (P: < 0.05) as shown by Western blotting, and expression of the active form of MMP-2 was also twice as high in the controls as in the DHEA-treated group (P: < 0.05) as shown by zymography. Dehydroepiandrosterone 96-100 matrix metallopeptidase 2 Rattus norvegicus 46-51 11133670-6 2001 Expression of both latent and active forms of MMP-2 in controls was more than twice that in the DHEA-induced group (P: < 0.05) as shown by Western blotting, and expression of the active form of MMP-2 was also twice as high in the controls as in the DHEA-treated group (P: < 0.05) as shown by zymography. Dehydroepiandrosterone 96-100 matrix metallopeptidase 2 Rattus norvegicus 197-202 11133670-6 2001 Expression of both latent and active forms of MMP-2 in controls was more than twice that in the DHEA-induced group (P: < 0.05) as shown by Western blotting, and expression of the active form of MMP-2 was also twice as high in the controls as in the DHEA-treated group (P: < 0.05) as shown by zymography. Dehydroepiandrosterone 252-256 matrix metallopeptidase 2 Rattus norvegicus 197-202 11824476-10 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion. Calcium 36-43 matrix metallopeptidase 2 Rattus norvegicus 116-121 11686853-3 2001 We tested the hypothesis that a short-term in vitro exposure to domoic acid, might lead to the activation of rat neonatal microglia and the concomitant release of the putative neurotoxic mediators tumor necrosis factor-alpha (TNF-alpha), matrix metalloproteinases-2 and-9 (MMP-2 and -9) and superoxide anion (O2-). domoic acid 64-75 matrix metallopeptidase 2 Rattus norvegicus 238-271 11686853-3 2001 We tested the hypothesis that a short-term in vitro exposure to domoic acid, might lead to the activation of rat neonatal microglia and the concomitant release of the putative neurotoxic mediators tumor necrosis factor-alpha (TNF-alpha), matrix metalloproteinases-2 and-9 (MMP-2 and -9) and superoxide anion (O2-). domoic acid 64-75 matrix metallopeptidase 2 Rattus norvegicus 273-285 11824471-8 2001 Activation of PKC by phorbol ester (PMA) resulted in a decrease in ECM protein deposition and an increase in MMP-2 secretion. Phorbol Esters 21-34 matrix metallopeptidase 2 Rattus norvegicus 109-114 11824476-10 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion. 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester 49-57 matrix metallopeptidase 2 Rattus norvegicus 116-121 11824471-8 2001 Activation of PKC by phorbol ester (PMA) resulted in a decrease in ECM protein deposition and an increase in MMP-2 secretion. Tetradecanoylphorbol Acetate 36-39 matrix metallopeptidase 2 Rattus norvegicus 109-114 10775124-8 2000 These vasodilatory effects of thrombin and MMP-2 were significantly (P < 0.05) inhibited by endothelium denudation and by PD-142893 (2 nmol), an antagonist of ET receptors. PD 142893 125-134 matrix metallopeptidase 2 Rattus norvegicus 43-48 11824471-9 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion, Our results show a complex pattern of regulation of ECM protein deposition by cAMP-mobilizing agents, and also indicate an inverse correlation between ECM protein deposition and secretion of MMP-2. Calcium 36-43 matrix metallopeptidase 2 Rattus norvegicus 116-121 11824471-9 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion, Our results show a complex pattern of regulation of ECM protein deposition by cAMP-mobilizing agents, and also indicate an inverse correlation between ECM protein deposition and secretion of MMP-2. Calcium 36-43 matrix metallopeptidase 2 Rattus norvegicus 324-329 11824471-9 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion, Our results show a complex pattern of regulation of ECM protein deposition by cAMP-mobilizing agents, and also indicate an inverse correlation between ECM protein deposition and secretion of MMP-2. 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester 49-57 matrix metallopeptidase 2 Rattus norvegicus 116-121 11824471-9 2001 Finally, chelation of intercellular calcium with BAPTA-AM resulted in an increased ECM deposition and a decrease in MMP-2 secretion, Our results show a complex pattern of regulation of ECM protein deposition by cAMP-mobilizing agents, and also indicate an inverse correlation between ECM protein deposition and secretion of MMP-2. 1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester 49-57 matrix metallopeptidase 2 Rattus norvegicus 324-329 11824476-9 2001 Activation of PKC by phorbol ester (PMA) resulted in a decrease in ECM protein deposition and an increase in MMP-2 secretion. Phorbol Esters 21-34 matrix metallopeptidase 2 Rattus norvegicus 109-114 11824476-9 2001 Activation of PKC by phorbol ester (PMA) resulted in a decrease in ECM protein deposition and an increase in MMP-2 secretion. Tetradecanoylphorbol Acetate 36-39 matrix metallopeptidase 2 Rattus norvegicus 109-114 11139426-1 2000 BAY 12-9566 (4-[4-(chlorophenyl)phenyl]-4-oxo-2S-(phenylthiomethyl) butanoic acid) is a newly developed, synthetic matrix metalloproteinase (MMP) inhibitor (MMPI) that selectively inhibits MMP-2, MMP-3 and MMP-9 isozymes. Bay 12-9566 0-11 matrix metallopeptidase 2 Rattus norvegicus 141-144 11139426-1 2000 BAY 12-9566 (4-[4-(chlorophenyl)phenyl]-4-oxo-2S-(phenylthiomethyl) butanoic acid) is a newly developed, synthetic matrix metalloproteinase (MMP) inhibitor (MMPI) that selectively inhibits MMP-2, MMP-3 and MMP-9 isozymes. Bay 12-9566 0-11 matrix metallopeptidase 2 Rattus norvegicus 189-194 11139426-1 2000 BAY 12-9566 (4-[4-(chlorophenyl)phenyl]-4-oxo-2S-(phenylthiomethyl) butanoic acid) is a newly developed, synthetic matrix metalloproteinase (MMP) inhibitor (MMPI) that selectively inhibits MMP-2, MMP-3 and MMP-9 isozymes. Bay 12-9566 13-81 matrix metallopeptidase 2 Rattus norvegicus 141-144 11139426-1 2000 BAY 12-9566 (4-[4-(chlorophenyl)phenyl]-4-oxo-2S-(phenylthiomethyl) butanoic acid) is a newly developed, synthetic matrix metalloproteinase (MMP) inhibitor (MMPI) that selectively inhibits MMP-2, MMP-3 and MMP-9 isozymes. Bay 12-9566 13-81 matrix metallopeptidase 2 Rattus norvegicus 189-194 11091246-8 2000 Although cyclosporin treatment reduced levels of the matrix-degrading enzymes, matrix metalloproteinase (MMP) 2 and MMP-9, this was not statistically significant. Cyclosporine 9-20 matrix metallopeptidase 2 Rattus norvegicus 79-111 10886721-5 2000 The bands for an active form of MMP-2 were more strongly expressed in the Thy-1 + MC group than in the Thy-1 group throughout the experimental period. Methylcellulose 82-84 matrix metallopeptidase 2 Rattus norvegicus 32-37 11423724-0 2001 High glucose decreases matrix metalloproteinase-2 activity in rat mesangial cells via transforming growth factor-beta1. Glucose 5-12 matrix metallopeptidase 2 Rattus norvegicus 23-49 11423724-3 2001 We have previously demonstrated that 72 kDa type IV collagenase activity is decreased in the rat mesangial cells cultured in high glucose media [Diabetes 1995;44:929-935]. Glucose 130-137 matrix metallopeptidase 2 Rattus norvegicus 37-63 11423724-9 2001 Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. Glucose 80-87 matrix metallopeptidase 2 Rattus norvegicus 178-183 11423724-9 2001 Incubation of primary cultures of rat mesangial cells for 5 days in 30 vs. 5 mM glucose resulted in a 3-fold increase in production of total TGF-beta1, a significant decrease in MMP-2 activity and immunoreactive MMP-2 levels, and an increase in TIMP-2 levels. Glucose 80-87 matrix metallopeptidase 2 Rattus norvegicus 212-217 11423724-10 2001 Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. Glucose 69-76 matrix metallopeptidase 2 Rattus norvegicus 151-156 11423724-10 2001 Addition of exogenous TGF-beta1 to mesangial cells incubated in 5 mM glucose replicated the high glucose effect by producing a significant decrease in MMP-2 levels with a concurrent increase in TIMP-2 levels. Glucose 97-104 matrix metallopeptidase 2 Rattus norvegicus 151-156 11423724-11 2001 Furthermore, glucose-induced inhibition of MMP-2 activity was completely blocked by neutralization of TGF-beta1 with anti-TGF-beta1 antibody. Glucose 13-20 matrix metallopeptidase 2 Rattus norvegicus 43-48 11423724-12 2001 We conclude that the decrease in MMP-2 activity induced by glucose loading is mediated via TGF-beta1. Glucose 59-66 matrix metallopeptidase 2 Rattus norvegicus 33-38 11500925-6 2001 Zymographic analysis revealed increased elastinolytic gelatinase A and B (MMP-2, -9) in homocysteine treated vessels and the treatment with nicotinamide decreases the homocysteine-induced MMP activation. Homocysteine 88-100 matrix metallopeptidase 2 Rattus norvegicus 54-72 11500925-6 2001 Zymographic analysis revealed increased elastinolytic gelatinase A and B (MMP-2, -9) in homocysteine treated vessels and the treatment with nicotinamide decreases the homocysteine-induced MMP activation. Homocysteine 88-100 matrix metallopeptidase 2 Rattus norvegicus 74-79 11500925-6 2001 Zymographic analysis revealed increased elastinolytic gelatinase A and B (MMP-2, -9) in homocysteine treated vessels and the treatment with nicotinamide decreases the homocysteine-induced MMP activation. Niacinamide 140-152 matrix metallopeptidase 2 Rattus norvegicus 54-72 11500925-6 2001 Zymographic analysis revealed increased elastinolytic gelatinase A and B (MMP-2, -9) in homocysteine treated vessels and the treatment with nicotinamide decreases the homocysteine-induced MMP activation. Niacinamide 140-152 matrix metallopeptidase 2 Rattus norvegicus 74-79 11134358-8 2001 While no changes in MMP-9 were observed, conversion from pro-MMP-2 to active MMP-2 was inhibited by L-ANT. l-ant 100-105 matrix metallopeptidase 2 Rattus norvegicus 61-66 11134358-8 2001 While no changes in MMP-9 were observed, conversion from pro-MMP-2 to active MMP-2 was inhibited by L-ANT. l-ant 100-105 matrix metallopeptidase 2 Rattus norvegicus 77-82 11078924-3 2000 Two matrix metalloproteinases (MMPs), MMP-2 and MMP-9, were differentially induced with respect to time after kainic acid in sensitive brain regions in both young and old rats. Kainic Acid 110-121 matrix metallopeptidase 2 Rattus norvegicus 31-35 11078924-3 2000 Two matrix metalloproteinases (MMPs), MMP-2 and MMP-9, were differentially induced with respect to time after kainic acid in sensitive brain regions in both young and old rats. Kainic Acid 110-121 matrix metallopeptidase 2 Rattus norvegicus 38-43 11058950-6 2000 Comparing the varied duration of hypoxia, the relative amount of MMP-2 protein was the highest in 6 h group (6h vs 12h, t=4. 6H 109-111 matrix metallopeptidase 2 Rattus norvegicus 65-70 11058950-6 2000 Comparing the varied duration of hypoxia, the relative amount of MMP-2 protein was the highest in 6 h group (6h vs 12h, t=4. 12-hydroxydodecanoic acid 115-118 matrix metallopeptidase 2 Rattus norvegicus 65-70 10769285-7 2000 MMP-2 antibody (1.5 to 15 microg/mL) and the inhibitors of MMPs doxycycline (10 to 100 micromol/L) and o-phenanthroline (3 to 100 micromol/L) improved whereas MMP-2 worsened the recovery of mechanical function during reperfusion. Doxycycline 64-75 matrix metallopeptidase 2 Rattus norvegicus 59-63 10660581-11 2000 Binding of MMP-7 and other MMPs to heparan sulfate in the extracellular space could prevent loss of secreted enzyme, provide a reservoir of latent enzyme, and facilitate cellular sensing and regulation of enzyme levels. Heparitin Sulfate 35-50 matrix metallopeptidase 2 Rattus norvegicus 27-31 10719174-3 2000 The inhibition of MMP-2 and MMP-9 caused by GTP was confirmed by gelatin zymography and was observed for MMPs associated with both various rat tissues and human brain tumors (glioblastoma and pituitary tumors). epigallocatechin gallate 44-47 matrix metallopeptidase 2 Rattus norvegicus 18-23 10719174-3 2000 The inhibition of MMP-2 and MMP-9 caused by GTP was confirmed by gelatin zymography and was observed for MMPs associated with both various rat tissues and human brain tumors (glioblastoma and pituitary tumors). epigallocatechin gallate 44-47 matrix metallopeptidase 2 Rattus norvegicus 105-109 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). Catechin 69-78 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). epigallocatechin gallate 113-141 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). epigallocatechin gallate 143-147 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). epicatechin gallate 150-173 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). gallocatechol 113-133 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). gallocatechol 143-146 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). Catechin 150-165 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). Catechin 174-176 matrix metallopeptidase 2 Rattus norvegicus 18-22 10719174-4 2000 The activities of MMPs were also measured in the presence of various catechins isolated from green tea including (-)-epigallocatechin gallate (EGCG), (-)-epicatechin gallate(ECG), (-)-epigallocatechin (EGC), (-)-epicatechin (EC) and (+)-catechin (C). Catechin 233-245 matrix metallopeptidase 2 Rattus norvegicus 18-22 10660581-13 2000 Dislodging MMPs by treatment with compounds such as heparin might be beneficial in attenuating excessive tissue breakdown such as occurs in cancer metastasis, arthritis, and angiogenesis. Heparin 52-59 matrix metallopeptidase 2 Rattus norvegicus 11-15 10878458-0 2000 Matrix metalloproteinases 2 and 9 in indomethacin-induced rat gastric ulcer. Indomethacin 37-49 matrix metallopeptidase 2 Rattus norvegicus 0-33 10604929-4 2000 Carboxyamido-triazole (CAI), an inhibitor of Ca(2+)-mediated signal transduction, has been previously shown to inhibit angiogenesis in vitro and in vivo and to down-regulate matrix metalloproteinase-2 in vitro. carboxyamido-triazole 0-21 matrix metallopeptidase 2 Rattus norvegicus 174-200 10604929-4 2000 Carboxyamido-triazole (CAI), an inhibitor of Ca(2+)-mediated signal transduction, has been previously shown to inhibit angiogenesis in vitro and in vivo and to down-regulate matrix metalloproteinase-2 in vitro. carboxyamido-triazole 23-26 matrix metallopeptidase 2 Rattus norvegicus 174-200 10674388-6 1999 Moreover, topical application of 1% minoxidil sulfate to the anterior dorsal skin of rats in telogen stimulated hair growth and increased the mRNA expressions of HGF and MMP-2. minoxidil sulfate ester 36-53 matrix metallopeptidase 2 Rattus norvegicus 170-175 10894363-5 2000 SDS-PAGE zymography and Western blotting revealed that the expression of proMMP-2 in rat brains with C6 glioma cells was significantly higher than that in normal or the sham-operated rat brains, and that the activated form of MMP-2 was detected only in the former but not in the latter. Sodium Dodecyl Sulfate 0-3 matrix metallopeptidase 2 Rattus norvegicus 76-81 10597259-5 1999 In addition, treatment of SR3Y1 with manumycin A, a potent inhibitor of Ras farnesyltransferase, strongly suppressed both augmented secretion and proteolytic activation of MMP-2. manumycin 37-48 matrix metallopeptidase 2 Rattus norvegicus 172-177 10508828-3 1999 We hypothesized that glutathione depletion activates matrix metalloproteinases (MMPs), thereby increasing degradation of the alveolar extracellular matrix (ECM) during sepsis. Glutathione 21-32 matrix metallopeptidase 2 Rattus norvegicus 80-84 10508828-5 1999 Ethanol ingestion increased (p < 0.05) MMP-9 and MMP-2 activity, as determined by zymography, in the lung tissue and lavage fluid compared with control-fed rats, and increased (p < 0.05) levels of the 7S fragment of type IV collagen in the lung lavage fluid. Ethanol 0-7 matrix metallopeptidase 2 Rattus norvegicus 52-57 10508828-6 1999 Ethanol ingestion increased activation, but not production, of the MMP-9 and MMP-2 zymogens. Ethanol 0-7 matrix metallopeptidase 2 Rattus norvegicus 77-82 10508828-7 1999 Finally, although concomitant ingestion of N-acetylcysteine had no effect (p > 0.05) on MMP production, it increased (p > 0.05) lung glutathione levels, blocked (p < 0.05) MMP-9 and MMP-2 activation, and decreased (p < 0.05) levels of the 7S fragment of type IV collagen. Acetylcysteine 43-59 matrix metallopeptidase 2 Rattus norvegicus 191-196 10508828-8 1999 We conclude that chronic ethanol ingestion, via glutathione depletion, activates MMPs during sepsis, thereby increasing degradation of the alveolar epithelial ECM. Ethanol 25-32 matrix metallopeptidase 2 Rattus norvegicus 81-85 10508828-8 1999 We conclude that chronic ethanol ingestion, via glutathione depletion, activates MMPs during sepsis, thereby increasing degradation of the alveolar epithelial ECM. Glutathione 48-59 matrix metallopeptidase 2 Rattus norvegicus 81-85 10544927-5 1999 The inhibitors of protein tyrosine kinase, herbymicin A, genistein, and tyrphostin 1288 (1 to 100 microM), enhanced the basal release of MMP-2 but did not affect the thrombin-induced secretion of MMP-2. herbymicin a 43-55 matrix metallopeptidase 2 Rattus norvegicus 137-142 10544927-5 1999 The inhibitors of protein tyrosine kinase, herbymicin A, genistein, and tyrphostin 1288 (1 to 100 microM), enhanced the basal release of MMP-2 but did not affect the thrombin-induced secretion of MMP-2. Genistein 57-66 matrix metallopeptidase 2 Rattus norvegicus 137-142 10544927-5 1999 The inhibitors of protein tyrosine kinase, herbymicin A, genistein, and tyrphostin 1288 (1 to 100 microM), enhanced the basal release of MMP-2 but did not affect the thrombin-induced secretion of MMP-2. tyrphostin 1288 72-87 matrix metallopeptidase 2 Rattus norvegicus 137-142 10544927-6 1999 The inhibitor of phosphotyrosine phosphatases, vanadate (100 microM), selectively inhibited the thrombin-induced, but not the basal, release of MMP-2. Vanadates 47-55 matrix metallopeptidase 2 Rattus norvegicus 144-149 10615432-7 1999 RESULTS: Epithelioid SMC, but not swirling SMC, secreted MMP-2 in response to uPA and tPA. Tetradecanoylphorbol Acetate 86-89 matrix metallopeptidase 2 Rattus norvegicus 57-62 10340932-13 1999 Rat alveolar macrophages were found to produce a low constitutive level of MMP-2 (72-kD gelatinase A) that was only modestly upregulated following stimulation with phorbol myristate acetate, bacterial lipopolysaccharide, or immunoglobulin A-containing immune complexes. Tetradecanoylphorbol Acetate 164-189 matrix metallopeptidase 2 Rattus norvegicus 75-80 10347097-5 1999 Normal porcine PAs in attached collagen gels were characterized by increasing activity of MMP-2 and MMP-9 assessed by zymography and TN deposition detected by Western immunoblotting and densitometric analysis of immunoreactivity. Protactinium 15-18 matrix metallopeptidase 2 Rattus norvegicus 90-95 10383745-12 1999 Glycyl-L-histidyl-L-lysine-Cu(II) injections increased pro-matrix metalloproteinase-2 and activated matrix metalloproteinase-2 during the later stages of healing (days 18 and/or 22). glycyl-l-histidyl-l-lysine-cu(ii) 0-33 matrix metallopeptidase 2 Rattus norvegicus 59-85 10383745-12 1999 Glycyl-L-histidyl-L-lysine-Cu(II) injections increased pro-matrix metalloproteinase-2 and activated matrix metalloproteinase-2 during the later stages of healing (days 18 and/or 22). glycyl-l-histidyl-l-lysine-cu(ii) 0-33 matrix metallopeptidase 2 Rattus norvegicus 100-126 10347097-6 1999 PAs on floating collagen showed reduced activity of both MMPs and deposition of TN. Protactinium 0-3 matrix metallopeptidase 2 Rattus norvegicus 57-61 10233857-7 1999 Furthermore, cleaved Ln-5, as well as MMP2, became detectable in remodeling glands from sexually immature rats treated with sex steroids. Steroids 128-136 matrix metallopeptidase 2 Rattus norvegicus 38-42 9916016-3 1999 The present study shows that endometrial mRNA levels for TIMPs 1, 2, and 3 were increased while gelatinase A levels remained unchanged and gelatinase B levels decreased during oil-induced decidualization. Oils 176-179 matrix metallopeptidase 2 Rattus norvegicus 96-108 9916016-6 1999 PGE2 decreased mRNA levels for TIMP-1 and gelatinase A but had no effect on gelatinase B or TIMPs 2 and 3. Dinoprostone 0-4 matrix metallopeptidase 2 Rattus norvegicus 42-54 9071708-1 1997 The synthetic inhibitor of matrix metalloproteinases (MMP) Ro 31-9790, a hydroxamic-acid derivative, was investigated for its effect on rat mesangial cells (MC) in culture. Hydroxamic Acids 73-88 matrix metallopeptidase 2 Rattus norvegicus 54-57 10503958-0 1999 Long-term alcohol consumption increases matrix metalloproteinase-2 activity in rat aorta. Alcohols 10-17 matrix metallopeptidase 2 Rattus norvegicus 40-66 10503958-3 1999 We studied the effect of chronic alcohol consumption on upregulation of the enzymatic activity of matrix metalloproteinase-2 (MMP-2) as a possible pathway for large vessel remodeling. Alcohols 33-40 matrix metallopeptidase 2 Rattus norvegicus 98-124 10503958-3 1999 We studied the effect of chronic alcohol consumption on upregulation of the enzymatic activity of matrix metalloproteinase-2 (MMP-2) as a possible pathway for large vessel remodeling. Alcohols 33-40 matrix metallopeptidase 2 Rattus norvegicus 126-131 10503958-7 1999 Aortic extracts from rats on long-term (72 weeks), but not the short-term (2 and 4 weeks), alcohol diets showed increased MMP-2 activity. Alcohols 91-98 matrix metallopeptidase 2 Rattus norvegicus 122-127 10503958-9 1999 These observations demonstrate that long-term alcohol consumption up-regulates MMP-2 activity, which is coincident with the alteration of aortic ECM composition through the degradation of vascular elastin components. Alcohols 46-53 matrix metallopeptidase 2 Rattus norvegicus 79-84 9756602-11 1998 There was a correlation between the levels of gelatinase A at 3 hours and the sucrose uptake (P<0.05). Sucrose 78-85 matrix metallopeptidase 2 Rattus norvegicus 46-58 9574526-4 1998 We report that rat A-NK cells produce two matrix metalloproteinases: MMP-2 and MMP-9, as determined by SDS-PAGE gelatin zymography. Sodium Dodecyl Sulfate 103-106 matrix metallopeptidase 2 Rattus norvegicus 69-74 9278454-9 1997 Bromodeoxyuridine-substituted UV cross-linking of the 40-bp enhancer element with MC nuclear extracts yielded a single protein of 52 kDa, while Southwestern blot analysis with MMP-2 RE1 demonstrated three hybridizing nuclear proteins of 52, 62, and 86 kDa size. Bromodeoxyuridine 0-17 matrix metallopeptidase 2 Rattus norvegicus 176-181 25989721-8 1997 Sodium dodecyl sulfate (SDS)-activated MMP-2 showed specific cleavage patterns on collagen types I and III but not on fibronectin, collagen type IV, or laminin. Sodium Dodecyl Sulfate 0-22 matrix metallopeptidase 2 Rattus norvegicus 39-44 25989721-8 1997 Sodium dodecyl sulfate (SDS)-activated MMP-2 showed specific cleavage patterns on collagen types I and III but not on fibronectin, collagen type IV, or laminin. Sodium Dodecyl Sulfate 24-27 matrix metallopeptidase 2 Rattus norvegicus 39-44 25989721-9 1997 The reaction of SDS-activated MMP-2 produced a 140-kDa fragment from collagen types I and III. Sodium Dodecyl Sulfate 16-19 matrix metallopeptidase 2 Rattus norvegicus 30-35 9166291-5 1997 After 1 month of aldosterone-salt treatment, proMMP-2, MMP-2, and proMMP-1 collagenolytic activities and their gene expression were unchanged compared with sham-operated rats. Aldosterone 17-28 matrix metallopeptidase 2 Rattus norvegicus 48-53 9175058-16 1997 CONCLUSIONS: These data suggest that the beneficial effects of enalapril and FR139317 may be related to modulation of glomerular mRNA expression of ECM components and ET-1 and that these agents may follow a different mechanism in regulating the glomerular mRNA expression for MMP-2 and TIMP-1 in PAN nephrosis. Enalapril 63-72 matrix metallopeptidase 2 Rattus norvegicus 276-281 9175058-16 1997 CONCLUSIONS: These data suggest that the beneficial effects of enalapril and FR139317 may be related to modulation of glomerular mRNA expression of ECM components and ET-1 and that these agents may follow a different mechanism in regulating the glomerular mRNA expression for MMP-2 and TIMP-1 in PAN nephrosis. FR 139317 77-85 matrix metallopeptidase 2 Rattus norvegicus 276-281 11820951-8 1999 The mRNA of MMP-1, MMP-2 were expressed at lower levels in the normal lung tissue and there was an increase in first week, and fourth week group of bleomycin rats with a peak in one week group. Bleomycin 148-157 matrix metallopeptidase 2 Rattus norvegicus 19-24 9884073-15 1998 The L-NAME treatment of hyperoxic animals reduced lung oedema and epithelial proliferation, but enhanced the activities of MMPs. NG-Nitroarginine Methyl Ester 4-10 matrix metallopeptidase 2 Rattus norvegicus 123-127 9824449-3 1998 The objective of this study was to determine whether MMPs are expressed in various regional areas of rat brain after administration of the neurotoxin, kainic acid. Kainic Acid 151-162 matrix metallopeptidase 2 Rattus norvegicus 53-57 9824449-14 1998 GFAP levels were induced 3 days after kainic acid injection in brain regions where MMP-2 was elevated. Kainic Acid 38-49 matrix metallopeptidase 2 Rattus norvegicus 83-88 9824449-17 1998 These data demonstrate that MMP-9 and MMP-2 are differentially expressed with respect to time after kainic acid injection, and suggest that they are regulated by convulsion and/or neurodegenerative-associated mechanisms, respectively. Kainic Acid 100-111 matrix metallopeptidase 2 Rattus norvegicus 38-43 9824449-18 1998 Although similar in catalytic activity, MMP-9 and MMP-2 may play different roles in response to kainic acid-induced seizure and neuronal degeneration. Kainic Acid 96-107 matrix metallopeptidase 2 Rattus norvegicus 50-55 9771487-7 1998 Zymograms demonstrated the highest level of gelatinase A (MMP-2) activity in BAL fluid in the first 2 weeks after bleomycin. Bleomycin 114-123 matrix metallopeptidase 2 Rattus norvegicus 44-56 9771487-7 1998 Zymograms demonstrated the highest level of gelatinase A (MMP-2) activity in BAL fluid in the first 2 weeks after bleomycin. Bleomycin 114-123 matrix metallopeptidase 2 Rattus norvegicus 58-63 9759374-5 1998 After 24 or 48 h of culture in medium supplemented with HGF, transforming growth factor-alpha (TGF-alpha) or sodium butyrate, MMP production by DHD/K12 cells was stimulated by HGF and TGF-alpha and inhibited by sodium butyrate. Butyric Acid 109-124 matrix metallopeptidase 2 Rattus norvegicus 126-129 9759374-5 1998 After 24 or 48 h of culture in medium supplemented with HGF, transforming growth factor-alpha (TGF-alpha) or sodium butyrate, MMP production by DHD/K12 cells was stimulated by HGF and TGF-alpha and inhibited by sodium butyrate. Butyric Acid 211-226 matrix metallopeptidase 2 Rattus norvegicus 126-129 9175201-3 1997 Therefore, the aim of this study was to examine the role of collagenase and gelatinases A and B in the development and healing of acetic acid-induced gastric ulcer in rats. Acetic Acid 130-141 matrix metallopeptidase 2 Rattus norvegicus 76-95 9083277-0 1997 Prostaglandin E2 stimulates expression of matrix metalloproteinase 2 in cultured rat mesangial cells. Dinoprostone 0-16 matrix metallopeptidase 2 Rattus norvegicus 42-68 9083277-6 1997 PGE2 increased MMP-2 mRNA levels beginning at one hour of incubation and remained elevated up to 24 hours. Dinoprostone 0-4 matrix metallopeptidase 2 Rattus norvegicus 15-20 9083277-7 1997 Nuclear run off experiments revealed that the PGE2-induced increase in mRNA expression for MMP-2 is due to stimulated gene transcription. Dinoprostone 46-50 matrix metallopeptidase 2 Rattus norvegicus 91-96 9083277-8 1997 Western blot analysis and zymography revealed that MMP-2 protein production and enzyme activity was also enhanced by PGE2. Dinoprostone 117-121 matrix metallopeptidase 2 Rattus norvegicus 51-56 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Cyclic AMP 4-8 matrix metallopeptidase 2 Rattus norvegicus 41-46 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Cyclic AMP 4-8 matrix metallopeptidase 2 Rattus norvegicus 138-143 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. 8-Bromo Cyclic Adenosine Monophosphate 18-30 matrix metallopeptidase 2 Rattus norvegicus 41-46 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. 8-Bromo Cyclic Adenosine Monophosphate 18-30 matrix metallopeptidase 2 Rattus norvegicus 138-143 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Dinoprostone 76-80 matrix metallopeptidase 2 Rattus norvegicus 41-46 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Dinoprostone 76-80 matrix metallopeptidase 2 Rattus norvegicus 138-143 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Cyclic AMP 26-30 matrix metallopeptidase 2 Rattus norvegicus 41-46 9083277-9 1997 The cAMP analogue 8-bromo-cAMP increased MMP-2 mRNA levels, suggesting that PGE2-induced generation of intracellular cAMP plays a role in MMP-2 induction in MC. Cyclic AMP 26-30 matrix metallopeptidase 2 Rattus norvegicus 138-143 9083277-10 1997 These studies demonstrate that PGE2 stimulates the transcription, protein formation and enzyme activity of MMP-2 in cultured rat MC. Dinoprostone 31-35 matrix metallopeptidase 2 Rattus norvegicus 107-112 9124530-8 1997 The elution profile of this activity from gelatin-Sepharose 4B was similar to matrix metalloproteinase 2 (MMP-2, a 72-kDa matrixin with a 62-kDa mature form), and the dimethyl sulfoxide eluant from these columns contained MMP-2 immunoreactivity. Sepharose 50-59 matrix metallopeptidase 2 Rattus norvegicus 222-227 9071708-3 1997 Ro 31-9790 inhibited activity of the rat MC MMP-2 in a concentration-dependent and competitive fashion, as analyzed by quantitative densitometry and by a continuously recording fluorescent assay. Ro 31-9790 0-10 matrix metallopeptidase 2 Rattus norvegicus 44-49 9068947-8 1997 The matrix metalloproteinases at 90/92 kDa (gelatinase B) and 66/63/57 kDa (gelatinase A) were significantly decreased in the corneas of the vitamin A deficient rats relative to the control corneas. Vitamin A 141-150 matrix metallopeptidase 2 Rattus norvegicus 76-88 9116149-4 1997 In contrast to controls, PA and gelatinase A activities were maintained through puberty (42 days) in PTU-treated rats but declined by 90 days. Propylthiouracil 101-104 matrix metallopeptidase 2 Rattus norvegicus 32-44 8770948-6 1996 On all substrates PTE produced the MMPS, gelatinase-A and -B and collagenase with an apparent increase in gelatinase-A and -B production when cultured on LN. pte 18-21 matrix metallopeptidase 2 Rattus norvegicus 35-39 8735589-15 1996 It resembles cytochalasin D in selectively inducing an activated form of gelatinase A in peritubular cells. Cytochalasin D 13-27 matrix metallopeptidase 2 Rattus norvegicus 73-85 8636146-4 1996 The processing proteinase activity secreted by cultured fibrogenic cells resists inhibitors of serine or aspartyl proteinases as well as tissue inhibitor of matrix metalloproteinases-2 (MMP-2) but is completely inhibited by metal ion chelators. Metals 164-169 matrix metallopeptidase 2 Rattus norvegicus 186-191 8611170-2 1996 Rat kidney mesangial cells secrete predominantly latent gelatinase A that can be activated following treatment with cytochalasin D. Cytochalasin D 116-130 matrix metallopeptidase 2 Rattus norvegicus 56-68 8907376-9 1996 In experiment II, intrastromal epithelial migration was delayed by topical application of beta-mercaptomethyl tripeptide, a synthetic inhibitor of MMPs (p < 0.05). beta-mercaptomethyl tripeptide 90-120 matrix metallopeptidase 2 Rattus norvegicus 147-151 8770948-6 1996 On all substrates PTE produced the MMPS, gelatinase-A and -B and collagenase with an apparent increase in gelatinase-A and -B production when cultured on LN. pte 18-21 matrix metallopeptidase 2 Rattus norvegicus 41-76 8770948-6 1996 On all substrates PTE produced the MMPS, gelatinase-A and -B and collagenase with an apparent increase in gelatinase-A and -B production when cultured on LN. pte 18-21 matrix metallopeptidase 2 Rattus norvegicus 41-60 32795487-4 2020 The protein levels of Wnt/beta-catenin signaling components including MMP-2, beta-catenin, Wnt3a, Wnt10b, Cyclin D1, and WISP1 were increased in PQ-treated rat lung tissues. Paraquat 145-147 matrix metallopeptidase 2 Rattus norvegicus 70-75 7606893-7 1995 Cyclic AMP elevation, which profoundly influences cell differentiation, increased the invasion potential of rat Schwann cells and caused a corresponding increase in secretion of MMP-2. Cyclic AMP 0-10 matrix metallopeptidase 2 Rattus norvegicus 178-183 7606893-8 1995 Schwann cells immortalized by protracted elevation of cAMP, as well as a schwannoma cell line (D6P2T), also rapidly invaded a reconstituted basement membrane and over-expressed MMP-2. Cyclic AMP 54-58 matrix metallopeptidase 2 Rattus norvegicus 177-182 7916617-11 1993 Steady-state levels of the 3.1 kb transcript of the 72 kDa type IV collagenase were low or undetectable in resting MC, but were greatly stimulated following incubation with IL-beta, TNF-alpha or phorbol ester. Phorbol Esters 195-208 matrix metallopeptidase 2 Rattus norvegicus 52-78 7916617-13 1993 Synthesis by MC of the 72 kDa type IV collagenase was also induced by second-messenger analogues, including 8-bromo-cyclic AMP and forskolin. 8-Bromo Cyclic Adenosine Monophosphate 108-126 matrix metallopeptidase 2 Rattus norvegicus 23-49 7916617-13 1993 Synthesis by MC of the 72 kDa type IV collagenase was also induced by second-messenger analogues, including 8-bromo-cyclic AMP and forskolin. Colforsin 131-140 matrix metallopeptidase 2 Rattus norvegicus 23-49 33588051-7 2021 Additionally, the downregulation of p-GSK3beta(Ser9) and SIRT1, upregulation of NF-kappaB(p-65), MMP-2 and MMP-9 in AAA were abolished by LiCl treatment. Lithium Chloride 138-142 matrix metallopeptidase 2 Rattus norvegicus 97-102 33588051-11 2021 This study provided the first evidence that LiCl prevented the development of AAA through inhibiting inflammation, MMPs, and superoxide production, and facilitating the biosynthesis of elastin. Lithium Chloride 44-48 matrix metallopeptidase 2 Rattus norvegicus 115-119 34823880-6 2022 The released Sc3+ shows statistically significant inhibition of S. mutans biofilm (1.2 log10 CFU reduction at 6 h) and matrix metalloproteinase-2 (MMP-2) activity, compared with Sc-free glass and positive control. sc3+ 13-17 matrix metallopeptidase 2 Rattus norvegicus 119-145 34823880-6 2022 The released Sc3+ shows statistically significant inhibition of S. mutans biofilm (1.2 log10 CFU reduction at 6 h) and matrix metalloproteinase-2 (MMP-2) activity, compared with Sc-free glass and positive control. sc3+ 13-17 matrix metallopeptidase 2 Rattus norvegicus 147-152 34961861-11 2021 Furthermore, after myocardial infarction, the administration of propofol significantly improved the diastolic strain rate, down-regulated the mRNA expression levels of myocardial hypertrophy markers, atrial natriuretic peptide and beta-myosin heavy chain, and reversed the up-regulation of matrix metalloproteinase 2 (MMP2), MMP9 and tissue inhibitor of metalloproteinase-2 (TIMP-2) induced by myocardial infarction. Propofol 64-72 matrix metallopeptidase 2 Rattus norvegicus 290-316 34718940-5 2022 METHODS AND RESULTS: In this context, we created a full-thickness excisional wound model in Wistar albino rats and, investigated NF-kappaB p65 DNA-binding activity and expression levels of RELA (p65), MMP2 and MMP9 in wound samples taken on days 0, 3, 7, and 14 from diabetic/non-diabetic rats treated with metformin and saline. Metformin 307-316 matrix metallopeptidase 2 Rattus norvegicus 201-205 34718940-6 2022 As a result of our study, we showed that topically applied metformin accelerates wound healing by suppressing NF-kappaB p65 activity and diminishing the expression of MMP2 and MMP9. Metformin 59-68 matrix metallopeptidase 2 Rattus norvegicus 167-171 34961861-11 2021 Furthermore, after myocardial infarction, the administration of propofol significantly improved the diastolic strain rate, down-regulated the mRNA expression levels of myocardial hypertrophy markers, atrial natriuretic peptide and beta-myosin heavy chain, and reversed the up-regulation of matrix metalloproteinase 2 (MMP2), MMP9 and tissue inhibitor of metalloproteinase-2 (TIMP-2) induced by myocardial infarction. Propofol 64-72 matrix metallopeptidase 2 Rattus norvegicus 318-322 34795593-13 2021 Pterostilbene significantly (p < 0.001) down-regulated the level of metalloproteinases (MMP) such as MMP-2 and MMP-9. pterostilbene 0-13 matrix metallopeptidase 2 Rattus norvegicus 88-91 34959676-0 2021 Matrix Metalloproteinase-2 Inhibition in Acute Ischemia-Reperfusion Heart Injury-Cardioprotective Properties of Carvedilol. Carvedilol 112-122 matrix metallopeptidase 2 Rattus norvegicus 0-26 34959676-9 2021 MMP-2 activity in the coronary effluent increased in the IR injury group and this was prevented by carvedilol. Carvedilol 99-109 matrix metallopeptidase 2 Rattus norvegicus 0-5 34959676-11 2021 Conclusions: These data suggest that the cardioprotective effect of carvedilol in myocardial IR injury may be mediated by inhibiting MMP-2 activation. Carvedilol 68-78 matrix metallopeptidase 2 Rattus norvegicus 133-138 34755764-0 2021 Effect of silibinin on the expression of MMP2, MMP3, MMP9 and TIMP2 in kidney and lung after hepatic ischemia/reperfusion injury in an experimental rat model. Silybin 10-19 matrix metallopeptidase 2 Rattus norvegicus 41-45 34755764-5 2021 Comparison of the control vs. silibinin groups showed a statistically significant decrease in the expression levels of MMP2, MMP3, and MMP9 and increase of TIMP2 in kidney and lung parenchyma. Silybin 30-39 matrix metallopeptidase 2 Rattus norvegicus 119-123 33620008-7 2021 Quantitative real time PCR revealed that MMP2 and MMP9 levels were significantly suppressed in response to LAA spanlastics treated rats by 30.4% and 65.3%, respectively, when compared to the control group after exposure to UV irradiation. Ascorbic Acid 107-110 matrix metallopeptidase 2 Rattus norvegicus 41-45 34792728-8 2022 The levels of 8-OHdG, MMP2, and MMP9, which increased with Cd administration, were observed to reduce after treatment with CRV. Cadmium 59-61 matrix metallopeptidase 2 Rattus norvegicus 22-26 34795593-13 2021 Pterostilbene significantly (p < 0.001) down-regulated the level of metalloproteinases (MMP) such as MMP-2 and MMP-9. pterostilbene 0-13 matrix metallopeptidase 2 Rattus norvegicus 101-106 34500301-8 2021 RESULTS: Myricetin dose-dependently inhibited the migration and proliferation in VSMCs, suppressed the expression of CDK4, cyclin D3, MMP2, and MMP9. myricetin 9-18 matrix metallopeptidase 2 Rattus norvegicus 134-138 34510666-3 2021 This study aimed to evaluate the changes in serum and liver tissue levels of VEGF, TGF-beta and MMP-2 in melatonin treated septic rats. Melatonin 105-114 matrix metallopeptidase 2 Rattus norvegicus 96-101 34600915-5 2021 Gelatin zymography and Western blots revealed decreases in MMP-2 and MMP-9 and increases in MMP-1 and MMP-7 in aorta, uterus and placenta of Preg+TNFalpha and RUPP, that were reversed in RUPP+Etanercept rats. rupp 159-163 matrix metallopeptidase 2 Rattus norvegicus 59-64 34600915-5 2021 Gelatin zymography and Western blots revealed decreases in MMP-2 and MMP-9 and increases in MMP-1 and MMP-7 in aorta, uterus and placenta of Preg+TNFalpha and RUPP, that were reversed in RUPP+Etanercept rats. rupp 187-191 matrix metallopeptidase 2 Rattus norvegicus 59-64 34790780-9 2021 Conclusions: In the animal model of BAPN-induced AAD, collagen types I, III and subunits were increased, while MMP2 and MMP9 were decreased in thoracic aorta, which may lead to stiffness of the aorta and be the cause of dissection. Aminopropionitrile 36-40 matrix metallopeptidase 2 Rattus norvegicus 111-115 34717626-6 2021 Treatment with BI113823 reduced TNF-alpha and IL-1beta, and macrophages recruitment in bronchoalveolar lavage, reduced CD-68 positive macrophages and expression of proliferating cell nuclear antigen (PCNA) in the perivascular areas, and reduced expression of iNOS, B1 receptors, matrix metalloproteinase (MMP)-2 and MMP-9 proteins, and the phosphorylation of ERK1/2 and AKT in lung. bi113823 15-23 matrix metallopeptidase 2 Rattus norvegicus 279-311 34706009-9 2021 Methylprednisolone acetate attenuated matrix metalloproteinase-2 activity, cardiac dilatation, and prevented the onset of pulmonary congestion, as well as avoided cardiac hypertrophy. Methylprednisolone Acetate 0-26 matrix metallopeptidase 2 Rattus norvegicus 38-64 34754156-13 2021 Furthermore, in immunohistochemical evaluations, MMP1, MMP2, MMP9, and TIMP1 staining increased in the cold exposure and capsaicin group compared with the DMH group. Capsaicin 121-130 matrix metallopeptidase 2 Rattus norvegicus 55-59 34754156-13 2021 Furthermore, in immunohistochemical evaluations, MMP1, MMP2, MMP9, and TIMP1 staining increased in the cold exposure and capsaicin group compared with the DMH group. 1,2-Dimethylhydrazine 155-158 matrix metallopeptidase 2 Rattus norvegicus 55-59 34515769-5 2021 Reduced levels of respiratory tumor necrosis factor-alpha, monocyte chemotactic protein-1, matrix metalloproteinases (MMP-2 and MMP-9) were observed on treatment with synthesized Ag-AXEPS. ag-axeps 179-187 matrix metallopeptidase 2 Rattus norvegicus 118-123 34631222-5 2021 In STZ-induced DNP rats, the activity of MMP-9 was increased, while MMP-2 was decreased in the dorsal root ganglion and spinal cord. Streptozocin 3-6 matrix metallopeptidase 2 Rattus norvegicus 68-73 34435588-7 2021 Meanwhile, after mannitol treatment, energy-dependent vimentin and F-actin, ATP content, and ATP5D expression were down-regulated, while MMP2 and MMP9 expression increased in the ischemic penumbra. Mannitol 17-25 matrix metallopeptidase 2 Rattus norvegicus 137-141 34697745-5 2021 Tubotaiwine treatment significantly suppressed Cd-induced increase in MMP-2 and MMP-9 in rat aortic artery tissues. Cadmium 47-49 matrix metallopeptidase 2 Rattus norvegicus 70-75 34685839-6 2021 DAE or PUE treatment decreased OA-induced overexpression of MMP-2, MMP-9, and MMP-13 in the knee joint tissue. o,p-dinitrophenyl aminoethyldiphosphate-beryllium trifluoride 0-3 matrix metallopeptidase 2 Rattus norvegicus 60-65 34565677-10 2022 Icariin treatment reduced MMP-2 and -9 activities and increased deposition of well-organized collagen. icariin 0-7 matrix metallopeptidase 2 Rattus norvegicus 26-38 34077763-7 2021 The sequences of changes in MMP2 spots from sham control animals suggested that the mild BOP exposure differences normalized within 72 hours. bop 89-92 matrix metallopeptidase 2 Rattus norvegicus 28-32 34287088-12 2021 Depletion of miR-511-3p showed a protective effect against MCT-induced HSOS, as evidenced by decreased HSOS pathogenesis factors, MMP-2, MMP-9, TNF-alpha and IL-1beta, and decreased LSEC apoptosis rates. mir-511-3p 13-23 matrix metallopeptidase 2 Rattus norvegicus 130-135 34357552-12 2021 RT-qPCR analysis has represented upregulation and downregulation of miR-149-5p and MMP-2,9, respectively, after miR-mimic and CoQ10 treatment. coenzyme Q10 126-131 matrix metallopeptidase 2 Rattus norvegicus 83-90 34357552-14 2021 Taking together miR-149 and CoQ10 has shown to have an impressive potential to prevent damage to dopaminergic neurons caused by 6-OHDA injection through reducing MMP-2,9, increased TH expression, and improved motor function. coenzyme Q10 28-33 matrix metallopeptidase 2 Rattus norvegicus 162-169 34357552-14 2021 Taking together miR-149 and CoQ10 has shown to have an impressive potential to prevent damage to dopaminergic neurons caused by 6-OHDA injection through reducing MMP-2,9, increased TH expression, and improved motor function. Oxidopamine 128-134 matrix metallopeptidase 2 Rattus norvegicus 162-169 34573170-9 2021 A coordinated regulation of several ECM metalloproteinases (e.g., Mmp2; Mmp14), their substrates (e.g., multiple collagen genes and myelin basic protein; Mbp), and a metalloproteinase inhibitor, Reck, suggests a specific mechanism for ECM re-organization in response to chronic alcohol, which may modulate neuronal activity and result in behavioral changes, such as an escalation of alcohol drinking. Alcohols 278-285 matrix metallopeptidase 2 Rattus norvegicus 66-70 34344565-0 2021 Notoginsenoside R1 intervenes degradation and redistribution of tight junctions to ameliorate blood-brain barrier permeability by Caveolin-1/MMP2/9 pathway after acute ischemic stroke. notoginsenoside R1 0-18 matrix metallopeptidase 2 Rattus norvegicus 141-147 34198223-0 2021 Captopril inhibits Matrix Metalloproteinase-2 and extends survival as a temozolomide adjuvant in an intracranial gliosarcoma model. Captopril 0-9 matrix metallopeptidase 2 Rattus norvegicus 19-45 34147541-9 2021 Simvastatin increased levels of circulating EPCs and decreased iNOS, MMP-2, MMP-9 and VEGF mRNA levels, while increased eNOS mRNA in aneurysmal tissue. Simvastatin 0-11 matrix metallopeptidase 2 Rattus norvegicus 69-74 34434231-9 2021 More importantly, apocynin could also inhibit the MMP-2 upregulation. acetovanillone 18-26 matrix metallopeptidase 2 Rattus norvegicus 50-55 34447306-1 2021 The aim of this study was to evaluate the role of chronic cadmium exposure in modulating cardiac matrix metalloproteinases (MMPs) in the heart of rats. Cadmium 58-65 matrix metallopeptidase 2 Rattus norvegicus 124-128 34447306-6 2021 This study provides evidence of cadmium-induced imbalance in the MMP-TIMP system in the cardiac tissue. Cadmium 32-39 matrix metallopeptidase 2 Rattus norvegicus 65-68 34198223-2 2021 Captopril"s known anti-cancer effects include inhibition of Matrix Metalloproteinase-2 (MMP-2), an endopeptidase which selectively breaks down the extracellular matrix to promote cell migration. Captopril 0-9 matrix metallopeptidase 2 Rattus norvegicus 60-86 34198223-2 2021 Captopril"s known anti-cancer effects include inhibition of Matrix Metalloproteinase-2 (MMP-2), an endopeptidase which selectively breaks down the extracellular matrix to promote cell migration. Captopril 0-9 matrix metallopeptidase 2 Rattus norvegicus 88-93 34198223-4 2021 Using an aggressive gliosarcoma model, we assessed captopril"s effects on MMP-2 expression in vitro and in vivo as well as its efficacy as an adjuvant in combination therapy regimens in vivo. Captopril 51-60 matrix metallopeptidase 2 Rattus norvegicus 74-79 34198223-8 2021 RESULTS: In vitro, captopril decreased MMP-2 protein expression and reduced migratory capacity in 9 L gliosarcoma cells. Captopril 19-28 matrix metallopeptidase 2 Rattus norvegicus 39-44 34198223-9 2021 In a gliosarcoma animal model, captopril decreased MMP-2 protein expression and extended survival as a TMZ adjuvant relative to untreated controls, captopril monotherapy, and TMZ monotherapy groups (27.5 versus 14 (p < 0.001), 16 (p < 0.001), and 23 (p = 0.018) days, respectively). Captopril 31-40 matrix metallopeptidase 2 Rattus norvegicus 51-56 34198223-10 2021 CONCLUSIONS: Captopril decreases gliosarcoma cell migration, which may be mediated by reduction in MMP-2 protein expression. Captopril 13-22 matrix metallopeptidase 2 Rattus norvegicus 99-104 34198223-12 2021 Captopril may represent a promising potential adjuvant to TMZ therapy in gliosarcoma as a modulator of the MMP-2 pathway. Captopril 0-9 matrix metallopeptidase 2 Rattus norvegicus 107-112 34202757-1 2021 The aim of this study was to investigate the effect of the application of homocysteine as well as its effect under the condition of aerobic physical activity on the activities of matrix metalloproteinases (MMP), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) in cardiac tissue and on hepato-renal biochemical parameters in sera of rats. Homocysteine 74-86 matrix metallopeptidase 2 Rattus norvegicus 206-209 34366855-8 2021 Reynoutrin is a potential natural drug for the treatment of IHF, and its mechanism of action involves the up-regulation of S100A1 expression, thereby inhibiting expressions of MMPs and the transcriptional activity of nuclear factor kappa-B. reynoutrin 0-10 matrix metallopeptidase 2 Rattus norvegicus 176-180 34430566-10 2021 In parallel, there were 17beta-estradiol effects in reducing MMP2 (P=0.0043), MMP9 (P=0.011), and IL-6 (P=0.024). Estradiol 24-40 matrix metallopeptidase 2 Rattus norvegicus 61-65 34202757-8 2021 Physical activity leads to activation of MMP-2 isoform and to increased activity of MMP-9 isoform in both homocysteine-treated and control rats. Homocysteine 106-118 matrix metallopeptidase 2 Rattus norvegicus 41-46 34250770-9 2021 Exposure to single and continuous administration of Cd caused a significant increase in MMP2 expression by 10.14-fold (P=0.016) and 27.61-fold (P(0.001), respectively. Cadmium 52-54 matrix metallopeptidase 2 Rattus norvegicus 88-92 34090401-9 2021 In the diabetic rat Achilles tendon, NOX1 protein expression and mRNA expression of NOX1, IL-6, MMP-2, TIMP-2, and type III collagen were significantly lower while type I collagen expression was significantly higher in the DHEA group than in the control group. Dehydroepiandrosterone 223-227 matrix metallopeptidase 2 Rattus norvegicus 96-101 34239443-4 2021 We found that knockdown of c-Jun N-terminal kinase (JNK) or p38 mitogen-activated protein kinase (MAPK), or treatment with ivabradine, reduced JNK and p38 MAPK phosphorylation and the protein expression of proliferating cell nuclear antigen, collagen I, collagen III, tissue inhibitor of matrix metalloproteinase 2, and alpha-smooth muscle actin, accompanied with upregulation of matrix metalloproteinase 2 both in high glucose-treated neonatal rat CFs and left ventricular CFs isolated from db/db mice. Glucose 420-427 matrix metallopeptidase 2 Rattus norvegicus 380-406 34250770-11 2021 NAC treatments decreased the expression of MMP2 and MMP9 in rats exposed to single or continuous Cd. Acetylcysteine 0-3 matrix metallopeptidase 2 Rattus norvegicus 43-47 34250770-11 2021 NAC treatments decreased the expression of MMP2 and MMP9 in rats exposed to single or continuous Cd. Cadmium 97-99 matrix metallopeptidase 2 Rattus norvegicus 43-47 34250770-12 2021 Cd exposure was strongly associated with Zn and Cu depletion, and overexpression of MMP2 and MMP9. Cadmium 0-2 matrix metallopeptidase 2 Rattus norvegicus 84-88 35143864-7 2022 RESULTS: MEHP exposure significantly induced oxidative damage in BRL-3A cells, which inhibited the expression of STAT5A and promoted the expression of fibrosis related proteins MMP2, MMP9, TIMP2 and CTGF. mono-(2-ethylhexyl)phthalate 9-13 matrix metallopeptidase 2 Rattus norvegicus 177-181 35608392-6 2022 Furthermore, gene expression results revealed that geraniol treatment inhibited the mitogen-activated protein kinase (MAPK) proteins, inflammatory responder (tumor necrosis factor-alpha, interleukin 6, nuclear factor-kappaB), and cardiac fibrotic proteins (matrix metalloproteinase-2(MMP-2), MMP-9) in ISO directed rats. geraniol 51-59 matrix metallopeptidase 2 Rattus norvegicus 257-283 35608392-6 2022 Furthermore, gene expression results revealed that geraniol treatment inhibited the mitogen-activated protein kinase (MAPK) proteins, inflammatory responder (tumor necrosis factor-alpha, interleukin 6, nuclear factor-kappaB), and cardiac fibrotic proteins (matrix metalloproteinase-2(MMP-2), MMP-9) in ISO directed rats. geraniol 51-59 matrix metallopeptidase 2 Rattus norvegicus 284-289 35504018-7 2022 We found that three formulations of the PA nanofibers were able to localize to AAA tissue, but the MMP-2 targeting PA substantially outperformed the other nanofibers. Protactinium 115-117 matrix metallopeptidase 2 Rattus norvegicus 99-104 35504018-8 2022 Additionally, we demonstrated that the MMP-2 targeting PA nanofibers had an optimal dose of 5 mg (~12 mg/kg). Protactinium 55-57 matrix metallopeptidase 2 Rattus norvegicus 39-44 34063987-10 2021 In H9c2 cardiac cells, empagliflozin decreased the MMP2,9 activity and prevented apoptosis. empagliflozin 23-36 matrix metallopeptidase 2 Rattus norvegicus 51-55 35143864-8 2022 After over-expression of STAT5A gene in BRL-3A cells, the elevated expression levels of CTGF, MMP2, MMP9 and TIMP2 induced by MEHP exposure were significantly reversed. mono-(2-ethylhexyl)phthalate 126-130 matrix metallopeptidase 2 Rattus norvegicus 94-98 35631351-7 2022 Although not significantly, MMP-2 activity decreased in the cortex of OCA-treated I/R rats. obeticholic acid 70-73 matrix metallopeptidase 2 Rattus norvegicus 28-33 35420738-0 2022 Diverse Impact of N-Acetylcysteine or Alpha-Lipoic Acid Supplementation during High-Fat Diet Regime on Matrix Metalloproteinase-2 and Matrix Metalloproteinase-9 in Visceral and Subcutaneous Adipose Tissue. Acetylcysteine 18-34 matrix metallopeptidase 2 Rattus norvegicus 103-129 35436360-8 2022 Additionally, the data also showed that intraperitoneal injection of melatonin in advance inhibited aldosterone-induced macrophage/microglia infiltration, and remarkably diminished the levels of inflammatory cytokines (IL-6, IL-1beta, and COX-2), chemokines (CCL-3, and CXCL-1), and matrix metalloproteinases (MMP-2, and MMP-9). Melatonin 69-78 matrix metallopeptidase 2 Rattus norvegicus 310-315 35420738-0 2022 Diverse Impact of N-Acetylcysteine or Alpha-Lipoic Acid Supplementation during High-Fat Diet Regime on Matrix Metalloproteinase-2 and Matrix Metalloproteinase-9 in Visceral and Subcutaneous Adipose Tissue. Thioctic Acid 38-55 matrix metallopeptidase 2 Rattus norvegicus 103-129 35420738-6 2022 Real-time PCR and western blot approaches were used to check whether NAC or ALA impacts MMP2/9 expression. Acetylcysteine 69-72 matrix metallopeptidase 2 Rattus norvegicus 88-94 35420738-6 2022 Real-time PCR and western blot approaches were used to check whether NAC or ALA impacts MMP2/9 expression. Thioctic Acid 76-79 matrix metallopeptidase 2 Rattus norvegicus 88-94 35420738-8 2022 Moreover, NAC and ALA have a divergent impact on MMP2 and MMP9 expression in different adipose tissue localization. Acetylcysteine 10-13 matrix metallopeptidase 2 Rattus norvegicus 49-53 35420738-8 2022 Moreover, NAC and ALA have a divergent impact on MMP2 and MMP9 expression in different adipose tissue localization. Thioctic Acid 18-21 matrix metallopeptidase 2 Rattus norvegicus 49-53 35420738-9 2022 CONCLUSION: Based on our results, we speculate that NAC and ALA have a prominent effect on the MMP2/9 functions under obesity conditions. Acetylcysteine 52-55 matrix metallopeptidase 2 Rattus norvegicus 95-101 35420738-9 2022 CONCLUSION: Based on our results, we speculate that NAC and ALA have a prominent effect on the MMP2/9 functions under obesity conditions. Thioctic Acid 60-63 matrix metallopeptidase 2 Rattus norvegicus 95-101 35167880-0 2022 Hyperbaric oxygen therapy mitigates left ventricular remodeling, upregulates MMP-2 and VEGF, and inhibits the induction of MMP-9, TGF-beta1, and TNF-alpha in streptozotocin-induced diabetic rat heart. Oxygen 11-17 matrix metallopeptidase 2 Rattus norvegicus 77-82 35313329-8 2022 Gene expression profile of quercetin treated rats revealed down regulation of HGF, TIMP1 and MMP2 expressed during CCl4 induction. Quercetin 27-36 matrix metallopeptidase 2 Rattus norvegicus 93-97 35347819-6 2022 DOX-induced fibrosis involves activation of transforming growth factor-beta1 (TGF-beta1), matrix metalloproteinase 2 (MMP-2), and MMP-9 with concomitant downregulation of tissue inhibitors of MMPs (TIMP)-1 and TIMP-2 expressions in H9c2 cardiomyoblasts. Doxorubicin 0-3 matrix metallopeptidase 2 Rattus norvegicus 90-116 35347819-6 2022 DOX-induced fibrosis involves activation of transforming growth factor-beta1 (TGF-beta1), matrix metalloproteinase 2 (MMP-2), and MMP-9 with concomitant downregulation of tissue inhibitors of MMPs (TIMP)-1 and TIMP-2 expressions in H9c2 cardiomyoblasts. Doxorubicin 0-3 matrix metallopeptidase 2 Rattus norvegicus 118-123 35064410-10 2022 Serum TNF-alpha, IL1-beta, MMP-1 and MMP-2 activities and tissue casp-3 and casp-9 activities significantly increased but the bcl-2/bax ratio significantly decreased in the MTX group compared those of the control group. Methotrexate 173-176 matrix metallopeptidase 2 Rattus norvegicus 37-42 35150824-0 2022 Omeprazole prevents stress induced gastric ulcer by direct inhibition of MMP-2/TIMP-3 interactions. Omeprazole 0-10 matrix metallopeptidase 2 Rattus norvegicus 73-78 35150824-7 2022 In contrast, omeprazole treatment suppressed TIMP-3 while increasing MMP-2 activity and thereby, restoring MMP-2/TIMP-3 balance. Omeprazole 13-23 matrix metallopeptidase 2 Rattus norvegicus 69-74 35150824-7 2022 In contrast, omeprazole treatment suppressed TIMP-3 while increasing MMP-2 activity and thereby, restoring MMP-2/TIMP-3 balance. Omeprazole 13-23 matrix metallopeptidase 2 Rattus norvegicus 107-112 35150824-8 2022 Additionally, nanomolar binding constant (Kd = 318 nM) of omeprazole with purified MMP-2 indicates a direct effect of omeprazole in restoring MMP-2 activity. Omeprazole 58-68 matrix metallopeptidase 2 Rattus norvegicus 83-88 35150824-8 2022 Additionally, nanomolar binding constant (Kd = 318 nM) of omeprazole with purified MMP-2 indicates a direct effect of omeprazole in restoring MMP-2 activity. Omeprazole 58-68 matrix metallopeptidase 2 Rattus norvegicus 142-147 35150824-8 2022 Additionally, nanomolar binding constant (Kd = 318 nM) of omeprazole with purified MMP-2 indicates a direct effect of omeprazole in restoring MMP-2 activity. Omeprazole 118-128 matrix metallopeptidase 2 Rattus norvegicus 83-88 35150824-8 2022 Additionally, nanomolar binding constant (Kd = 318 nM) of omeprazole with purified MMP-2 indicates a direct effect of omeprazole in restoring MMP-2 activity. Omeprazole 118-128 matrix metallopeptidase 2 Rattus norvegicus 142-147 35150824-10 2022 Altogether, omeprazole restores MMP-2 activity and reduces apoptosis while preventing acute stress-induced gastric ulcer that occurs via suppression of nuclear factor kappa B (NF-kappaB) activity and peroxisome proliferator-activated receptor gamma activity (PPAR-gamma). Omeprazole 12-22 matrix metallopeptidase 2 Rattus norvegicus 32-37 35282381-14 2022 The expression and activity of matrix metalloproteinase 2 (MMP2) and MMP9 in the PPE + CaCl2 group, PPE group, and PPE + BNPA group were significantly higher than those in the control group (P < 0.05). Calcium Chloride 87-92 matrix metallopeptidase 2 Rattus norvegicus 31-57 35282381-14 2022 The expression and activity of matrix metalloproteinase 2 (MMP2) and MMP9 in the PPE + CaCl2 group, PPE group, and PPE + BNPA group were significantly higher than those in the control group (P < 0.05). Calcium Chloride 87-92 matrix metallopeptidase 2 Rattus norvegicus 59-63 35282381-14 2022 The expression and activity of matrix metalloproteinase 2 (MMP2) and MMP9 in the PPE + CaCl2 group, PPE group, and PPE + BNPA group were significantly higher than those in the control group (P < 0.05). bnpa 121-125 matrix metallopeptidase 2 Rattus norvegicus 31-57 35183192-3 2022 Ultrasmall copper oxide (CuO) NPs are conjugated with type 2 collagen and MSC dual-targeting peptide (designated WPV) with a matrix metalloproteinase 2 (MMP-2)-sensitive sequence as a spacer to achieve hierarchical targeting. cupric oxide 11-23 matrix metallopeptidase 2 Rattus norvegicus 125-151 35183192-3 2022 Ultrasmall copper oxide (CuO) NPs are conjugated with type 2 collagen and MSC dual-targeting peptide (designated WPV) with a matrix metalloproteinase 2 (MMP-2)-sensitive sequence as a spacer to achieve hierarchical targeting. cupric oxide 11-23 matrix metallopeptidase 2 Rattus norvegicus 153-158 35155962-9 2022 The experiment validated quercetin might suppress chondrocyte apoptosis mediated by IL-1beta and reduce SELE, MMP2, and COL1 expression. Quercetin 25-34 matrix metallopeptidase 2 Rattus norvegicus 110-114 35155962-10 2022 Via the AGE-RAGE signaling pathway in diabetic complications, quercetin could aim at SELE, MMP2, and COL1 and exert antagonistic effects against OA. Quercetin 62-71 matrix metallopeptidase 2 Rattus norvegicus 91-95 35282267-12 2022 Gossypin significantly (P < 0.001) suppressed the MMP-2 and MMP-9 in ISO-induced I/R rats. gossypin 0-8 matrix metallopeptidase 2 Rattus norvegicus 50-55 34636119-9 2022 The pharmacology network results showed that Sal B and its metabolites could regulate ALB, PLG, ACE, CASP3, MMP9, MMP2, MTOR, etc. salvianolic acid B 45-50 matrix metallopeptidase 2 Rattus norvegicus 114-118