PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34518608-9 2021 Ketamine treatment in depressive-like mice significantly increased the expression levels of p-ERK1/2 and GLUT3 in the prefrontal cortex (P < 0.01), whereas an ERK1/2 inhibitor significantly inhibited ketamine-induced increases (P < 0.01).Our present findings demonstrate that ketamine mitigated depressive-like behaviors in female mice by activating the ERK/GLUT3 signal pathway, which further increased glucose uptake in the prefrontal cortex. Glucose 404-411 mitogen-activated protein kinase 3 Mus musculus 94-100 34865281-0 2022 CDK5 inhibition improves glucose uptake in insulin resistant neuronal cells via ERK1/2 pathway. Glucose 25-32 mitogen-activated protein kinase 3 Mus musculus 80-86 34518608-7 2021 An ERK1/2 inhibitor significantly inhibited ketamine-induced increases in the glucose uptake in depressive-like mice (P < 0.05), as well as prolonged the immobility time (P < 0.01). Glucose 78-85 mitogen-activated protein kinase 3 Mus musculus 3-9 34518608-9 2021 Ketamine treatment in depressive-like mice significantly increased the expression levels of p-ERK1/2 and GLUT3 in the prefrontal cortex (P < 0.01), whereas an ERK1/2 inhibitor significantly inhibited ketamine-induced increases (P < 0.01).Our present findings demonstrate that ketamine mitigated depressive-like behaviors in female mice by activating the ERK/GLUT3 signal pathway, which further increased glucose uptake in the prefrontal cortex. Glucose 404-411 mitogen-activated protein kinase 3 Mus musculus 159-165 34179020-9 2021 The Arnt Delta EC, ERT2 mutation also reduced measures of cell viability, while increasing the production of reactive oxygen species (ROS) in microvascular endothelial cells (MVECs) isolated from mouse skeletal muscle, and the viability of Arnt Delta EC, ERT2 MVECs under high-glucose concentrations increased when the cells were treated with an ROS inhibitor. Glucose 277-284 mitogen-activated protein kinase 3 Mus musculus 19-23 34053181-6 2021 As ERK1/2 has been implicated in the regulation of glucose transport and metabolism this increase could potentially underlie MT protective effect in MT-TG/Akt2-KO mice. Glucose 51-58 mitogen-activated protein kinase 3 Mus musculus 3-9 34859931-7 2022 In addition, high glucose (HG) increased VSMC apoptosis, up-regulated IGF-1-IGF-1R and HB-EGF-EGFR, and stimulated ERK1/2 and PI3K-Akt pathways. Glucose 18-25 mitogen-activated protein kinase 3 Mus musculus 115-121 35513431-3 2022 In combination with high glucose, FGF21 induces cardiac myocyte growth in width mediated by extracellular signal-regulated kinase 1/2 (ERK1/2) signaling. Glucose 25-32 mitogen-activated protein kinase 3 Mus musculus 135-141 35281932-15 2022 Dapagliflozin alleviated HRMECs apoptosis induced by high glucose through ERK/1/2/cPLA2/AA/ROS pathway. Glucose 58-65 mitogen-activated protein kinase 3 Mus musculus 74-81 35173145-9 2022 In cultured GEnCs, high glucose dramatically upregulated the expressions of HPSE and p-ERK1/2, both of which were markedly blocked by HPSE siRNA. Glucose 24-31 mitogen-activated protein kinase 3 Mus musculus 87-93 31365278-5 2019 ERK1/2 inhibitor U0126 abrogated NF-kappaB activation in d-glucose-treated BV2 cells. Glucose 57-66 mitogen-activated protein kinase 3 Mus musculus 0-6 32945406-7 2020 The results revealed that glucose activated ERK1/2 phosphorylation, but inhibited JNK and p38 phosphorylation in a concentration-dependent manner. Glucose 26-33 mitogen-activated protein kinase 3 Mus musculus 44-50 32512010-0 2020 High glucose-induced ROS accumulation is a critical regulator of ERK1/2-Akt-tuberin-mTOR signalling in RGC-5 cells. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 65-71 31899483-13 2020 Mechanistically, Renalase attenuated high glucose-induced profibrotic gene expression and p21 activity through inhibiting extracellular regulated protein kinases (ERK1/2). Glucose 42-49 mitogen-activated protein kinase 3 Mus musculus 163-169 30597356-7 2019 ERK1/2 inhibitor U0126 reduced ROS formation, the activation of NFkappaB and Egr1, and the elevated TNFalpha expression in D-glucose-stimulated BV2 cells. Glucose 123-132 mitogen-activated protein kinase 3 Mus musculus 0-6 31755338-3 2019 Glucose enhances cell apoptosis mediated through PI3K/Akt, ERK1/2, and Bax/Bcl-2 pathways. Glucose 0-7 mitogen-activated protein kinase 3 Mus musculus 59-65 31040360-7 2019 In vitro, insulin inhibited high glucose-stimulation of Bmf expression, predominantly via p44/42 mitogen-activated protein kinase (MAPK) signaling. Glucose 33-40 mitogen-activated protein kinase 3 Mus musculus 90-93 29018002-10 2018 These results indicate that glucose uptake by GLUT1 is required for RANKL and osteocalcin expressions in osteocytes, and that inhibition of glucose uptake decreases their expressions through AMPK, ERK1/2, and p38 MAPK pathways. Glucose 140-147 mitogen-activated protein kinase 3 Mus musculus 197-203 30352794-6 2018 Glucose-responsive ERK1/2 and S6 phosphorylation were also disrupted by chronic CMA2 treatment. Glucose 0-7 mitogen-activated protein kinase 3 Mus musculus 19-25 28190775-5 2017 Inducible deletion of DRP1 of mature POMC neurons (Drp1fl/fl-POMC-cre:ERT2) resulted in improved leptin sensitivity and glucose responsiveness. Glucose 120-127 mitogen-activated protein kinase 3 Mus musculus 70-74 28721437-8 2017 RESULTS: Glucose induced rapid subplasmalemmal recruitment of ERK1 and ERK2. Glucose 9-16 mitogen-activated protein kinase 3 Mus musculus 62-66 28721437-10 2017 By contrast, ERK1 was required for glucose-induced full activation of several targets involved in beta cell survival; MSK1 and CREB were less active in Erk1 -/- mouse beta cells (p < 0.01) compared with Erk1 +/+ mouse beta cells, and their phosphorylation could only be restored when ERK1 was re-expressed and not when ERK2 was overexpressed. Glucose 35-42 mitogen-activated protein kinase 3 Mus musculus 13-17 28721437-10 2017 By contrast, ERK1 was required for glucose-induced full activation of several targets involved in beta cell survival; MSK1 and CREB were less active in Erk1 -/- mouse beta cells (p < 0.01) compared with Erk1 +/+ mouse beta cells, and their phosphorylation could only be restored when ERK1 was re-expressed and not when ERK2 was overexpressed. Glucose 35-42 mitogen-activated protein kinase 3 Mus musculus 152-156 28721437-10 2017 By contrast, ERK1 was required for glucose-induced full activation of several targets involved in beta cell survival; MSK1 and CREB were less active in Erk1 -/- mouse beta cells (p < 0.01) compared with Erk1 +/+ mouse beta cells, and their phosphorylation could only be restored when ERK1 was re-expressed and not when ERK2 was overexpressed. Glucose 35-42 mitogen-activated protein kinase 3 Mus musculus 206-210 28721437-10 2017 By contrast, ERK1 was required for glucose-induced full activation of several targets involved in beta cell survival; MSK1 and CREB were less active in Erk1 -/- mouse beta cells (p < 0.01) compared with Erk1 +/+ mouse beta cells, and their phosphorylation could only be restored when ERK1 was re-expressed and not when ERK2 was overexpressed. Glucose 35-42 mitogen-activated protein kinase 3 Mus musculus 287-291 28721437-0 2017 ERK1 is dispensable for mouse pancreatic beta cell function but is necessary for glucose-induced full activation of MSK1 and CREB. Glucose 81-88 mitogen-activated protein kinase 3 Mus musculus 0-4 28947919-5 2017 The insulin levels (151.08+-14.34 microIU/ml) and ERK1/2 phosphorylation in beta-TC-6 cells peaked in response to 1.38 mM glucose stimulation compared with 0, 5.5 and 11.1 mM glucose stimulation. Glucose 122-129 mitogen-activated protein kinase 3 Mus musculus 50-56 28947919-5 2017 The insulin levels (151.08+-14.34 microIU/ml) and ERK1/2 phosphorylation in beta-TC-6 cells peaked in response to 1.38 mM glucose stimulation compared with 0, 5.5 and 11.1 mM glucose stimulation. Glucose 175-182 mitogen-activated protein kinase 3 Mus musculus 50-56 28433068-0 2017 The role of interleukin-1beta and extracellular signal-regulated kinase 1/2 in glucose-stimulated insulin secretion. Glucose 79-86 mitogen-activated protein kinase 3 Mus musculus 34-75 28433068-8 2017 Compared with the 0mM glucose group, the level of ERK1/2 phosphorylation was increased in the 1.38mM and 5.5mM glucose groups. Glucose 22-29 mitogen-activated protein kinase 3 Mus musculus 50-56 28433068-8 2017 Compared with the 0mM glucose group, the level of ERK1/2 phosphorylation was increased in the 1.38mM and 5.5mM glucose groups. Glucose 111-118 mitogen-activated protein kinase 3 Mus musculus 50-56 28433068-9 2017 After intervention by 0.15 ng/mL, 1.5 ng/mL, and 15 ng/mL IL-1beta, the level of ERK1/2 phosphorylation induced by 1.38mM glucose stimulation decreased in a dose-dependent manner, and the insulin level correspondingly decreased. Glucose 122-129 mitogen-activated protein kinase 3 Mus musculus 81-87 27488452-10 2016 ROS-activated ERK1/2 signaling is involved in high glucose-induced NRK cell activation. Glucose 51-58 mitogen-activated protein kinase 3 Mus musculus 14-20 27975141-0 2017 Glucose and angiotensin II-derived endothelial extracellular vesicles regulate endothelial dysfunction via ERK1/2 activation. Glucose 0-7 mitogen-activated protein kinase 3 Mus musculus 107-113 27975141-7 2017 Furthermore, high glucose + Ang II-derived EEVs induced ERK1/2 signalling and decreased endothelial NO synthase (eNOS) protein expression in mice aortas. Glucose 18-25 mitogen-activated protein kinase 3 Mus musculus 56-62 27975141-8 2017 Furthermore, in the presence of the MEK/ERK1/2 inhibitor PD98059, high glucose plus Ang II treatment stimulated EEVs in HUVECs and those EEVs prevented the impairments of ACh-induced relaxation and NO production in mice aortas. Glucose 71-78 mitogen-activated protein kinase 3 Mus musculus 40-46 27975141-9 2017 These data strongly indicate that high glucose and Ang II directly affect endothelial cells and the production of EEVs; the resultant EEVs aggravate endothelial dysfunction by regulating eNOS protein levels and ERK1/2 signalling in mice aortas. Glucose 39-46 mitogen-activated protein kinase 3 Mus musculus 211-217 27488452-3 2016 ROS-mediated ERK1/2 activation was found to play a crucial role in high glucose-induced fibroblast proliferation and activation. Glucose 72-79 mitogen-activated protein kinase 3 Mus musculus 13-19 24885625-0 2014 High glucose increases LPS-induced DC apoptosis through modulation of ERK1/2, AKT and Bax/Bcl-2. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 70-76 27498780-5 2016 RESULTS: Glucose (1-40 mmol/L) and Ang II (10-8-10-5 mol/L) dose-dependently increased the expression of fibronectin, collagens, phospho-ERK1/2 and phospho-NF-kappaB-p65 in cardiac fibroblasts. Glucose 9-16 mitogen-activated protein kinase 3 Mus musculus 137-143 27498780-7 2016 ERK1/2 inhibitor U0126 (10 mumol/L) and NF-kappaB inhibitor JSH-23 (10 mumol/L) both markedly suppressed glucose- and angiotensin II-induced fibronectin and collagen expressions in cardiac fibroblasts. Glucose 105-112 mitogen-activated protein kinase 3 Mus musculus 0-6 27095850-9 2016 We found that glucose- and H2O2-induced activation of FAK, paxillin, ERK1/2 and Akt was significantly blocked by silencing SCGN. Glucose 14-21 mitogen-activated protein kinase 3 Mus musculus 69-75 27035884-1 2016 The present study aimed to investigate the role of the extracellular signal-regulated kinase (ERK)1/2 signal transduction pathway in glucose-stimulated insulin secretion in beta-TC6 mouse pancreatic cells. Glucose 133-140 mitogen-activated protein kinase 3 Mus musculus 55-101 27035884-3 2016 Furthermore, glucose stimulation enhanced the phosphorylation of ERK1/2, which was dose-dependently inhibited by PD98059, as indicated by western blot analysis. Glucose 13-20 mitogen-activated protein kinase 3 Mus musculus 65-71 27035884-4 2016 These results indicated that the activation of the ERK1/2 signal transduction pathway may have an important role in glucose-stimulated insulin secretion in beta-TC6 cells. Glucose 116-123 mitogen-activated protein kinase 3 Mus musculus 51-57 23379999-14 2013 The exposure of RGC-5 cells to high glucose activated ERK1/2 and JNK MAPK signaling blocking by GPR91 shRNA (P < 0.01). Glucose 36-43 mitogen-activated protein kinase 3 Mus musculus 54-60 25133193-3 2014 TGF-beta1 and collagen type IV regulated by high glucose through ERK1/2 MAPK were downregulated by silencing TRB3 in renal mesangial cells. Glucose 49-56 mitogen-activated protein kinase 3 Mus musculus 65-71 23942551-6 2013 High glucose stimulated Src, TACE, epidermal growth factor receptor (EGFR), mitogen-activated protein kinases (MAPKs), extracellular signal-regulated kinase (ERK1/2, p38), and collagen IV accumulation in mesangial cells. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 158-164 23766264-7 2013 In vitro, the inhibitors of PKCbeta and extracellular signal-regulated kinase 1/2, as well as small interfering RNA to Egr-1, significantly decreased high-glucose-induced expression of CD11c (integrin, alpha X 9 complement component 3 receptor 4 subunit]), chemokine (C-C motif) ligand 2, and interleukin-1beta in U937 macrophages. Glucose 155-162 mitogen-activated protein kinase 3 Mus musculus 40-81 23428406-0 2013 Diastereomeric mixture of calophyllic acid and isocalophyllic acid stimulates glucose uptake in skeletal muscle cells: involvement of PI-3-kinase- and ERK1/2-dependent pathways. Glucose 78-85 mitogen-activated protein kinase 3 Mus musculus 151-157 23428406-5 2013 F015 significantly increased the phosphorylation of AKT, AS160 and ERK1/2, account for the augmented glucose transport capacity in L6 myotubes. Glucose 101-108 mitogen-activated protein kinase 3 Mus musculus 67-73 23344729-8 2013 Following pharmacological activation of ERK1/2 all agonists caused a significant increase in insulin release from islets incubated with sub-stimulatory levels of glucose. Glucose 162-169 mitogen-activated protein kinase 3 Mus musculus 40-46 23344729-9 2013 ERK1/2 inhibition significantly reduced the glucose-dependent decreases in filamentous actin observed in primary beta cells, while pharmacological dissociation of actin filaments enabled all receptor-operated secretagogues tested to significantly stimulate insulin release from islets at a sub-stimulatory glucose concentration. Glucose 44-51 mitogen-activated protein kinase 3 Mus musculus 0-6 23344729-10 2013 CONCLUSIONS/INTERPRETATION: Glucose-induced ERK1/2 activation in beta cells mediates the permissive effects of stimulatory glucose concentrations on receptor-operated insulin secretagogues, at least in part through effects on actin depolymerisation and cytoskeletal remodelling. Glucose 28-35 mitogen-activated protein kinase 3 Mus musculus 44-50 23344729-10 2013 CONCLUSIONS/INTERPRETATION: Glucose-induced ERK1/2 activation in beta cells mediates the permissive effects of stimulatory glucose concentrations on receptor-operated insulin secretagogues, at least in part through effects on actin depolymerisation and cytoskeletal remodelling. Glucose 123-130 mitogen-activated protein kinase 3 Mus musculus 44-50 23379999-15 2013 These results indicate that GPR91 modulates the high glucose-induced VEGF release of RGC-5 cells, possibly by inhibiting ERK1/2 and JNK MAPK signaling. Glucose 53-60 mitogen-activated protein kinase 3 Mus musculus 121-127 21099329-8 2010 Glucose stimulation of isolated Pim3-/- islets resulted in increased phosphorylation of ERK1/2, a kinase involved in regulating beta-cell response to glucose. Glucose 0-7 mitogen-activated protein kinase 3 Mus musculus 88-94 20953578-7 2011 Hyperinsulinaemic-euglycaemic clamp studies demonstrated an increase in whole-body insulin sensitivity in the ob/ob-Erk1-(/)- mice associated with an increase in both insulin-stimulated glucose disposal in skeletal muscles and adipose tissue insulin sensitivity. Glucose 186-193 mitogen-activated protein kinase 3 Mus musculus 116-120 20953578-11 2011 CONCLUSIONS/INTERPRETATION: Our results demonstrate that the targeting of ERK1 could partially protect obese mice against insulin resistance and liver steatosis by decreasing adipose tissue inflammation and by increasing muscle glucose uptake. Glucose 228-235 mitogen-activated protein kinase 3 Mus musculus 74-78 21099329-10 2010 Overexpression of SOCS6 inhibited glucose-induced ERK1/2 activation, strongly suggesting that Pim3 regulates ERK1/2 activity through SOCS6. Glucose 34-41 mitogen-activated protein kinase 3 Mus musculus 109-115 21099329-11 2010 These data reveal that Pim3 is a novel glucose-responsive gene in the beta cell that negatively regulates insulin secretion by inhibiting the activation of ERK1/2, and through its effect on insulin sensitivity, has potentially a more global function in glucose homeostasis. Glucose 39-46 mitogen-activated protein kinase 3 Mus musculus 156-162 22800886-12 2012 When cells were stimulated with glucose, increased phosphorylation of extracellular signal-regulated kinase (ERK) 1/2 and serine-threonine kinase (Akt) were observed in MIN6-LRP16. Glucose 32-39 mitogen-activated protein kinase 3 Mus musculus 70-117 22139838-6 2012 In addition, blockade of the interaction between beta1 integrins and the extracellular matrix with an anti-beta1 integrin antibody (Ha2/5) inhibited short term glucose-induced phosphorylation of FAK (Tyr-397), paxillin (Tyr-118), and ERK1/2 (Thr-202/Tyr-204). Glucose 160-167 mitogen-activated protein kinase 3 Mus musculus 234-240 22139838-9 2012 In conclusion, these results indicate 1) that glucose-induced activation of FAK, paxillin, and ERK1/2 is mediated by beta1 integrin intracellular signaling, 2) a mechanism whereby FAK mediates glucose-induced actin cytoskeleton remodeling, hence allowing docking and fusion of insulin granules to the plasma membrane, and 3) a possible functional role for the Akt/AS160 signaling pathway in the FAK-mediated regulation of glucose-stimulated insulin secretion. Glucose 46-53 mitogen-activated protein kinase 3 Mus musculus 95-101 22139838-9 2012 In conclusion, these results indicate 1) that glucose-induced activation of FAK, paxillin, and ERK1/2 is mediated by beta1 integrin intracellular signaling, 2) a mechanism whereby FAK mediates glucose-induced actin cytoskeleton remodeling, hence allowing docking and fusion of insulin granules to the plasma membrane, and 3) a possible functional role for the Akt/AS160 signaling pathway in the FAK-mediated regulation of glucose-stimulated insulin secretion. Glucose 193-200 mitogen-activated protein kinase 3 Mus musculus 95-101 22139838-9 2012 In conclusion, these results indicate 1) that glucose-induced activation of FAK, paxillin, and ERK1/2 is mediated by beta1 integrin intracellular signaling, 2) a mechanism whereby FAK mediates glucose-induced actin cytoskeleton remodeling, hence allowing docking and fusion of insulin granules to the plasma membrane, and 3) a possible functional role for the Akt/AS160 signaling pathway in the FAK-mediated regulation of glucose-stimulated insulin secretion. Glucose 193-200 mitogen-activated protein kinase 3 Mus musculus 95-101 21099329-8 2010 Glucose stimulation of isolated Pim3-/- islets resulted in increased phosphorylation of ERK1/2, a kinase involved in regulating beta-cell response to glucose. Glucose 150-157 mitogen-activated protein kinase 3 Mus musculus 88-94 21099329-10 2010 Overexpression of SOCS6 inhibited glucose-induced ERK1/2 activation, strongly suggesting that Pim3 regulates ERK1/2 activity through SOCS6. Glucose 34-41 mitogen-activated protein kinase 3 Mus musculus 50-56 19500499-9 2009 CONCLUSION: Losartan can inhibit high glucose-induced CTGF expression in mouse mesangial cells, and the mechanisms maybe involve the interruption of ERK1/2 MAPK pathway. Glucose 38-45 mitogen-activated protein kinase 3 Mus musculus 149-155 19502418-7 2009 RESULTS: Exposure of MIN6 cells and islets to elevated glucose induced ERK1/2 and PKB phosphorylation, which was further enhanced by palmitate. Glucose 55-62 mitogen-activated protein kinase 3 Mus musculus 71-77 19500499-0 2009 [Losartan inhibits high glucose-induced CTGF expression via ERK1/2 MAPK pathways in mouse mesangial cells]. Glucose 24-31 mitogen-activated protein kinase 3 Mus musculus 60-66 19500499-6 2009 RESULTS: High glucose induced the phosphorylation of ERK1/2 in a time-dependent manner. Glucose 14-21 mitogen-activated protein kinase 3 Mus musculus 53-59 19500499-7 2009 The protein expression of phosphor-ERK1/2 and CTGF were increased in high glucose group comparing with low glucose group(P<0.01), and reduced in losartan group and ERK inhibitors group comparing with high glucose group(P<0.05). Glucose 74-81 mitogen-activated protein kinase 3 Mus musculus 35-41 17962352-7 2008 Further studies showed that glucose induced CREB phosphorylation through Ca(2+)-PKA-ERK1/2 and Ca(2+)-PKC pathways. Glucose 28-35 mitogen-activated protein kinase 3 Mus musculus 84-90 19500499-7 2009 The protein expression of phosphor-ERK1/2 and CTGF were increased in high glucose group comparing with low glucose group(P<0.01), and reduced in losartan group and ERK inhibitors group comparing with high glucose group(P<0.05). Glucose 107-114 mitogen-activated protein kinase 3 Mus musculus 35-41 19500499-7 2009 The protein expression of phosphor-ERK1/2 and CTGF were increased in high glucose group comparing with low glucose group(P<0.01), and reduced in losartan group and ERK inhibitors group comparing with high glucose group(P<0.05). Glucose 107-114 mitogen-activated protein kinase 3 Mus musculus 35-41 19091959-0 2009 Sphingosine-1-phosphate inhibits high glucose-mediated ERK1/2 action in endothelium through induction of MAP kinase phosphatase-3. Glucose 38-45 mitogen-activated protein kinase 3 Mus musculus 55-61 19091959-11 2009 Overexpression of MKP-3 in glucose-cultured HAEC decreased ERK1/2 phosphorylation and resulted in decreased monocyte:endothelial interactions in a static monocyte adhesion assay. Glucose 27-34 mitogen-activated protein kinase 3 Mus musculus 59-65 18456735-0 2008 Microvessel vascular smooth muscle cells contribute to collagen type I deposition through ERK1/2 MAP kinase, alphavbeta3-integrin, and TGF-beta1 in response to ANG II and high glucose. Glucose 176-183 mitogen-activated protein kinase 3 Mus musculus 90-96 17962352-8 2008 Thus, the Ca(2+)-PKA-ERK1/2-CREB and Ca(2+)-PKC-CREB signaling pathways are involved in glucose-induced PANDER gene expression. Glucose 88-95 mitogen-activated protein kinase 3 Mus musculus 21-27 16873684-0 2006 ERK1/2 control phosphorylation and protein level of cAMP-responsive element-binding protein: a key role in glucose-mediated pancreatic beta-cell survival. Glucose 107-114 mitogen-activated protein kinase 3 Mus musculus 0-6 16985513-10 2006 High glucose-induced Pax-2 gene expression is mediated, at least in part, via ROS generation and activation of the nuclear factor kappa B signaling pathway, but not via protein kinase C, p38 mitogen-activated protein kinase (MAPK), and p44/42 MAPK signaling. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 236-239 16985513-10 2006 High glucose-induced Pax-2 gene expression is mediated, at least in part, via ROS generation and activation of the nuclear factor kappa B signaling pathway, but not via protein kinase C, p38 mitogen-activated protein kinase (MAPK), and p44/42 MAPK signaling. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 243-247 17440593-8 2007 High glucose medium induced phosphorylation of ERK1/2 as early as 30 minutes, reached the peak at hour 6; maintained the activation from hour 12 to 24, and declined to the basal level at hour 48. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 47-53 17440593-10 2007 Blockade of activation of ERK1/2 with PD98059, a specific ERK1/2 activation inhibitor, attenuated the high glucose-induced expression of podocalyxin protein on the 6th day. Glucose 107-114 mitogen-activated protein kinase 3 Mus musculus 26-32 17440593-10 2007 Blockade of activation of ERK1/2 with PD98059, a specific ERK1/2 activation inhibitor, attenuated the high glucose-induced expression of podocalyxin protein on the 6th day. Glucose 107-114 mitogen-activated protein kinase 3 Mus musculus 58-64 17440593-11 2007 CONCLUSION: High ambient glucose decreases the protein level of podocalyxin by podocyte in vitro and in vivo, and the decrease in podocalyxin protein is ERK1/2jdependent in cultured podocytes. Glucose 25-32 mitogen-activated protein kinase 3 Mus musculus 153-159 17198096-0 2007 Activations of nPKCepsilon and ERK1/2 were involved in oxygen-glucose deprivation-induced neuroprotection via NMDA receptors in hippocampal slices of mice. Glucose 62-69 mitogen-activated protein kinase 3 Mus musculus 31-37 16873684-3 2006 We observed that 10 mmol/l glucose-induced CREB phosphorylation was totally inhibited by the protein kinase A (PKA) inhibitor H89 (2 micromol/l) and reduced by 50% with the extracellular signal-regulated kinase (ERK)1/2 inhibitor PD98059 (20 micromol/l). Glucose 27-34 mitogen-activated protein kinase 3 Mus musculus 173-219 16873684-4 2006 This indicates that ERK1/2, reported to be located downstream of PKA, participates in the PKA-mediated CREB phosphorylation elicited by glucose. Glucose 136-143 mitogen-activated protein kinase 3 Mus musculus 20-26 16873684-5 2006 In ERK1/2-downregulated MIN6 cells by siRNA, glucose-stimulated CREB phosphorylation was highly reduced and CREB protein content was decreased by 60%. Glucose 45-52 mitogen-activated protein kinase 3 Mus musculus 3-9 16873684-6 2006 In MIN6 cells and islets cultured for 24-48 h in optimal glucose concentration (10 mmol/l), which promotes survival, blockade of ERK1/2 activity with PD98059 caused a significant decrease in CREB protein level, whereas CREB mRNA remained unaffected (measured by real-time quantitative PCR). Glucose 57-64 mitogen-activated protein kinase 3 Mus musculus 129-135 16873684-8 2006 Our results indicate that ERK1 and -2 control the phosphorylation and protein level of CREB and play a key role in glucose-mediated pancreatic beta-cell survival. Glucose 115-122 mitogen-activated protein kinase 3 Mus musculus 26-37 15498890-3 2005 We observed that the majority of ERK1/2 activity induced by glucose remains in the cytoplasm and physically interacts with synapsin I, allowing phosphorylation of the substrate. Glucose 60-67 mitogen-activated protein kinase 3 Mus musculus 33-39 16778968-10 2006 CONCLUSION: Acute high glucose (2-4 days) stimulated the expression of CTGF protein via ERK1/2-dependent signaling pathway in cultured podocytes, while cultured in high glucose for 6-8 days, the podocytes did not increase its CTGF level. Glucose 23-30 mitogen-activated protein kinase 3 Mus musculus 88-94 16396989-11 2006 Interestingly, in beta-IR(-/-) beta-cells, glucose failed to stimulate phosphatidylinositol 3 kinase activity but induced p44/p42 MAPKs and mTOR/p70S(6)K phosphorylation and beta-cell mitogenesis. Glucose 43-50 mitogen-activated protein kinase 3 Mus musculus 122-125 16778968-6 2006 High glucose medium induced phosphorylation of ERK1/2 at as early as minute 30, reached the peak at hour 6; maintained the activity at hours 12 and 24, and declined to the basal level at hour 48. Glucose 5-12 mitogen-activated protein kinase 3 Mus musculus 47-53 16778968-8 2006 Blockade of phosphorylation of ERK1/2 with PD98059, a specific ERK1/2 activation inhibitor, did decrease the high glucose-triggered expression of CTGF protein in 4 days. Glucose 114-121 mitogen-activated protein kinase 3 Mus musculus 31-37 16778968-8 2006 Blockade of phosphorylation of ERK1/2 with PD98059, a specific ERK1/2 activation inhibitor, did decrease the high glucose-triggered expression of CTGF protein in 4 days. Glucose 114-121 mitogen-activated protein kinase 3 Mus musculus 63-69 16638805-5 2006 In parallel, glucose-stimulated ERK1/2 activation is greater in B1 than in C3 cells, and is potentiated in both sublines following F-actin depolymerisation. Glucose 13-20 mitogen-activated protein kinase 3 Mus musculus 32-38 16487264-15 2006 Glucose (25 mmol/L) activated p38 mitogen-activated protein kinase (MAPK) and p44/42 MAPK. Glucose 0-7 mitogen-activated protein kinase 3 Mus musculus 78-81 16061020-0 2005 [High glucose regulates the production of MMP-9 in podocyte through ERK1/2 signal pathway]. Glucose 6-13 mitogen-activated protein kinase 3 Mus musculus 68-74 16061020-14 2005 Phosphorylation of ERK1/2 occurred as early as 30 min after simulation by high glucose, reached the peak level 6 hours later, remained at this level for 24 hours, then backed to the basal level 48 hours later, whereas the activation of p38 and JNK remained undetectable. Glucose 79-86 mitogen-activated protein kinase 3 Mus musculus 19-25 15498890-5 2005 Blocking activation of ERK1/2 using MEK1/2, the MAPK kinase inhibitor PD98059 or using small interfering RNA-mediated silencing of ERK1 and ERK2 expressions resulted in partial inhibition of glucose-induced insulin release, indicating that ERK1/2 pathway participates also in the regulation of insulin secretion. Glucose 191-198 mitogen-activated protein kinase 3 Mus musculus 23-29 15498890-5 2005 Blocking activation of ERK1/2 using MEK1/2, the MAPK kinase inhibitor PD98059 or using small interfering RNA-mediated silencing of ERK1 and ERK2 expressions resulted in partial inhibition of glucose-induced insulin release, indicating that ERK1/2 pathway participates also in the regulation of insulin secretion. Glucose 191-198 mitogen-activated protein kinase 3 Mus musculus 23-27 15498890-5 2005 Blocking activation of ERK1/2 using MEK1/2, the MAPK kinase inhibitor PD98059 or using small interfering RNA-mediated silencing of ERK1 and ERK2 expressions resulted in partial inhibition of glucose-induced insulin release, indicating that ERK1/2 pathway participates also in the regulation of insulin secretion. Glucose 191-198 mitogen-activated protein kinase 3 Mus musculus 240-246 15498890-6 2005 Moreover, using the pancreatic islet perifusion model, we found that the ERK1/2 activity participates in the first and second phases of insulin release induced by glucose. Glucose 163-170 mitogen-activated protein kinase 3 Mus musculus 73-79 15498890-7 2005 Taken together, our results demonstrate new aspects of the glucose-dependent actions of ERK1/2 in beta-cells exerted on cytoplasmic proteins, including synapsin I, and participating in the overall glucose-induced insulin secretion. Glucose 59-66 mitogen-activated protein kinase 3 Mus musculus 88-94 15498890-7 2005 Taken together, our results demonstrate new aspects of the glucose-dependent actions of ERK1/2 in beta-cells exerted on cytoplasmic proteins, including synapsin I, and participating in the overall glucose-induced insulin secretion. Glucose 197-204 mitogen-activated protein kinase 3 Mus musculus 88-94 14988413-9 2004 Our results uncover a novel mechanism by which the PKA/ERK1/2 signaling network engaged by glucagon, in situation of low glucose concentration, regulates phosphorylation of CREB, a transcription factor crucial for normal beta cell function and survival. Glucose 121-128 mitogen-activated protein kinase 3 Mus musculus 55-61 15659802-6 2004 In high-glucose-treated, ERK1/2- and CREB-downregulated beta cells, there was a loss of glucose (10 mM, 5 min)-stimulated ERK1/2 and CREB phosphorylation that was associated with nuclear apoptotic characteristics. Glucose 8-15 mitogen-activated protein kinase 3 Mus musculus 122-128 15659802-6 2004 In high-glucose-treated, ERK1/2- and CREB-downregulated beta cells, there was a loss of glucose (10 mM, 5 min)-stimulated ERK1/2 and CREB phosphorylation that was associated with nuclear apoptotic characteristics. Glucose 88-95 mitogen-activated protein kinase 3 Mus musculus 25-31 15659802-6 2004 In high-glucose-treated, ERK1/2- and CREB-downregulated beta cells, there was a loss of glucose (10 mM, 5 min)-stimulated ERK1/2 and CREB phosphorylation that was associated with nuclear apoptotic characteristics. Glucose 88-95 mitogen-activated protein kinase 3 Mus musculus 122-128 14988413-1 2004 By using the MIN6 cell line and pancreatic islets, we show that in the presence of a low glucose concentration, corresponding to physiological glucagon release from alpha cells, glucagon treatment of the beta cell caused a rapid, time-dependent phosphorylation and activation of p44/p42 mitogen-activated protein kinase (ERK1/2) independently from extracellular calcium influx. Glucose 89-96 mitogen-activated protein kinase 3 Mus musculus 279-282 14988413-1 2004 By using the MIN6 cell line and pancreatic islets, we show that in the presence of a low glucose concentration, corresponding to physiological glucagon release from alpha cells, glucagon treatment of the beta cell caused a rapid, time-dependent phosphorylation and activation of p44/p42 mitogen-activated protein kinase (ERK1/2) independently from extracellular calcium influx. Glucose 89-96 mitogen-activated protein kinase 3 Mus musculus 321-327 15659802-0 2004 Cooperative effects between protein kinase A and p44/p42 mitogen-activated protein kinase to promote cAMP-responsive element binding protein activation after beta cell stimulation by glucose and its alteration due to glucotoxicity. Glucose 183-190 mitogen-activated protein kinase 3 Mus musculus 49-52 15659802-3 2004 We report that glucose (10 mM) induces an increase in cytosolic calcium concentration that leads to cAMP-induced protein kinase A (PKA) activation, promoting nuclear translocation of activated ERK1/2. Glucose 15-22 mitogen-activated protein kinase 3 Mus musculus 193-199 15659802-4 2004 The observation that glucose-induced CREB phosphorylation was totally inhibited by the PKA inhibitor H89 (2 microM) and reduced by 50% with the ERK1/2 inhibitor PD98059 (20 microM) indicates that ERK1/2, located downstream of PKA, cooperates with PKA and is responsible for half of the PKA-mediated CREB phosphorylation elicited by glucose in MIN6 beta cells. Glucose 21-28 mitogen-activated protein kinase 3 Mus musculus 144-150 15659802-4 2004 The observation that glucose-induced CREB phosphorylation was totally inhibited by the PKA inhibitor H89 (2 microM) and reduced by 50% with the ERK1/2 inhibitor PD98059 (20 microM) indicates that ERK1/2, located downstream of PKA, cooperates with PKA and is responsible for half of the PKA-mediated CREB phosphorylation elicited by glucose in MIN6 beta cells. Glucose 21-28 mitogen-activated protein kinase 3 Mus musculus 196-202 15659802-4 2004 The observation that glucose-induced CREB phosphorylation was totally inhibited by the PKA inhibitor H89 (2 microM) and reduced by 50% with the ERK1/2 inhibitor PD98059 (20 microM) indicates that ERK1/2, located downstream of PKA, cooperates with PKA and is responsible for half of the PKA-mediated CREB phosphorylation elicited by glucose in MIN6 beta cells. Glucose 332-339 mitogen-activated protein kinase 3 Mus musculus 196-202 15659802-5 2004 We also found that exposure of mu cells for 24 h to high glucose (25 mM) induced a 70% decrease in cellular ERK1/2 and a 50% decrease in CREB content. Glucose 57-64 mitogen-activated protein kinase 3 Mus musculus 108-114 15659802-6 2004 In high-glucose-treated, ERK1/2- and CREB-downregulated beta cells, there was a loss of glucose (10 mM, 5 min)-stimulated ERK1/2 and CREB phosphorylation that was associated with nuclear apoptotic characteristics. Glucose 8-15 mitogen-activated protein kinase 3 Mus musculus 25-31 10844601-2 2000 Phorbol esters increase both HK activity and glucose utilization in cultured mesangial cells via a protein kinase C (PKC)- and extracellular signal-regulated kinases 1 and 2 (ERK1/2)-dependent mechanism. Glucose 45-52 mitogen-activated protein kinase 3 Mus musculus 175-181 15121835-8 2004 We also found that basal threonine and tyrosine phosphorylation (within the TEY motif) of extracellular signal-regulated kinases 1 and 2 (ERK1/2) and the corresponding ERK1/2 activity were defective in hypoxic HIF-1 alpha-null mEFs but not in wild-type mEFs, independently of glucose uptake. Glucose 276-283 mitogen-activated protein kinase 3 Mus musculus 90-136 15121835-8 2004 We also found that basal threonine and tyrosine phosphorylation (within the TEY motif) of extracellular signal-regulated kinases 1 and 2 (ERK1/2) and the corresponding ERK1/2 activity were defective in hypoxic HIF-1 alpha-null mEFs but not in wild-type mEFs, independently of glucose uptake. Glucose 276-283 mitogen-activated protein kinase 3 Mus musculus 138-144 15121835-8 2004 We also found that basal threonine and tyrosine phosphorylation (within the TEY motif) of extracellular signal-regulated kinases 1 and 2 (ERK1/2) and the corresponding ERK1/2 activity were defective in hypoxic HIF-1 alpha-null mEFs but not in wild-type mEFs, independently of glucose uptake. Glucose 276-283 mitogen-activated protein kinase 3 Mus musculus 168-174 12856081-0 2003 Erk 1,2 phosphorylates p27(Kip1): Functional evidence for a role in high glucose-induced hypertrophy of mesangial cells. Glucose 73-80 mitogen-activated protein kinase 3 Mus musculus 0-7 12856081-5 2003 It was tested by Western blotting and autoradiography whether high glucose medium activates Erk 1,2 and whether this activation phosphorylates p27(Kip1). Glucose 67-74 mitogen-activated protein kinase 3 Mus musculus 92-99 12856081-8 2003 RESULTS: High glucose stimulates phosphorylation of MAP kinases Erk 1,2 in p27(Kip1 )+/+ and -/- mesangial cells. Glucose 14-21 mitogen-activated protein kinase 3 Mus musculus 64-71 12856081-13 2003 CONCLUSIONS/INTERPRETATION: Our study shows that high glucose stimulates Erk 1,2 that phosphorylate p27(Kip1) at serine(178) increasing its expression. Glucose 54-61 mitogen-activated protein kinase 3 Mus musculus 73-80 10229678-1 1999 Physiological concentrations of glucose that lead to Ca2+ entry and insulin secretion activate extracellular signal-regulated protein kinases (ERK1 and ERK2) in the MIN6 pancreatic beta-cell line. Glucose 32-39 mitogen-activated protein kinase 3 Mus musculus 143-147 9624138-2 1998 We report below that the response to glucose in the MIN6 cells includes an activation of the p42 and p44 mitogen-activated protein (MAP) kinases (ERK2 and ERK1). Glucose 37-44 mitogen-activated protein kinase 3 Mus musculus 155-159