PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22483459-7 2012 The increased expression of caspase-3 and number of TUNEL-positive cells in the CsA group were decreased with concomitant paricalcitol treatment. Cyclosporine 80-83 caspase 3 Rattus norvegicus 28-37 21776863-0 2011 [Apoptosis and expression of Bcl-2 and caspase-3 in ciclosporin-induced gingival overgrowth of rats]. Cyclosporine 52-63 caspase 3 Rattus norvegicus 39-48 21776863-1 2011 OBJECTIVE: To observe the effect of Ciclosporin (CsP) on apoptosis and expression of the associated protein Bcl-2, Caspase-3 in gingival epithelium of rats in order to approach the mechanism of CsP-induced gingival epithelium overgrowth. Cyclosporine 36-47 caspase 3 Rattus norvegicus 115-124 21328998-6 2010 CsA suppressed apoptosis as well as CytC release and caspase-3 activity (P < 0.01). Cyclosporine 0-3 caspase 3 Rattus norvegicus 53-62 19359911-13 2009 CsA treatment decreased the HS-induced rise in cytosolic cytochrome c levels and caspase-3 activity (p < 0.05). Cyclosporine 0-3 caspase 3 Rattus norvegicus 81-90 19359911-14 2009 CONCLUSIONS: These findings demonstrate that CsA protects mitochondrial permeability transition pores to prevent HS-induced release of cytochrome c and caspase-3 activation. Cyclosporine 45-48 caspase 3 Rattus norvegicus 152-161 17385075-4 2007 Caspase-3 activation was accompanied by CsA- and FK506-induced cell death and inhibited by NGF. Cyclosporine 40-43 caspase 3 Rattus norvegicus 0-9 17578461-8 2007 RESULTS: CsA significantly reduced infarct size (48.8 +/- 5.8% of left ventricle in vehicle + I/R group and 30.3 +/- 2.7% of left ventricle in CsA + I/R, respectively) and decreased caspase-3 activity in the myocardium [(0.62 +/- 0.17)/microg of protein and (0.42 +/- 0.15)/microg of protein, respectively] and relieved the injury of mitochondria. Cyclosporine 9-12 caspase 3 Rattus norvegicus 182-191 17578461-10 2007 The cardioprotective effects of CsA might be associated with the protection of mitochondria and the inhibition of caspase-3 activity. Cyclosporine 32-35 caspase 3 Rattus norvegicus 114-123 17490613-6 2007 Cyclosporin A, an inhibitor of the mitochondrial permeability transition (MPT), inhibited MPT opening, the release of cytochrome c and caspase-3 activation. Cyclosporine 0-13 caspase 3 Rattus norvegicus 135-144 17114439-0 2006 Cyclosporin A abolishes CD28-mediated resistance to CD95-induced apoptosis via superinduction of caspase-3. Cyclosporine 0-13 caspase 3 Rattus norvegicus 97-106 17114439-7 2006 Taken together, these findings suggest that CsA promotes sensitivity to CD95-mediated apoptosis in CD28-stimulated T cells by superinduction of the caspase-3 gene via a mechanism involving suppression of the calcineurin pathway. Cyclosporine 44-47 caspase 3 Rattus norvegicus 148-157 16625421-4 2006 Cyclosporin A (CsA), trifluoperazine and aristolochic acid, inhibitors of mitochondrial permeability transition, significantly attenuated the MPP(+)-induced mitochondrial damage leading to caspase-3 activation, increased oxidative stress and cell death. Cyclosporine 0-13 caspase 3 Rattus norvegicus 189-198 16625421-4 2006 Cyclosporin A (CsA), trifluoperazine and aristolochic acid, inhibitors of mitochondrial permeability transition, significantly attenuated the MPP(+)-induced mitochondrial damage leading to caspase-3 activation, increased oxidative stress and cell death. Cyclosporine 15-18 caspase 3 Rattus norvegicus 189-198 16980055-11 2006 CsA treatment caused proteolytic cleavage of caspase-3 and induced the degradation of 116-kDa PARP into 89-kDa fragment. Cyclosporine 0-3 caspase 3 Rattus norvegicus 45-54 16980055-13 2006 CONCLUSIONS: In this study, CsA induced apoptosis by up-regulating proapoptotic factors, caspase-3 and -6, p53, Bax, cleaving PARP, and down-regulating antiapoptotic factor, Bcl-2, and cIAP. Cyclosporine 28-31 caspase 3 Rattus norvegicus 89-105 16732183-9 2006 Active caspase-3 staining and 24-kDa active caspase-3 protein was enhanced in I/R-injured and CsA-treated kidneys, but decreased by Tac, Rap, and MMF. Cyclosporine 94-97 caspase 3 Rattus norvegicus 7-16 16732183-9 2006 Active caspase-3 staining and 24-kDa active caspase-3 protein was enhanced in I/R-injured and CsA-treated kidneys, but decreased by Tac, Rap, and MMF. Cyclosporine 94-97 caspase 3 Rattus norvegicus 44-53 16246479-6 2006 Caspase 3 activation was markedly inhibited by cyclosporin A (CsA) and Ac-DEVD-CHO. Cyclosporine 47-60 caspase 3 Rattus norvegicus 0-9 16246479-6 2006 Caspase 3 activation was markedly inhibited by cyclosporin A (CsA) and Ac-DEVD-CHO. Cyclosporine 62-65 caspase 3 Rattus norvegicus 0-9 16221205-10 2005 The 24 kD caspase-3, which proved to be an active caspase-3 subunit, was increased in I/R and CsA groups and deceased by tacrolimus, rapamycin, or MMF (P < 0.05), but not 32 kD precursor or 17 kD active caspase-3. Cyclosporine 94-97 caspase 3 Rattus norvegicus 10-19 16221205-10 2005 The 24 kD caspase-3, which proved to be an active caspase-3 subunit, was increased in I/R and CsA groups and deceased by tacrolimus, rapamycin, or MMF (P < 0.05), but not 32 kD precursor or 17 kD active caspase-3. Cyclosporine 94-97 caspase 3 Rattus norvegicus 50-59 16221205-10 2005 The 24 kD caspase-3, which proved to be an active caspase-3 subunit, was increased in I/R and CsA groups and deceased by tacrolimus, rapamycin, or MMF (P < 0.05), but not 32 kD precursor or 17 kD active caspase-3. Cyclosporine 94-97 caspase 3 Rattus norvegicus 50-59 15365088-6 2005 In accordance, cyclosporin A and the inhibitors of caspase-9 and caspase-3 inhibited cocaine-induced caspase activation and apoptosis. Cyclosporine 15-28 caspase 3 Rattus norvegicus 65-74 14599462-8 2003 Cyclosporine A and decylubiquinone, MPT specific inhibitor, prevented the activation of caspase 3, thus showing that diclofenac opened the MPT pore. Cyclosporine 0-14 caspase 3 Rattus norvegicus 88-97 14527363-8 2003 The expression of caspase-3 mRNA and caspase-3 activity was significantly higher in the CsA-treated group than that of the CsA plus tea polyphenols (TP)-treated group (P < 0.05). Cyclosporine 88-91 caspase 3 Rattus norvegicus 18-27 14527363-8 2003 The expression of caspase-3 mRNA and caspase-3 activity was significantly higher in the CsA-treated group than that of the CsA plus tea polyphenols (TP)-treated group (P < 0.05). Cyclosporine 88-91 caspase 3 Rattus norvegicus 37-46 14527363-8 2003 The expression of caspase-3 mRNA and caspase-3 activity was significantly higher in the CsA-treated group than that of the CsA plus tea polyphenols (TP)-treated group (P < 0.05). Cyclosporine 123-126 caspase 3 Rattus norvegicus 18-27 12787063-6 2003 When rats were treated with neuroprotective doses of cyclosporin A, but not with FK 506, the redistribution of apoptosis-inducing factor and cytochrome c was reduced and fodrin breakdown products and active caspase-3 immuno-reactivity was diminished whereas the extracellular calcium concentration was unaffected. Cyclosporine 53-66 caspase 3 Rattus norvegicus 207-216 12557154-10 2003 Cyclosporin A also blocked caspase-3 activation. Cyclosporine 0-13 caspase 3 Rattus norvegicus 27-36 20021159-3 2003 As previously reported, cultured rat hepatocytes exposed to CsA exhibited concentration-dependent signs of apoptotic cell injury, including chromatin condensation and fragmentation, increased caspase-3 activity, and release of cytosolic lactate dehydrogenase. Cyclosporine 60-63 caspase 3 Rattus norvegicus 192-201 12445861-10 2002 Further, the results suggest that SDZ IMM125-induced uptake of extracellular calcium is also a redox-sensitive process and that the increased intracellular calcium might directly cause apoptosis by increasing the caspase-3 activity as a central event in the cyclosporine-induced apoptotic mechanism. Cyclosporine 258-270 caspase 3 Rattus norvegicus 213-222 12411148-7 2002 The expression of caspase-3 mRNA and caspase-3 activity of CsA-treated group was significantly higher than that of CsA plus TP-treated group (P < 0.05). Cyclosporine 59-62 caspase 3 Rattus norvegicus 18-27 12411148-7 2002 The expression of caspase-3 mRNA and caspase-3 activity of CsA-treated group was significantly higher than that of CsA plus TP-treated group (P < 0.05). Cyclosporine 59-62 caspase 3 Rattus norvegicus 37-46 12411148-7 2002 The expression of caspase-3 mRNA and caspase-3 activity of CsA-treated group was significantly higher than that of CsA plus TP-treated group (P < 0.05). Cyclosporine 115-118 caspase 3 Rattus norvegicus 18-27 12029627-6 2002 There was release of mitochondrial cytochrome c into the cytosol and activation of caspase 3, which were prevented by cyclosporine, diallylsulfide, and Trolox. Cyclosporine 118-130 caspase 3 Rattus norvegicus 83-92 12066135-8 2002 The decreased expression of Bcl-2 and the ratio of Bcl-2 to Bax protein seen in cyclosporine-treated rat kidneys were significantly increased after colchicine treatment, accompanying a suppression of caspase-3 activity (P <.05). Cyclosporine 80-92 caspase 3 Rattus norvegicus 200-209 11903043-5 2002 The activation of all four caspases was inhibited by cyclosporin A, with the order of susceptibility caspase-8=caspase-9=caspase-6>caspase-3. Cyclosporine 53-66 caspase 3 Rattus norvegicus 134-143 11677240-9 2001 The PTP inhibitors cyclosporin A and bongkrekic acid prevented the H(2)O(2)-induced decrease in cell viability and caspase-3 activation. Cyclosporine 19-32 caspase 3 Rattus norvegicus 115-124 11557554-9 2001 Moreover, cyclosporin A, an inhibitor of mitochondrial permeability transition, attenuated staurosporine-induced apoptosis and necrosis through the inhibition of DeltaPsi(m) reduction, cytochrome c release, and caspase-3 activation. Cyclosporine 10-23 caspase 3 Rattus norvegicus 211-220 10702360-6 2000 After 20 h of CsA incubation apoptosis parameters were further increased and were accompanied by the increased activity of the cysteine protease, caspase-3 (CPP 32), and slightly increased caspase-6 (Mch 2), but not caspase-1 (ICE). Cyclosporine 14-17 caspase 3 Rattus norvegicus 146-155 10702360-6 2000 After 20 h of CsA incubation apoptosis parameters were further increased and were accompanied by the increased activity of the cysteine protease, caspase-3 (CPP 32), and slightly increased caspase-6 (Mch 2), but not caspase-1 (ICE). Cyclosporine 14-17 caspase 3 Rattus norvegicus 157-163 10702360-7 2000 The caspase-3 inhibitor, Ac-DEVD-CHO, inhibited caspase-3 activation and attenuated CsA-induced apoptosis and LDH leakage. Cyclosporine 84-87 caspase 3 Rattus norvegicus 4-13 9774651-6 1998 Caspase 3 activation, cytochrome c release, and apoptotic nuclear morphological changes were induced after onset of the MPT and were prevented by CsA. Cyclosporine 146-149 caspase 3 Rattus norvegicus 0-9 32569592-9 2020 In addition, exposure to CsA resulted in an increased expression of Bax, and a decreased expresion in that of Bcl-2, with a concomitant up-regulation of the Bax/Bcl-2, c-Caspase-3/p-Caspase-3 ratio and cytochrome c level. Cyclosporine 25-28 caspase 3 Rattus norvegicus 170-179 31251898-8 2019 CONCLUSIONS: Pre- and post-reperfusion CsA diminished MDA and caspase-3levels and normalized antioxidant enzymes activities. Cyclosporine 39-42 caspase 3 Rattus norvegicus 62-71 30725434-7 2019 CsA significantly decreased the Bax/Bcl-2 ratio, cl-casp-9/casp-9, and cl-casp-3/casp-3 in a concentration-dependent manner. Cyclosporine 0-3 caspase 3 Rattus norvegicus 74-80 30658157-5 2019 Celecoxib also reversed the CSA-evoked (i) reductions in the tubular and glomerular protein expression of CSE and levels of H2S, prostaglandin E2 (PGE2), and total antioxidant capacity (TAC), and (ii) increases in inflammatory (tumor necrosis factor-alpha, TNF-alpha), fibrotic (transforming growth factor-beta1, TGF-beta1) and apoptotic (caspase-3) cytokines. Cyclosporine 28-31 caspase 3 Rattus norvegicus 339-348 30403017-9 2018 In western blot, caspase-3 was significantly increased in MCT group, and was attenuated in CsA treatment. Cyclosporine 91-94 caspase 3 Rattus norvegicus 17-26 29571015-5 2018 CSA or indomethacin caused: (i) renal tubular atrophy and interstitial fibrosis, (ii) increases in serum creatinine, blood urea nitrogen (BUN), and renal LTD4, LTB4, TNF-alpha, TGF-beta1, and caspase-3, and (iii) decreases in renal PGE2 and total antioxidant capacity (TAC). Cyclosporine 0-3 caspase 3 Rattus norvegicus 192-201 29863267-11 2018 Western blotting showed that the protein expressions of Caspase 3 and Caspase 9 were remarkably elevated in cells after the use of CsA, but were significantly reduced after administration of CST (p < 0.01). Cyclosporine 131-134 caspase 3 Rattus norvegicus 56-65 29333572-12 2018 Moreover, kidney caspase-3 expression that was triggered by CSA and/or gamma radiation was decreased. Cyclosporine 60-63 caspase 3 Rattus norvegicus 17-26 27861627-3 2016 Cyclosporin A (CsA) prevented mitochondrial permeability transition pore opening and apoptosis; there was mitochondrial ultrastructural disruption, mitochondrial cytochrome c (cyt c) translocation to the cytoplasm, and subsequent caspase-9 and caspase-3 activation. Cyclosporine 0-13 caspase 3 Rattus norvegicus 244-253 27861627-3 2016 Cyclosporin A (CsA) prevented mitochondrial permeability transition pore opening and apoptosis; there was mitochondrial ultrastructural disruption, mitochondrial cytochrome c (cyt c) translocation to the cytoplasm, and subsequent caspase-9 and caspase-3 activation. Cyclosporine 15-18 caspase 3 Rattus norvegicus 244-253 27357441-4 2016 In addition, CsA treatment blocked the CoCl2-induced increases in ROS production and mitochondrial dysfunction, including a decrease in membrane potential, cytochrome c (cyto-c) release, Bax/Bcl-2 imbalance, as well as the ratios of cl-casp-9/casp-9 and cl-casp-3/casp-3 ratios, via the inhibition of p38 and ERK MAPK signaling pathways. Cyclosporine 13-16 caspase 3 Rattus norvegicus 257-263 27357441-4 2016 In addition, CsA treatment blocked the CoCl2-induced increases in ROS production and mitochondrial dysfunction, including a decrease in membrane potential, cytochrome c (cyto-c) release, Bax/Bcl-2 imbalance, as well as the ratios of cl-casp-9/casp-9 and cl-casp-3/casp-3 ratios, via the inhibition of p38 and ERK MAPK signaling pathways. Cyclosporine 13-16 caspase 3 Rattus norvegicus 264-270 26082307-4 2016 Simultaneously, Pb-induced caspase-3 activation and apoptosis can be significantly inhibited by three MPTP inhibitors (CsA, DIDS, BA), which target different regulatory components of MPTP (Cyp-D, VDAC, ANT), respectively, demonstrating that Cyp-D, VDAC and ANT participate in MPTP regulation during lead exposure. Cyclosporine 119-122 caspase 3 Rattus norvegicus 27-36 27298826-7 2016 The following biochemical changes were observed in CsA-treated animals: increased levels of ALT, AST, and bilirubin in the serum, statistically significant changes in oxidative stress parameters, and lipid peroxidation products in the liver supernatants: MDA+4HAE, GSH, GSSG, caspase 3 activity, and ADP/ATP, NAD(+)/NADH, and NADP(+)/NADPH ratios. Cyclosporine 51-54 caspase 3 Rattus norvegicus 276-285 24261911-7 2014 RESULTS: In CsA-treated rats, bcl-2 expression was significantly upregulated, whereas caspase-3 expression was downregulated, along with a reduced number of TUNEL-positive cells. Cyclosporine 12-15 caspase 3 Rattus norvegicus 86-95 25199566-10 2014 Furthermore, the down-regulation of cytochrome c and ICAD protein expression and the blockage of caspase-3 activity were observed upon CSA treatment. Cyclosporine 135-138 caspase 3 Rattus norvegicus 97-106 24157049-6 2013 RESULTS: CsA treatment caused diabetes, renal dysfunction, tubulointerstitial inflammation (ED-1-positive cells), and fibrosis, which were accompanied by an increase in 8-OHdG production and upregulation of TGF-beta1, caspase-3, and LC3-II. Cyclosporine 9-12 caspase 3 Rattus norvegicus 218-227 23595141-6 2013 Both diazoxide and cyclosporin A exerted significant protective effects on cell viability by ameliorating the decrease in Bcl-2 and the increase in cytochrome c and caspase-3 activity induced by A-beta1-42. Cyclosporine 19-32 caspase 3 Rattus norvegicus 165-174 23683031-10 2013 CsA increased the protein expression of bax, cleaved caspase-9, caspase-3 and the activity of caspase-3; however, the anti-apoptotic bcl-2 protein was reduced. Cyclosporine 0-3 caspase 3 Rattus norvegicus 64-73 23683031-10 2013 CsA increased the protein expression of bax, cleaved caspase-9, caspase-3 and the activity of caspase-3; however, the anti-apoptotic bcl-2 protein was reduced. Cyclosporine 0-3 caspase 3 Rattus norvegicus 94-103 23160799-10 2013 Dvl-1 down-regulation decreased the apoptotic rate, caspase-3 activity, and the Bax/Bcl-2 ratio in H9c2 cells treated with CsA. Cyclosporine 123-126 caspase 3 Rattus norvegicus 52-61 24282430-6 2013 In addition, apoptotic cells, infiltrated inflammatory cells, and active caspase-3+ cells were greatly reduced by HBSP in the both IR and IR + CsA groups. Cyclosporine 143-146 caspase 3 Rattus norvegicus 73-82 24282430-8 2013 Taken together, it has been demonstrated, for the first time, that HBSP effectively improved renal function and tissue damage caused by IR and/or CsA, which might be through reducing caspase-3 activation and synthesis, apoptosis, and inflammation. Cyclosporine 146-149 caspase 3 Rattus norvegicus 183-192 22678567-5 2012 H9c2 cells were treated with CsA in a dose-dependent manner, and decreased Bcl-2 expression, increased Bax expression, and caspase-3 activation were observed. Cyclosporine 29-32 caspase 3 Rattus norvegicus 123-132 22678567-9 2012 Furthermore, the MEK1/2 inhibitor U0126 and the p38 MAPK inhibitor SB203580 markedly blocked the effect of CsA on cell apoptosis, apoptotic-related protein expression, and caspase-3 activation. Cyclosporine 107-110 caspase 3 Rattus norvegicus 172-181