Participation of protein kinase C in the activation of Nrf2 signaling by ischemic preconditioning in the isolated rabbit heart
Activation of protein kinase C (PKC) is a critical intracellular signaling triggered by ischemic preconditioning (IPC), but the precise mechanisms underlying the actions of PKC in IPC-mediated cardioprotection remain unclear. Here, we investigated the role of PKC activation on the antioxidant activi...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2013, Vol.372 (1-2), p.169-179 |
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| creator | Zhang, Xin Xiao, Zhibin Yao, Jianmin Zhao, Genshang Fa, Xianen Niu, Jianli |
| description | Activation of protein kinase C (PKC) is a critical intracellular signaling triggered by ischemic preconditioning (IPC), but the precise mechanisms underlying the actions of PKC in IPC-mediated cardioprotection remain unclear. Here, we investigated the role of PKC activation on the antioxidant activity by IPC in rabbit hearts. Isolated rabbit hearts were subjected to 60 min of global ischemia by cold cardioplegic arrest (4 °C) and 60 min of reperfusion (37 °C). IPC was induced by three cycles of 2-min ischemia following 3 min of reperfusion (37 °C) before cardioplegic arrest. IPC resulted in a better recovery of mechanical function, increased tissue reduced glutathione-to-oxidized glutathione ratio (GSH/GSSG), superoxide dismutase and catalase content, and decreased tissue malondialdehyde (MDA) content compared to control hearts subjected to 60 min of cardioplegic ischemia and 60 min of reperfusion. IPC also significantly induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and the inductions of antioxidant genes heme oxygenase-1 (HO-1) and manganese superoxide dismutase (MnSOD). Injection of phorbol 12-myristate 13 acetate, an activator of PKC, before cardioplegic ischemia induced translocation of PKC-δ and -ε isoforms to membrane fraction, nuclear accumulation of Nrf2, and conferred cardioprotection similar to IPC. Polymyxin B, an inhibitor of PKC, blocked the membrane translocation of PKC-δ and -ε during IPC, inhibited Nrf2 nuclear accumulation, and significantly diminished the IPC-induced cardioprotection when administrated before IPC. These results indicate that the activation of PKC induces the translocation of Nrf2 and the enhancement of endogenous antioxidant defenses in the IPC hearts and suggest that PKC may target Nrf2 to confer cardioprotection. |
| doi_str_mv | 10.1007/s11010-012-1458-9 |
| format | Article |
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Here, we investigated the role of PKC activation on the antioxidant activity by IPC in rabbit hearts. Isolated rabbit hearts were subjected to 60 min of global ischemia by cold cardioplegic arrest (4 °C) and 60 min of reperfusion (37 °C). IPC was induced by three cycles of 2-min ischemia following 3 min of reperfusion (37 °C) before cardioplegic arrest. IPC resulted in a better recovery of mechanical function, increased tissue reduced glutathione-to-oxidized glutathione ratio (GSH/GSSG), superoxide dismutase and catalase content, and decreased tissue malondialdehyde (MDA) content compared to control hearts subjected to 60 min of cardioplegic ischemia and 60 min of reperfusion. IPC also significantly induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and the inductions of antioxidant genes heme oxygenase-1 (HO-1) and manganese superoxide dismutase (MnSOD). Injection of phorbol 12-myristate 13 acetate, an activator of PKC, before cardioplegic ischemia induced translocation of PKC-δ and -ε isoforms to membrane fraction, nuclear accumulation of Nrf2, and conferred cardioprotection similar to IPC. Polymyxin B, an inhibitor of PKC, blocked the membrane translocation of PKC-δ and -ε during IPC, inhibited Nrf2 nuclear accumulation, and significantly diminished the IPC-induced cardioprotection when administrated before IPC. These results indicate that the activation of PKC induces the translocation of Nrf2 and the enhancement of endogenous antioxidant defenses in the IPC hearts and suggest that PKC may target Nrf2 to confer cardioprotection.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-012-1458-9</identifier><identifier>PMID: 23010891</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Animals ; Antioxidants ; Antioxidants - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Cardiology ; Cardioplegic Solutions - pharmacology ; Cell Nucleus - metabolism ; Coronary Vessels - physiopathology ; Enzyme Activation - drug effects ; Female ; Gene Expression - drug effects ; Glutathione - metabolism ; Heart ; In Vitro Techniques ; Ischemia ; Ischemic Preconditioning ; Isoenzymes - antagonists & inhibitors ; Isoenzymes - metabolism ; Isoenzymes - physiology ; L-Lactate Dehydrogenase - metabolism ; Life Sciences ; Male ; Malondialdehyde - metabolism ; Manganese ; Medical Biochemistry ; Myocardial Contraction - drug effects ; Myocardium - enzymology ; Myocardium - metabolism ; NF-E2-Related Factor 2 - metabolism ; Oncology ; Oxidative Stress ; Polymyxin B - pharmacology ; Protein Kinase C-delta - antagonists & inhibitors ; Protein Kinase C-delta - metabolism ; Protein Kinase C-delta - physiology ; Protein Kinase C-epsilon - antagonists & inhibitors ; Protein Kinase C-epsilon - metabolism ; Protein Kinase C-epsilon - physiology ; Protein kinases ; Protein Transport ; Proteins ; Rabbits ; Signaling ; Superoxide ; Superoxide Dismutase - metabolism ; Tetradecanoylphorbol Acetate - pharmacology ; Translocation ; Ventricular Function, Left ; Ventricular Pressure</subject><ispartof>Molecular and cellular biochemistry, 2013, Vol.372 (1-2), p.169-179</ispartof><rights>Springer Science+Business Media New York 2012</rights><rights>COPYRIGHT 2013 Springer</rights><rights>Springer Science+Business Media New York 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c439t-523e43b2047029659d5560f6769c308a66f303ee828f353176a5e460021647293</citedby><cites>FETCH-LOGICAL-c439t-523e43b2047029659d5560f6769c308a66f303ee828f353176a5e460021647293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11010-012-1458-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11010-012-1458-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27922,27923,41486,42555,51317</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23010891$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Xin</creatorcontrib><creatorcontrib>Xiao, Zhibin</creatorcontrib><creatorcontrib>Yao, Jianmin</creatorcontrib><creatorcontrib>Zhao, Genshang</creatorcontrib><creatorcontrib>Fa, Xianen</creatorcontrib><creatorcontrib>Niu, Jianli</creatorcontrib><title>Participation of protein kinase C in the activation of Nrf2 signaling by ischemic preconditioning in the isolated rabbit heart</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>Activation of protein kinase C (PKC) is a critical intracellular signaling triggered by ischemic preconditioning (IPC), but the precise mechanisms underlying the actions of PKC in IPC-mediated cardioprotection remain unclear. Here, we investigated the role of PKC activation on the antioxidant activity by IPC in rabbit hearts. Isolated rabbit hearts were subjected to 60 min of global ischemia by cold cardioplegic arrest (4 °C) and 60 min of reperfusion (37 °C). IPC was induced by three cycles of 2-min ischemia following 3 min of reperfusion (37 °C) before cardioplegic arrest. IPC resulted in a better recovery of mechanical function, increased tissue reduced glutathione-to-oxidized glutathione ratio (GSH/GSSG), superoxide dismutase and catalase content, and decreased tissue malondialdehyde (MDA) content compared to control hearts subjected to 60 min of cardioplegic ischemia and 60 min of reperfusion. IPC also significantly induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and the inductions of antioxidant genes heme oxygenase-1 (HO-1) and manganese superoxide dismutase (MnSOD). Injection of phorbol 12-myristate 13 acetate, an activator of PKC, before cardioplegic ischemia induced translocation of PKC-δ and -ε isoforms to membrane fraction, nuclear accumulation of Nrf2, and conferred cardioprotection similar to IPC. Polymyxin B, an inhibitor of PKC, blocked the membrane translocation of PKC-δ and -ε during IPC, inhibited Nrf2 nuclear accumulation, and significantly diminished the IPC-induced cardioprotection when administrated before IPC. These results indicate that the activation of PKC induces the translocation of Nrf2 and the enhancement of endogenous antioxidant defenses in the IPC hearts and suggest that PKC may target Nrf2 to confer cardioprotection.</description><subject>Animals</subject><subject>Antioxidants</subject><subject>Antioxidants - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cardiology</subject><subject>Cardioplegic Solutions - pharmacology</subject><subject>Cell Nucleus - metabolism</subject><subject>Coronary Vessels - physiopathology</subject><subject>Enzyme Activation - drug effects</subject><subject>Female</subject><subject>Gene Expression - drug effects</subject><subject>Glutathione - metabolism</subject><subject>Heart</subject><subject>In Vitro Techniques</subject><subject>Ischemia</subject><subject>Ischemic Preconditioning</subject><subject>Isoenzymes - antagonists & inhibitors</subject><subject>Isoenzymes - metabolism</subject><subject>Isoenzymes - physiology</subject><subject>L-Lactate Dehydrogenase - metabolism</subject><subject>Life Sciences</subject><subject>Male</subject><subject>Malondialdehyde - metabolism</subject><subject>Manganese</subject><subject>Medical Biochemistry</subject><subject>Myocardial Contraction - drug effects</subject><subject>Myocardium - enzymology</subject><subject>Myocardium - metabolism</subject><subject>NF-E2-Related Factor 2 - metabolism</subject><subject>Oncology</subject><subject>Oxidative Stress</subject><subject>Polymyxin B - pharmacology</subject><subject>Protein Kinase C-delta - antagonists & inhibitors</subject><subject>Protein Kinase C-delta - metabolism</subject><subject>Protein Kinase C-delta - physiology</subject><subject>Protein Kinase C-epsilon - antagonists & inhibitors</subject><subject>Protein Kinase C-epsilon - metabolism</subject><subject>Protein Kinase C-epsilon - physiology</subject><subject>Protein kinases</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Signaling</subject><subject>Superoxide</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><subject>Translocation</subject><subject>Ventricular Function, Left</subject><subject>Ventricular 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of protein kinase C in the activation of Nrf2 signaling by ischemic preconditioning in the isolated rabbit heart</title><author>Zhang, Xin ; Xiao, Zhibin ; Yao, Jianmin ; Zhao, Genshang ; Fa, Xianen ; Niu, Jianli</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-523e43b2047029659d5560f6769c308a66f303ee828f353176a5e460021647293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Antioxidants</topic><topic>Antioxidants - metabolism</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cardiology</topic><topic>Cardioplegic Solutions - pharmacology</topic><topic>Cell Nucleus - metabolism</topic><topic>Coronary Vessels - physiopathology</topic><topic>Enzyme Activation - drug effects</topic><topic>Female</topic><topic>Gene Expression - drug effects</topic><topic>Glutathione - metabolism</topic><topic>Heart</topic><topic>In Vitro Techniques</topic><topic>Ischemia</topic><topic>Ischemic Preconditioning</topic><topic>Isoenzymes - antagonists & inhibitors</topic><topic>Isoenzymes - metabolism</topic><topic>Isoenzymes - physiology</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Life Sciences</topic><topic>Male</topic><topic>Malondialdehyde - metabolism</topic><topic>Manganese</topic><topic>Medical Biochemistry</topic><topic>Myocardial Contraction - drug effects</topic><topic>Myocardium - enzymology</topic><topic>Myocardium - metabolism</topic><topic>NF-E2-Related Factor 2 - metabolism</topic><topic>Oncology</topic><topic>Oxidative Stress</topic><topic>Polymyxin B - pharmacology</topic><topic>Protein Kinase C-delta - antagonists & inhibitors</topic><topic>Protein Kinase C-delta - metabolism</topic><topic>Protein Kinase C-delta - physiology</topic><topic>Protein Kinase C-epsilon - antagonists & inhibitors</topic><topic>Protein Kinase C-epsilon - metabolism</topic><topic>Protein Kinase C-epsilon - physiology</topic><topic>Protein kinases</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Signaling</topic><topic>Superoxide</topic><topic>Superoxide Dismutase - metabolism</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><topic>Translocation</topic><topic>Ventricular Function, Left</topic><topic>Ventricular Pressure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Xin</creatorcontrib><creatorcontrib>Xiao, Zhibin</creatorcontrib><creatorcontrib>Yao, Jianmin</creatorcontrib><creatorcontrib>Zhao, Genshang</creatorcontrib><creatorcontrib>Fa, Xianen</creatorcontrib><creatorcontrib>Niu, Jianli</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Xin</au><au>Xiao, Zhibin</au><au>Yao, Jianmin</au><au>Zhao, Genshang</au><au>Fa, Xianen</au><au>Niu, Jianli</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Participation of protein kinase C in the activation of Nrf2 signaling by ischemic preconditioning in the isolated rabbit heart</atitle><jtitle>Molecular and cellular biochemistry</jtitle><stitle>Mol Cell Biochem</stitle><addtitle>Mol Cell Biochem</addtitle><date>2013</date><risdate>2013</risdate><volume>372</volume><issue>1-2</issue><spage>169</spage><epage>179</epage><pages>169-179</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>Activation of protein kinase C (PKC) is a critical intracellular signaling triggered by ischemic preconditioning (IPC), but the precise mechanisms underlying the actions of PKC in IPC-mediated cardioprotection remain unclear. Here, we investigated the role of PKC activation on the antioxidant activity by IPC in rabbit hearts. Isolated rabbit hearts were subjected to 60 min of global ischemia by cold cardioplegic arrest (4 °C) and 60 min of reperfusion (37 °C). IPC was induced by three cycles of 2-min ischemia following 3 min of reperfusion (37 °C) before cardioplegic arrest. IPC resulted in a better recovery of mechanical function, increased tissue reduced glutathione-to-oxidized glutathione ratio (GSH/GSSG), superoxide dismutase and catalase content, and decreased tissue malondialdehyde (MDA) content compared to control hearts subjected to 60 min of cardioplegic ischemia and 60 min of reperfusion. IPC also significantly induced activation of nuclear factor erythroid 2-related factor 2 (Nrf2) and the inductions of antioxidant genes heme oxygenase-1 (HO-1) and manganese superoxide dismutase (MnSOD). Injection of phorbol 12-myristate 13 acetate, an activator of PKC, before cardioplegic ischemia induced translocation of PKC-δ and -ε isoforms to membrane fraction, nuclear accumulation of Nrf2, and conferred cardioprotection similar to IPC. Polymyxin B, an inhibitor of PKC, blocked the membrane translocation of PKC-δ and -ε during IPC, inhibited Nrf2 nuclear accumulation, and significantly diminished the IPC-induced cardioprotection when administrated before IPC. These results indicate that the activation of PKC induces the translocation of Nrf2 and the enhancement of endogenous antioxidant defenses in the IPC hearts and suggest that PKC may target Nrf2 to confer cardioprotection.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>23010891</pmid><doi>10.1007/s11010-012-1458-9</doi><tpages>11</tpages></addata></record> |
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| subjects | Animals Antioxidants Antioxidants - metabolism Biochemistry Biomedical and Life Sciences Cardiology Cardioplegic Solutions - pharmacology Cell Nucleus - metabolism Coronary Vessels - physiopathology Enzyme Activation - drug effects Female Gene Expression - drug effects Glutathione - metabolism Heart In Vitro Techniques Ischemia Ischemic Preconditioning Isoenzymes - antagonists & inhibitors Isoenzymes - metabolism Isoenzymes - physiology L-Lactate Dehydrogenase - metabolism Life Sciences Male Malondialdehyde - metabolism Manganese Medical Biochemistry Myocardial Contraction - drug effects Myocardium - enzymology Myocardium - metabolism NF-E2-Related Factor 2 - metabolism Oncology Oxidative Stress Polymyxin B - pharmacology Protein Kinase C-delta - antagonists & inhibitors Protein Kinase C-delta - metabolism Protein Kinase C-delta - physiology Protein Kinase C-epsilon - antagonists & inhibitors Protein Kinase C-epsilon - metabolism Protein Kinase C-epsilon - physiology Protein kinases Protein Transport Proteins Rabbits Signaling Superoxide Superoxide Dismutase - metabolism Tetradecanoylphorbol Acetate - pharmacology Translocation Ventricular Function, Left Ventricular Pressure |
| title | Participation of protein kinase C in the activation of Nrf2 signaling by ischemic preconditioning in the isolated rabbit heart |
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