Heat shock protein 70 inhibits cardiomyocyte necroptosis through repressing autophagy in myocardial ischemia/reperfusion injury
Irreversible damage of cardiac function arisen from myocardial ischemia/reperfusion injury (MIRI) leads to an emerging challenge in the treatments of cardiac ischemic diseases. Molecular chaperone heat shock protein 70 (HSP70) attenuates heat-stimulated cell autophagy, apoptosis, and damage in the h...
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| Veröffentlicht in: | In vitro cellular & developmental biology. Animal 2016-06, Vol.52 (6), p.690-698 |
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| container_title | In vitro cellular & developmental biology. Animal |
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| creator | Liu, Xiaojuan Zhang, Chao Zhang, Chi Li, Jingjing Guo, Wanwan Yan, Daliang Yang, Chen Zhao, Jianhua Xia, Tian Wang, Yuqing Xu, Rong Wu, Xiang Shi, Jiahai |
| description | Irreversible damage of cardiac function arisen from myocardial ischemia/reperfusion injury (MIRI) leads to an emerging challenge in the treatments of cardiac ischemic diseases. Molecular chaperone heat shock protein 70 (HSP70) attenuates heat-stimulated cell autophagy, apoptosis, and damage in the heart. Under specific conditions, autophagy may, directly or indirectly, induce cell death including necroptosis. Whether HSP70 inhibits cardiomyocyte necroptosis via suppressing autophagy during MIRI is unknown. In our study, HSP70 expression was opposite to necroptosis marker RIP1 and autophagy marker LC3A/B expression after myocardial ischemia/reperfusion (MIR) in vivo. Furthermore, in vitro primary rat cardiomyocytes mimicked MIRI by hypoxia/reoxygenation (H/R) treatment. Knockdown of HSP70 expression promoted cardiomyocyte autophagy and necroptosis following H/R treatment, while the increase tendency was downregulated by autophagy inhibitor 3-MA, showing that autophagy-induced necroptosis could be suppressed by HSP70. In summary, HSP70 downregulates cardiomyocyte necroptosis through suppressing autophagy during myocardial IR, revealing the novel protective mechanism of HSP70 and supplying a novel molecular target for the treatment of heart ischemic diseases. |
| doi_str_mv | 10.1007/s11626-016-0039-8 |
| format | Article |
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Molecular chaperone heat shock protein 70 (HSP70) attenuates heat-stimulated cell autophagy, apoptosis, and damage in the heart. Under specific conditions, autophagy may, directly or indirectly, induce cell death including necroptosis. Whether HSP70 inhibits cardiomyocyte necroptosis via suppressing autophagy during MIRI is unknown. In our study, HSP70 expression was opposite to necroptosis marker RIP1 and autophagy marker LC3A/B expression after myocardial ischemia/reperfusion (MIR) in vivo. Furthermore, in vitro primary rat cardiomyocytes mimicked MIRI by hypoxia/reoxygenation (H/R) treatment. Knockdown of HSP70 expression promoted cardiomyocyte autophagy and necroptosis following H/R treatment, while the increase tendency was downregulated by autophagy inhibitor 3-MA, showing that autophagy-induced necroptosis could be suppressed by HSP70. In summary, HSP70 downregulates cardiomyocyte necroptosis through suppressing autophagy during myocardial IR, revealing the novel protective mechanism of HSP70 and supplying a novel molecular target for the treatment of heart ischemic diseases.</description><identifier>ISSN: 1071-2690</identifier><identifier>EISSN: 1543-706X</identifier><identifier>DOI: 10.1007/s11626-016-0039-8</identifier><identifier>PMID: 27130675</identifier><identifier>CODEN: IVCAED</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Animal Genetics and Genomics ; Animals ; Autophagy - physiology ; Biomedical and Life Sciences ; CELL AND TISSUE MODELS ; Cell Biology ; Cell Culture ; Cell Hypoxia ; Developmental Biology ; Down-Regulation ; Gene Knockdown Techniques ; HSP70 Heat-Shock Proteins - antagonists & inhibitors ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - physiology ; Immunohistochemistry ; Life Sciences ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; Myocardial Reperfusion Injury - pathology ; Myocytes, Cardiac - metabolism ; Myocytes, Cardiac - pathology ; Necrosis - physiopathology ; Protein-Serine-Threonine Kinases ; Rats ; Rats, Sprague-Dawley ; Stem Cells</subject><ispartof>In vitro cellular & developmental biology. Animal, 2016-06, Vol.52 (6), p.690-698</ispartof><rights>2016 Society for In Vitro Biology</rights><rights>The Society for In Vitro Biology 2016</rights><rights>Copyright Society for In Vitro Biology Jun 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-a77571bdd0cb7bd6661483e011aed4791e7b42f910c88862da27227313ef12853</citedby><cites>FETCH-LOGICAL-c418t-a77571bdd0cb7bd6661483e011aed4791e7b42f910c88862da27227313ef12853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/26588330$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/26588330$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,27924,27925,41488,42557,51319,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27130675$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Xiaojuan</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Li, Jingjing</creatorcontrib><creatorcontrib>Guo, Wanwan</creatorcontrib><creatorcontrib>Yan, Daliang</creatorcontrib><creatorcontrib>Yang, Chen</creatorcontrib><creatorcontrib>Zhao, Jianhua</creatorcontrib><creatorcontrib>Xia, Tian</creatorcontrib><creatorcontrib>Wang, Yuqing</creatorcontrib><creatorcontrib>Xu, Rong</creatorcontrib><creatorcontrib>Wu, Xiang</creatorcontrib><creatorcontrib>Shi, Jiahai</creatorcontrib><title>Heat shock protein 70 inhibits cardiomyocyte necroptosis through repressing autophagy in myocardial ischemia/reperfusion injury</title><title>In vitro cellular & developmental biology. Animal</title><addtitle>In Vitro Cell.Dev.Biol.-Animal</addtitle><addtitle>In Vitro Cell Dev Biol Anim</addtitle><description>Irreversible damage of cardiac function arisen from myocardial ischemia/reperfusion injury (MIRI) leads to an emerging challenge in the treatments of cardiac ischemic diseases. Molecular chaperone heat shock protein 70 (HSP70) attenuates heat-stimulated cell autophagy, apoptosis, and damage in the heart. Under specific conditions, autophagy may, directly or indirectly, induce cell death including necroptosis. Whether HSP70 inhibits cardiomyocyte necroptosis via suppressing autophagy during MIRI is unknown. In our study, HSP70 expression was opposite to necroptosis marker RIP1 and autophagy marker LC3A/B expression after myocardial ischemia/reperfusion (MIR) in vivo. Furthermore, in vitro primary rat cardiomyocytes mimicked MIRI by hypoxia/reoxygenation (H/R) treatment. Knockdown of HSP70 expression promoted cardiomyocyte autophagy and necroptosis following H/R treatment, while the increase tendency was downregulated by autophagy inhibitor 3-MA, showing that autophagy-induced necroptosis could be suppressed by HSP70. In summary, HSP70 downregulates cardiomyocyte necroptosis through suppressing autophagy during myocardial IR, revealing the novel protective mechanism of HSP70 and supplying a novel molecular target for the treatment of heart ischemic diseases.</description><subject>Animal Genetics and Genomics</subject><subject>Animals</subject><subject>Autophagy - physiology</subject><subject>Biomedical and Life Sciences</subject><subject>CELL AND TISSUE MODELS</subject><subject>Cell Biology</subject><subject>Cell Culture</subject><subject>Cell Hypoxia</subject><subject>Developmental Biology</subject><subject>Down-Regulation</subject><subject>Gene Knockdown Techniques</subject><subject>HSP70 Heat-Shock Proteins - antagonists & inhibitors</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - physiology</subject><subject>Immunohistochemistry</subject><subject>Life Sciences</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Myocardial Reperfusion Injury - pathology</subject><subject>Myocytes, Cardiac - metabolism</subject><subject>Myocytes, Cardiac - pathology</subject><subject>Necrosis - physiopathology</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Stem Cells</subject><issn>1071-2690</issn><issn>1543-706X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kU-P1SAUxYnROOPoB3ChkrhxU4cLLdDlZKKOySQudBJ3hLa05flaKtBFV35170vHP3EhCYHk_s6Bew8hz4G9BcbUZQKQXBYMcDNRF_oBOYeqFIVi8utDvDMFBZc1OyNPUjowXDXIx-SMKxBMquqc_LhxNtM0hvYbXWLIzs9UMern0Tc-J9ra2PkwbaHdsqOza2NYckg-0TzGsA4jjW6JLiU_D9SuOSyjHTbU05PmJLZH6lM7usnbS2Rd7Nfkw4zIYY3bU_Kot8fknt2fF-Tu_bsv1zfF7acPH6-vbou2BJ0Lq1SloOk61jaq6aSUUGrhGIB1XalqcKopeV8Da7XWkneWK86VAOF64LoSF-TN7otNfl9dymbCX7nj0c4urMmAqiuteMkloq__QQ9hjTP-zoBmDCoco0IKdgonklJ0vVmin2zcDDBzSsfs6RhMx5zSMRo1L--d12Zy3W_FrzgQ4DuQsDQPLv719H9cX-yiQ8oh_jGVldZCMKy_2uu9DcYO0Sdz95mjAfaCbwolfgIAaa6l</recordid><startdate>20160601</startdate><enddate>20160601</enddate><creator>Liu, Xiaojuan</creator><creator>Zhang, Chao</creator><creator>Zhang, Chi</creator><creator>Li, Jingjing</creator><creator>Guo, Wanwan</creator><creator>Yan, Daliang</creator><creator>Yang, Chen</creator><creator>Zhao, Jianhua</creator><creator>Xia, Tian</creator><creator>Wang, Yuqing</creator><creator>Xu, Rong</creator><creator>Wu, Xiang</creator><creator>Shi, Jiahai</creator><general>Springer US</general><general>Springer Science & Business Media LLC</general><general>Society for In Vitro Biology</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>4T-</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope></search><sort><creationdate>20160601</creationdate><title>Heat shock protein 70 inhibits cardiomyocyte necroptosis through repressing autophagy in myocardial ischemia/reperfusion injury</title><author>Liu, Xiaojuan ; Zhang, Chao ; Zhang, Chi ; Li, Jingjing ; Guo, Wanwan ; Yan, Daliang ; Yang, Chen ; Zhao, Jianhua ; Xia, Tian ; Wang, Yuqing ; Xu, Rong ; Wu, Xiang ; Shi, Jiahai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-a77571bdd0cb7bd6661483e011aed4791e7b42f910c88862da27227313ef12853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animal Genetics and Genomics</topic><topic>Animals</topic><topic>Autophagy - physiology</topic><topic>Biomedical and Life Sciences</topic><topic>CELL AND TISSUE MODELS</topic><topic>Cell Biology</topic><topic>Cell Culture</topic><topic>Cell Hypoxia</topic><topic>Developmental Biology</topic><topic>Down-Regulation</topic><topic>Gene Knockdown Techniques</topic><topic>HSP70 Heat-Shock Proteins - antagonists & inhibitors</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - physiology</topic><topic>Immunohistochemistry</topic><topic>Life Sciences</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Myocardial Reperfusion Injury - pathology</topic><topic>Myocytes, Cardiac - metabolism</topic><topic>Myocytes, Cardiac - pathology</topic><topic>Necrosis - physiopathology</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Stem Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Xiaojuan</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Zhang, Chi</creatorcontrib><creatorcontrib>Li, Jingjing</creatorcontrib><creatorcontrib>Guo, Wanwan</creatorcontrib><creatorcontrib>Yan, Daliang</creatorcontrib><creatorcontrib>Yang, Chen</creatorcontrib><creatorcontrib>Zhao, Jianhua</creatorcontrib><creatorcontrib>Xia, Tian</creatorcontrib><creatorcontrib>Wang, Yuqing</creatorcontrib><creatorcontrib>Xu, Rong</creatorcontrib><creatorcontrib>Wu, Xiang</creatorcontrib><creatorcontrib>Shi, Jiahai</creatorcontrib><collection>AGRIS</collection><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 (Corporate)</collection><collection>Docstoc</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - 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Animal</jtitle><stitle>In Vitro Cell.Dev.Biol.-Animal</stitle><addtitle>In Vitro Cell Dev Biol Anim</addtitle><date>2016-06-01</date><risdate>2016</risdate><volume>52</volume><issue>6</issue><spage>690</spage><epage>698</epage><pages>690-698</pages><issn>1071-2690</issn><eissn>1543-706X</eissn><coden>IVCAED</coden><abstract>Irreversible damage of cardiac function arisen from myocardial ischemia/reperfusion injury (MIRI) leads to an emerging challenge in the treatments of cardiac ischemic diseases. Molecular chaperone heat shock protein 70 (HSP70) attenuates heat-stimulated cell autophagy, apoptosis, and damage in the heart. Under specific conditions, autophagy may, directly or indirectly, induce cell death including necroptosis. Whether HSP70 inhibits cardiomyocyte necroptosis via suppressing autophagy during MIRI is unknown. In our study, HSP70 expression was opposite to necroptosis marker RIP1 and autophagy marker LC3A/B expression after myocardial ischemia/reperfusion (MIR) in vivo. Furthermore, in vitro primary rat cardiomyocytes mimicked MIRI by hypoxia/reoxygenation (H/R) treatment. Knockdown of HSP70 expression promoted cardiomyocyte autophagy and necroptosis following H/R treatment, while the increase tendency was downregulated by autophagy inhibitor 3-MA, showing that autophagy-induced necroptosis could be suppressed by HSP70. In summary, HSP70 downregulates cardiomyocyte necroptosis through suppressing autophagy during myocardial IR, revealing the novel protective mechanism of HSP70 and supplying a novel molecular target for the treatment of heart ischemic diseases.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>27130675</pmid><doi>10.1007/s11626-016-0039-8</doi><tpages>9</tpages></addata></record> |
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| subjects | Animal Genetics and Genomics Animals Autophagy - physiology Biomedical and Life Sciences CELL AND TISSUE MODELS Cell Biology Cell Culture Cell Hypoxia Developmental Biology Down-Regulation Gene Knockdown Techniques HSP70 Heat-Shock Proteins - antagonists & inhibitors HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - physiology Immunohistochemistry Life Sciences Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Myocardial Reperfusion Injury - pathology Myocytes, Cardiac - metabolism Myocytes, Cardiac - pathology Necrosis - physiopathology Protein-Serine-Threonine Kinases Rats Rats, Sprague-Dawley Stem Cells |
| title | Heat shock protein 70 inhibits cardiomyocyte necroptosis through repressing autophagy in myocardial ischemia/reperfusion injury |
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