Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion
A tight quality control system over protein folding, turnover and synthesis, involving molecular chaperones and co-chaperones, maintains the balance of cardiac proteins. Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misf...
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| Veröffentlicht in: | Molecular and cellular biochemistry 2020, Vol.464 (1-2), p.21-26 |
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| creator | Nair, Sreejit Parameswaran Sharma, Rajendra K. |
| description | A tight quality control system over protein folding, turnover and synthesis, involving molecular chaperones and co-chaperones, maintains the balance of cardiac proteins. Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misfolding due to an overwhelmed quality control system. The toxic nature of accumulated misfolded proteins further worsens the condition. The important molecular chaperones which act as quality control proteins are involved in protecting the heart, these include heat shock protein70 (HSP70) and HSP90. Here, we review the emerging roles of heat shock proteins in the maintenance of cardiac cell populations in experimental models of ischemia/reperfusion (I/R) injury. Furthermore, we discuss the expression of HSP70 and HSP90 with therapeutic and diagnostic considerations. Although there is only a partial understanding of these important HSPs in I/R injury, there is an immense therapeutic potential of modulating these HSPs to counteract the imbalance between misfolding and endogenous protein quality control systems. |
| doi_str_mv | 10.1007/s11010-019-03645-1 |
| format | Article |
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Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misfolding due to an overwhelmed quality control system. The toxic nature of accumulated misfolded proteins further worsens the condition. The important molecular chaperones which act as quality control proteins are involved in protecting the heart, these include heat shock protein70 (HSP70) and HSP90. Here, we review the emerging roles of heat shock proteins in the maintenance of cardiac cell populations in experimental models of ischemia/reperfusion (I/R) injury. Furthermore, we discuss the expression of HSP70 and HSP90 with therapeutic and diagnostic considerations. Although there is only a partial understanding of these important HSPs in I/R injury, there is an immense therapeutic potential of modulating these HSPs to counteract the imbalance between misfolding and endogenous protein quality control systems.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1007/s11010-019-03645-1</identifier><identifier>PMID: 31677029</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Analysis ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Cardiology ; Cell culture ; Chaperones ; Chemical synthesis ; Control systems ; Diagnostic systems ; Gene Expression Regulation ; Heart ; Heart attack ; Heat shock proteins ; HSP70 Heat-Shock Proteins - biosynthesis ; Hsp70 protein ; HSP90 Heat-Shock Proteins - biosynthesis ; Hsp90 protein ; Humans ; Ischemia ; Life Sciences ; Medical Biochemistry ; Mice ; Myocardial infarction ; Myocardial Infarction - metabolism ; Myocardial Infarction - pathology ; Myocardial Reperfusion Injury - metabolism ; Myocardial Reperfusion Injury - pathology ; Myocardium - metabolism ; Myocardium - pathology ; Oncology ; Populations ; Post-translation ; Protein biosynthesis ; Protein folding ; Protein turnover ; Proteins ; Quality control ; Quality management ; Reperfusion</subject><ispartof>Molecular and cellular biochemistry, 2020, Vol.464 (1-2), p.21-26</ispartof><rights>Springer Science+Business Media, LLC, part of Springer Nature 2019</rights><rights>COPYRIGHT 2020 Springer</rights><rights>Molecular and Cellular Biochemistry is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-f05b8c63b79df119c384a84d8153f618b304bcf842d3ecdea7588f365867d23b3</citedby><cites>FETCH-LOGICAL-c442t-f05b8c63b79df119c384a84d8153f618b304bcf842d3ecdea7588f365867d23b3</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/s11010-019-03645-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11010-019-03645-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31677029$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nair, Sreejit Parameswaran</creatorcontrib><creatorcontrib>Sharma, Rajendra K.</creatorcontrib><title>Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><addtitle>Mol Cell Biochem</addtitle><description>A tight quality control system over protein folding, turnover and synthesis, involving molecular chaperones and co-chaperones, maintains the balance of cardiac proteins. Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misfolding due to an overwhelmed quality control system. The toxic nature of accumulated misfolded proteins further worsens the condition. The important molecular chaperones which act as quality control proteins are involved in protecting the heart, these include heat shock protein70 (HSP70) and HSP90. Here, we review the emerging roles of heat shock proteins in the maintenance of cardiac cell populations in experimental models of ischemia/reperfusion (I/R) injury. Furthermore, we discuss the expression of HSP70 and HSP90 with therapeutic and diagnostic considerations. Although there is only a partial understanding of these important HSPs in I/R injury, there is an immense therapeutic potential of modulating these HSPs to counteract the imbalance between misfolding and endogenous protein quality control systems.</description><subject>Analysis</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cardiology</subject><subject>Cell culture</subject><subject>Chaperones</subject><subject>Chemical synthesis</subject><subject>Control systems</subject><subject>Diagnostic systems</subject><subject>Gene Expression Regulation</subject><subject>Heart</subject><subject>Heart attack</subject><subject>Heat shock proteins</subject><subject>HSP70 Heat-Shock Proteins - biosynthesis</subject><subject>Hsp70 protein</subject><subject>HSP90 Heat-Shock Proteins - biosynthesis</subject><subject>Hsp90 protein</subject><subject>Humans</subject><subject>Ischemia</subject><subject>Life Sciences</subject><subject>Medical Biochemistry</subject><subject>Mice</subject><subject>Myocardial infarction</subject><subject>Myocardial Infarction - metabolism</subject><subject>Myocardial Infarction - pathology</subject><subject>Myocardial Reperfusion Injury - metabolism</subject><subject>Myocardial Reperfusion Injury - pathology</subject><subject>Myocardium - metabolism</subject><subject>Myocardium - pathology</subject><subject>Oncology</subject><subject>Populations</subject><subject>Post-translation</subject><subject>Protein biosynthesis</subject><subject>Protein folding</subject><subject>Protein turnover</subject><subject>Proteins</subject><subject>Quality control</subject><subject>Quality management</subject><subject>Reperfusion</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</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>eNp9kU9rFTEUxYMo9tn2C7iQgBs3U3MnmSSzLKW1QsGNrkMmuelLnX8mM6Df3kzf06KIZBFIfudw7j2EvAZ2AYyp9xmAAasYtBXjUjQVPCM7aBSvRAvtc7JjnLFKg1In5FXOD6zQDOAlOeEglWJ1uyP5Fu1C835yX-mcpgXjmKkdPV32GBPF73PCnOM00jgWIA42_aDDmuKI1Nnko3XUYd_TeZrX3i6FzNRv__c0ZrfHIdpHv4QzprBuVmfkRbB9xvPjfUq-3Fx_vrqt7j59-Hh1eVc5IeqlCqzptJO8U60PAK3jWlgtvIaGBwm640x0LmhRe47Oo1WN1oHLRkvla97xU_Lu4FsG-7ZiXsxQIpWwdsRpzabmAFIIJpuCvv0LfZjWNJZ0hRK81qoR7RN1b3s0cQzTkqzbTM2lBKaV4HrzuvgHVY4vy3DTiCGW9z8E9UHg0pRzwmCOizbAzNa0OTRtStPmsWkDRfTmmHjtBvS_Jb-qLQA_AHne2sD0NNJ_bH8Cn-ezDQ</recordid><startdate>2020</startdate><enddate>2020</enddate><creator>Nair, Sreejit Parameswaran</creator><creator>Sharma, Rajendra K.</creator><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</general><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>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2020</creationdate><title>Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion</title><author>Nair, Sreejit Parameswaran ; Sharma, Rajendra K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-f05b8c63b79df119c384a84d8153f618b304bcf842d3ecdea7588f365867d23b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Analysis</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cardiology</topic><topic>Cell culture</topic><topic>Chaperones</topic><topic>Chemical synthesis</topic><topic>Control systems</topic><topic>Diagnostic systems</topic><topic>Gene Expression Regulation</topic><topic>Heart</topic><topic>Heart attack</topic><topic>Heat shock proteins</topic><topic>HSP70 Heat-Shock Proteins - biosynthesis</topic><topic>Hsp70 protein</topic><topic>HSP90 Heat-Shock Proteins - biosynthesis</topic><topic>Hsp90 protein</topic><topic>Humans</topic><topic>Ischemia</topic><topic>Life Sciences</topic><topic>Medical Biochemistry</topic><topic>Mice</topic><topic>Myocardial infarction</topic><topic>Myocardial Infarction - metabolism</topic><topic>Myocardial Infarction - pathology</topic><topic>Myocardial Reperfusion Injury - metabolism</topic><topic>Myocardial Reperfusion Injury - pathology</topic><topic>Myocardium - metabolism</topic><topic>Myocardium - pathology</topic><topic>Oncology</topic><topic>Populations</topic><topic>Post-translation</topic><topic>Protein biosynthesis</topic><topic>Protein folding</topic><topic>Protein turnover</topic><topic>Proteins</topic><topic>Quality control</topic><topic>Quality management</topic><topic>Reperfusion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nair, Sreejit Parameswaran</creatorcontrib><creatorcontrib>Sharma, Rajendra K.</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 (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>ProQuest Pharma Collection</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 Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nair, Sreejit Parameswaran</au><au>Sharma, Rajendra K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion</atitle><jtitle>Molecular and cellular biochemistry</jtitle><stitle>Mol Cell Biochem</stitle><addtitle>Mol Cell Biochem</addtitle><date>2020</date><risdate>2020</risdate><volume>464</volume><issue>1-2</issue><spage>21</spage><epage>26</epage><pages>21-26</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>A tight quality control system over protein folding, turnover and synthesis, involving molecular chaperones and co-chaperones, maintains the balance of cardiac proteins. Various cardiac pathologies, including myocardial infarction, increase stresses and post-translational modifications favoring misfolding due to an overwhelmed quality control system. The toxic nature of accumulated misfolded proteins further worsens the condition. The important molecular chaperones which act as quality control proteins are involved in protecting the heart, these include heat shock protein70 (HSP70) and HSP90. Here, we review the emerging roles of heat shock proteins in the maintenance of cardiac cell populations in experimental models of ischemia/reperfusion (I/R) injury. Furthermore, we discuss the expression of HSP70 and HSP90 with therapeutic and diagnostic considerations. Although there is only a partial understanding of these important HSPs in I/R injury, there is an immense therapeutic potential of modulating these HSPs to counteract the imbalance between misfolding and endogenous protein quality control systems.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>31677029</pmid><doi>10.1007/s11010-019-03645-1</doi><tpages>6</tpages></addata></record> |
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| subjects | Analysis Animals Biochemistry Biomedical and Life Sciences Cardiology Cell culture Chaperones Chemical synthesis Control systems Diagnostic systems Gene Expression Regulation Heart Heart attack Heat shock proteins HSP70 Heat-Shock Proteins - biosynthesis Hsp70 protein HSP90 Heat-Shock Proteins - biosynthesis Hsp90 protein Humans Ischemia Life Sciences Medical Biochemistry Mice Myocardial infarction Myocardial Infarction - metabolism Myocardial Infarction - pathology Myocardial Reperfusion Injury - metabolism Myocardial Reperfusion Injury - pathology Myocardium - metabolism Myocardium - pathology Oncology Populations Post-translation Protein biosynthesis Protein folding Protein turnover Proteins Quality control Quality management Reperfusion |
| title | Heat shock proteins and their expression in primary murine cardiac cell populations during ischemia and reperfusion |
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