Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes
Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia...
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Veröffentlicht in: | Molecular and cellular biochemistry 1997-08, Vol.173 (1-2), p.153-159 |
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creator | Laios, E Rebeyka, I M Prody, C A |
description | Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. Our results indicate that hypothermia is capable of inducing the heat shock response in neonatal cardiomyocytes. |
doi_str_mv | 10.1023/A:1006844114348 |
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To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. Our results indicate that hypothermia is capable of inducing the heat shock response in neonatal cardiomyocytes.</description><identifier>ISSN: 0300-8177</identifier><identifier>EISSN: 1573-4919</identifier><identifier>DOI: 10.1023/A:1006844114348</identifier><identifier>PMID: 9278266</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Animals ; Animals, Newborn - metabolism ; Bacteria ; Cardiomyocytes ; Cold Temperature ; Heat shock proteins ; Heat-Shock Proteins - biosynthesis ; HSP70 Heat-Shock Proteins - biosynthesis ; HSP90 Heat-Shock Proteins - biosynthesis ; Hypothermia ; Hypothermia - physiopathology ; Myocardium - cytology ; Myocardium - metabolism ; Proteins ; Rats ; Rats, Wistar ; RNA, Messenger - analysis ; RNA, Messenger - biosynthesis ; Temperature ; Time Factors</subject><ispartof>Molecular and cellular biochemistry, 1997-08, Vol.173 (1-2), p.153-159</ispartof><rights>Kluwer Academic Publishers 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c279t-51b164eb95f682b59f2fb288edd4b84a1849919ea298b579ac4cd12e1ceedde03</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9278266$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Laios, E</creatorcontrib><creatorcontrib>Rebeyka, I M</creatorcontrib><creatorcontrib>Prody, C A</creatorcontrib><title>Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes</title><title>Molecular and cellular biochemistry</title><addtitle>Mol Cell Biochem</addtitle><description>Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. Our results indicate that hypothermia is capable of inducing the heat shock response in neonatal cardiomyocytes.</description><subject>Animals</subject><subject>Animals, Newborn - metabolism</subject><subject>Bacteria</subject><subject>Cardiomyocytes</subject><subject>Cold Temperature</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>HSP70 Heat-Shock Proteins - biosynthesis</subject><subject>HSP90 Heat-Shock Proteins - biosynthesis</subject><subject>Hypothermia</subject><subject>Hypothermia - physiopathology</subject><subject>Myocardium - cytology</subject><subject>Myocardium - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>RNA, Messenger - analysis</subject><subject>RNA, Messenger - biosynthesis</subject><subject>Temperature</subject><subject>Time Factors</subject><issn>0300-8177</issn><issn>1573-4919</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</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>eNpd0E1LxDAQBuAgyrqunj0JxYO3aiZNm8SbLH7Bghc9SkmTKdu1bdYkBddfb8Q9eRoGHl7eGULOgV4DZcXN3S1QWknOAXjB5QGZQymKnCtQh2ROC0pzCUIck5MQNpQmDDAjM8WEZFU1J-_LtfbaRPTdt46dGzPXZsb1Nu9GOxm02Rp1zMLamY9s613Ebszwa-sxhF-dthHdqKPuM5-g0d52btg5s4sYTslRq_uAZ_u5IG8P96_Lp3z18vi8vFvlhgkV8xIaqDg2qmwryZpStaxtmJRoLW8k1yC5SgehZko2pVDacGOBIRhMBGmxIFd_uanh54Qh1kMXDPa9TuWmUAvFKkYFS_DyH9y4yY-pWy3KigEtFU_oYo-mZkBbb303aL-r908rfgBCTG-R</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Laios, E</creator><creator>Rebeyka, I M</creator><creator>Prody, C A</creator><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>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>19970801</creationdate><title>Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes</title><author>Laios, E ; Rebeyka, I M ; Prody, C A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c279t-51b164eb95f682b59f2fb288edd4b84a1849919ea298b579ac4cd12e1ceedde03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Animals, Newborn - metabolism</topic><topic>Bacteria</topic><topic>Cardiomyocytes</topic><topic>Cold Temperature</topic><topic>Heat shock proteins</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>HSP70 Heat-Shock Proteins - biosynthesis</topic><topic>HSP90 Heat-Shock Proteins - biosynthesis</topic><topic>Hypothermia</topic><topic>Hypothermia - physiopathology</topic><topic>Myocardium - cytology</topic><topic>Myocardium - metabolism</topic><topic>Proteins</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>RNA, Messenger - analysis</topic><topic>RNA, Messenger - biosynthesis</topic><topic>Temperature</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Laios, E</creatorcontrib><creatorcontrib>Rebeyka, I M</creatorcontrib><creatorcontrib>Prody, C A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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>Laios, E</au><au>Rebeyka, I M</au><au>Prody, C A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes</atitle><jtitle>Molecular and cellular biochemistry</jtitle><addtitle>Mol Cell Biochem</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>173</volume><issue>1-2</issue><spage>153</spage><epage>159</epage><pages>153-159</pages><issn>0300-8177</issn><eissn>1573-4919</eissn><abstract>Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. Our results indicate that hypothermia is capable of inducing the heat shock response in neonatal cardiomyocytes.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>9278266</pmid><doi>10.1023/A:1006844114348</doi><tpages>7</tpages></addata></record> |
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subjects | Animals Animals, Newborn - metabolism Bacteria Cardiomyocytes Cold Temperature Heat shock proteins Heat-Shock Proteins - biosynthesis HSP70 Heat-Shock Proteins - biosynthesis HSP90 Heat-Shock Proteins - biosynthesis Hypothermia Hypothermia - physiopathology Myocardium - cytology Myocardium - metabolism Proteins Rats Rats, Wistar RNA, Messenger - analysis RNA, Messenger - biosynthesis Temperature Time Factors |
title | Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes |
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