Constitutive Expression of HSP 72 in Swine Heart
Stress-induced regulation of the 72 kD heat shock protein (HSP 72), the major stress inducible protein in mammalian cells, is mediated by the activation and binding of a heat shock transcription factor (HSF) to a specific sequence in the 5′ region of the promoter termed the heat shock element (HSE)....
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Veröffentlicht in: | Journal of molecular and cellular cardiology 1996-03, Vol.28 (3), p.467-474 |
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creator | Locke, Marius Tanguay, Robert M. Ianuzzo, David C. |
description | Stress-induced regulation of the 72 kD heat shock protein (HSP 72), the major stress inducible protein in mammalian cells, is mediated by the activation and binding of a heat shock transcription factor (HSF) to a specific sequence in the 5′ region of the promoter termed the heat shock element (HSE). In agreement with this regulation, HSP 72 is absent in most cells under unstressed conditions but is rapidly synthesized following exposure to protein damaging stressors. An exception is the skeletal muscle, where HSP 72 is constitutively expressed in muscles that express the beta myosin heavy chain (β-MHC) protein. Since β-MHC is also expressed in the ventricles of large mammals, we have examined if HSP 72 was also constitutively expressed in β-MHC positive hearts. Chambers of the heart muscle from Yorkshire swine were examined for α-MHC, β-MHC and HSP 72 content. HSF:HSE activation was also assessed by gel shift analyses. In the swine heart, atria and ventricles differed in their α-MHC and β-MHC protein content but all expressed a high HSP 72 content. Gel shift analyses demonstrated no HSF:HSE binding in extracts from unstressed swine hearts. These results indicate that HSP 72 is constitutively expressed in all portions of the swine heart and this expression may not be dependent on an HSF:HSE interaction. |
doi_str_mv | 10.1006/jmcc.1996.0043 |
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In agreement with this regulation, HSP 72 is absent in most cells under unstressed conditions but is rapidly synthesized following exposure to protein damaging stressors. An exception is the skeletal muscle, where HSP 72 is constitutively expressed in muscles that express the beta myosin heavy chain (β-MHC) protein. Since β-MHC is also expressed in the ventricles of large mammals, we have examined if HSP 72 was also constitutively expressed in β-MHC positive hearts. Chambers of the heart muscle from Yorkshire swine were examined for α-MHC, β-MHC and HSP 72 content. HSF:HSE activation was also assessed by gel shift analyses. In the swine heart, atria and ventricles differed in their α-MHC and β-MHC protein content but all expressed a high HSP 72 content. Gel shift analyses demonstrated no HSF:HSE binding in extracts from unstressed swine hearts. These results indicate that HSP 72 is constitutively expressed in all portions of the swine heart and this expression may not be dependent on an HSF:HSE interaction.</description><identifier>ISSN: 0022-2828</identifier><identifier>EISSN: 1095-8584</identifier><identifier>DOI: 10.1006/jmcc.1996.0043</identifier><identifier>PMID: 9011630</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Constitutive expression ; DNA-Binding Proteins - metabolism ; Female ; Gene Expression ; Heart ; Heat shock protein ; Heat shock transcription factor ; Heat Shock Transcription Factors ; Heat-Shock Proteins - biosynthesis ; Heat-Shock Proteins - genetics ; HSP72 Heat-Shock Proteins ; Male ; Myocardium - metabolism ; Myosin heavy chain ; Rats ; Rats, Sprague-Dawley ; Spleen - metabolism ; Swine ; Transcription Factors</subject><ispartof>Journal of molecular and cellular cardiology, 1996-03, Vol.28 (3), p.467-474</ispartof><rights>1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-2eb7d392d13856f93dc5211ca8cdfd17e5b6cd1007dcca000665595ff7c97fab3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022282896900437$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9011630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Locke, Marius</creatorcontrib><creatorcontrib>Tanguay, Robert M.</creatorcontrib><creatorcontrib>Ianuzzo, David C.</creatorcontrib><title>Constitutive Expression of HSP 72 in Swine Heart</title><title>Journal of molecular and cellular cardiology</title><addtitle>J Mol Cell Cardiol</addtitle><description>Stress-induced regulation of the 72 kD heat shock protein (HSP 72), the major stress inducible protein in mammalian cells, is mediated by the activation and binding of a heat shock transcription factor (HSF) to a specific sequence in the 5′ region of the promoter termed the heat shock element (HSE). In agreement with this regulation, HSP 72 is absent in most cells under unstressed conditions but is rapidly synthesized following exposure to protein damaging stressors. An exception is the skeletal muscle, where HSP 72 is constitutively expressed in muscles that express the beta myosin heavy chain (β-MHC) protein. Since β-MHC is also expressed in the ventricles of large mammals, we have examined if HSP 72 was also constitutively expressed in β-MHC positive hearts. Chambers of the heart muscle from Yorkshire swine were examined for α-MHC, β-MHC and HSP 72 content. HSF:HSE activation was also assessed by gel shift analyses. In the swine heart, atria and ventricles differed in their α-MHC and β-MHC protein content but all expressed a high HSP 72 content. Gel shift analyses demonstrated no HSF:HSE binding in extracts from unstressed swine hearts. These results indicate that HSP 72 is constitutively expressed in all portions of the swine heart and this expression may not be dependent on an HSF:HSE interaction.</description><subject>Animals</subject><subject>Constitutive expression</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Female</subject><subject>Gene Expression</subject><subject>Heart</subject><subject>Heat shock protein</subject><subject>Heat shock transcription factor</subject><subject>Heat Shock Transcription Factors</subject><subject>Heat-Shock Proteins - biosynthesis</subject><subject>Heat-Shock Proteins - genetics</subject><subject>HSP72 Heat-Shock Proteins</subject><subject>Male</subject><subject>Myocardium - metabolism</subject><subject>Myosin heavy chain</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Spleen - metabolism</subject><subject>Swine</subject><subject>Transcription Factors</subject><issn>0022-2828</issn><issn>1095-8584</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kM9LwzAUx4Moc06v3oSevLW-JEubHGVMJwwUpufQJi-QsbYzaaf-97ZsePP0Dt8fvO-HkFsKGQXIH7a1MRlVKs8A5vyMTCkokUoh5-dkCsBYyiSTl-Qqxi0AqDnnEzJRQGnOYUpg0Tax813f-QMmy-99wBh92yStS1abt6RgiW-SzZdvMFlhGbprcuHKXcSb052Rj6fl-2KVrl-fXxaP69RwrrqUYVVYrpilXIrcKW6NYJSaUhrrLC1QVLmxw4LCGlMOj-W5EEo4VxhVuLLiM3J_7N2H9rPH2OnaR4O7Xdlg20ddSMpgyA_G7Gg0oY0xoNP74Osy_GgKekSkR0R6RKRHREPg7tTcVzXaP_uJyaDLo47DvIPHoKPx2Bi0PqDptG39f9W_Ds1zkw</recordid><startdate>19960301</startdate><enddate>19960301</enddate><creator>Locke, Marius</creator><creator>Tanguay, Robert M.</creator><creator>Ianuzzo, David C.</creator><general>Elsevier Ltd</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>7X8</scope></search><sort><creationdate>19960301</creationdate><title>Constitutive Expression of HSP 72 in Swine Heart</title><author>Locke, Marius ; Tanguay, Robert M. ; Ianuzzo, David C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-2eb7d392d13856f93dc5211ca8cdfd17e5b6cd1007dcca000665595ff7c97fab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Constitutive expression</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Female</topic><topic>Gene Expression</topic><topic>Heart</topic><topic>Heat shock protein</topic><topic>Heat shock transcription factor</topic><topic>Heat Shock Transcription Factors</topic><topic>Heat-Shock Proteins - biosynthesis</topic><topic>Heat-Shock Proteins - genetics</topic><topic>HSP72 Heat-Shock Proteins</topic><topic>Male</topic><topic>Myocardium - metabolism</topic><topic>Myosin heavy chain</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Spleen - metabolism</topic><topic>Swine</topic><topic>Transcription Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Locke, Marius</creatorcontrib><creatorcontrib>Tanguay, Robert M.</creatorcontrib><creatorcontrib>Ianuzzo, David C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular and cellular cardiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Locke, Marius</au><au>Tanguay, Robert M.</au><au>Ianuzzo, David C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Constitutive Expression of HSP 72 in Swine Heart</atitle><jtitle>Journal of molecular and cellular cardiology</jtitle><addtitle>J Mol Cell Cardiol</addtitle><date>1996-03-01</date><risdate>1996</risdate><volume>28</volume><issue>3</issue><spage>467</spage><epage>474</epage><pages>467-474</pages><issn>0022-2828</issn><eissn>1095-8584</eissn><abstract>Stress-induced regulation of the 72 kD heat shock protein (HSP 72), the major stress inducible protein in mammalian cells, is mediated by the activation and binding of a heat shock transcription factor (HSF) to a specific sequence in the 5′ region of the promoter termed the heat shock element (HSE). In agreement with this regulation, HSP 72 is absent in most cells under unstressed conditions but is rapidly synthesized following exposure to protein damaging stressors. An exception is the skeletal muscle, where HSP 72 is constitutively expressed in muscles that express the beta myosin heavy chain (β-MHC) protein. Since β-MHC is also expressed in the ventricles of large mammals, we have examined if HSP 72 was also constitutively expressed in β-MHC positive hearts. Chambers of the heart muscle from Yorkshire swine were examined for α-MHC, β-MHC and HSP 72 content. HSF:HSE activation was also assessed by gel shift analyses. In the swine heart, atria and ventricles differed in their α-MHC and β-MHC protein content but all expressed a high HSP 72 content. Gel shift analyses demonstrated no HSF:HSE binding in extracts from unstressed swine hearts. These results indicate that HSP 72 is constitutively expressed in all portions of the swine heart and this expression may not be dependent on an HSF:HSE interaction.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>9011630</pmid><doi>10.1006/jmcc.1996.0043</doi><tpages>8</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Animals Constitutive expression DNA-Binding Proteins - metabolism Female Gene Expression Heart Heat shock protein Heat shock transcription factor Heat Shock Transcription Factors Heat-Shock Proteins - biosynthesis Heat-Shock Proteins - genetics HSP72 Heat-Shock Proteins Male Myocardium - metabolism Myosin heavy chain Rats Rats, Sprague-Dawley Spleen - metabolism Swine Transcription Factors |
title | Constitutive Expression of HSP 72 in Swine Heart |
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