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
Hauptverfasser: Locke, Marius, Tanguay, Robert M., Ianuzzo, David C.
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container_title Journal of molecular and cellular cardiology
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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. 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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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