Heat stress inhibits skeletal muscle hypertrophy
Heat shock proteins (Hsps) are molecular chaperones that aid in protein synthesis and trafficking and have been shown to protect cells/tissues from various protein damaging stressors. To determine the extent to which a single heat stress and the concurrent accumulation of Hsps influences the early e...
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Veröffentlicht in: | Cell stress & chaperones 2007-06, Vol.12 (2), p.132-141 |
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description | Heat shock proteins (Hsps) are molecular chaperones that aid in protein synthesis and trafficking and have been shown to protect cells/tissues from various protein damaging stressors. To determine the extent to which a single heat stress and the concurrent accumulation of Hsps influences the early events of skeletal muscle hypertrophy, Sprague-Dawley rats were heat stressed (42°C, 15 minutes) 24 hours prior to overloading 1 plantaris muscle by surgical removal of the gastrocnemius muscle. The contralateral plantaris muscles served as controls. Heat-stressed and/or overloaded plantaris muscles were assessed for muscle mass, total muscle protein, muscle protein concentration, Type I myosin heavy chain (Type I MHC) content, as well as Hsp72 and Hsp25 content over the course of 7 days following removal of the gastrocnemius muscle. As expected, in non–heat-stressed animals, muscle mass, total muscle protein and MHC I content were significantly increased (P < 0.05) following overload. In addition, Hsp25 and Hsp72 increased significantly after 2 and 3 days of overload, respectively. A prior heat stress–elevated Hsp25 content to levels similar to those measured following overload alone, but heat stress–induced Hsp72 content was increased significantly greater than was elicited by overload alone. Moreover, overloaded muscles from animals that experienced a prior heat stress showed a lower muscle mass increase at 5 and 7 days; a reduced total muscle protein elevation at 3, 5, and 7 days; reduced protein concentration; and a diminished Type I MHC content accumulation at 3, 5, and 7 days relative to non– heat-stressed animals. These data suggest that a prior heat stress and/or the consequent accumulation of Hsps may inhibit increases in muscle mass, total muscle protein content, and Type I MHC in muscles undergoing hypertrophy. |
doi_str_mv | 10.1379/CSC-233R.1 |
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To determine the extent to which a single heat stress and the concurrent accumulation of Hsps influences the early events of skeletal muscle hypertrophy, Sprague-Dawley rats were heat stressed (42°C, 15 minutes) 24 hours prior to overloading 1 plantaris muscle by surgical removal of the gastrocnemius muscle. The contralateral plantaris muscles served as controls. Heat-stressed and/or overloaded plantaris muscles were assessed for muscle mass, total muscle protein, muscle protein concentration, Type I myosin heavy chain (Type I MHC) content, as well as Hsp72 and Hsp25 content over the course of 7 days following removal of the gastrocnemius muscle. As expected, in non–heat-stressed animals, muscle mass, total muscle protein and MHC I content were significantly increased (P < 0.05) following overload. In addition, Hsp25 and Hsp72 increased significantly after 2 and 3 days of overload, respectively. A prior heat stress–elevated Hsp25 content to levels similar to those measured following overload alone, but heat stress–induced Hsp72 content was increased significantly greater than was elicited by overload alone. Moreover, overloaded muscles from animals that experienced a prior heat stress showed a lower muscle mass increase at 5 and 7 days; a reduced total muscle protein elevation at 3, 5, and 7 days; reduced protein concentration; and a diminished Type I MHC content accumulation at 3, 5, and 7 days relative to non– heat-stressed animals. These data suggest that a prior heat stress and/or the consequent accumulation of Hsps may inhibit increases in muscle mass, total muscle protein content, and Type I MHC in muscles undergoing hypertrophy.</description><identifier>ISSN: 1355-8145</identifier><identifier>EISSN: 1466-1268</identifier><identifier>DOI: 10.1379/CSC-233R.1</identifier><identifier>PMID: 17688192</identifier><language>eng</language><publisher>Netherlands: Churchill Livingstone</publisher><subject>Animal physiology ; Animals ; Body Temperature ; Body Weight ; Gels ; Heat stress disorders ; Heat-Shock Proteins - metabolism ; Histocompatibility Antigens Class I - metabolism ; Homogenization ; HSP27 Heat-Shock Proteins ; HSP72 Heat-Shock Proteins - metabolism ; Hyperthermia, Induced ; Hypertrophy ; Male ; Muscle fibers ; Muscle proteins ; Muscle, Skeletal - pathology ; Muscles ; Neoplasm Proteins - metabolism ; Organ Size ; Original ; Original s ; Rats ; Rats, Sprague-Dawley ; Skeletal muscle ; Transcriptional regulatory elements</subject><ispartof>Cell stress & chaperones, 2007-06, Vol.12 (2), p.132-141</ispartof><rights>Cell Stress Society International</rights><rights>Copyright 2007 Cell Stress Society International</rights><rights>Copyright Alliance Communications Group, A Division of Allen Press, Inc. Summer 2007</rights><rights>Copyright © 2007, Cell Stress Society International 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b457t-91ffe949db8e071108edc5ed344e1998e1b7e3ca605af469d3f69b7aecef62ee3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://bioone.org/doi/pdf/10.1379/CSC-233R.1$$EPDF$$P50$$Gbioone$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4539759$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,26978,27924,27925,52363,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17688192$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Frier, Bruce C.</creatorcontrib><creatorcontrib>Locke, Marius</creatorcontrib><title>Heat stress inhibits skeletal muscle hypertrophy</title><title>Cell stress & chaperones</title><addtitle>Cell Stress Chaperones</addtitle><description>Heat shock proteins (Hsps) are molecular chaperones that aid in protein synthesis and trafficking and have been shown to protect cells/tissues from various protein damaging stressors. To determine the extent to which a single heat stress and the concurrent accumulation of Hsps influences the early events of skeletal muscle hypertrophy, Sprague-Dawley rats were heat stressed (42°C, 15 minutes) 24 hours prior to overloading 1 plantaris muscle by surgical removal of the gastrocnemius muscle. The contralateral plantaris muscles served as controls. Heat-stressed and/or overloaded plantaris muscles were assessed for muscle mass, total muscle protein, muscle protein concentration, Type I myosin heavy chain (Type I MHC) content, as well as Hsp72 and Hsp25 content over the course of 7 days following removal of the gastrocnemius muscle. As expected, in non–heat-stressed animals, muscle mass, total muscle protein and MHC I content were significantly increased (P < 0.05) following overload. In addition, Hsp25 and Hsp72 increased significantly after 2 and 3 days of overload, respectively. A prior heat stress–elevated Hsp25 content to levels similar to those measured following overload alone, but heat stress–induced Hsp72 content was increased significantly greater than was elicited by overload alone. Moreover, overloaded muscles from animals that experienced a prior heat stress showed a lower muscle mass increase at 5 and 7 days; a reduced total muscle protein elevation at 3, 5, and 7 days; reduced protein concentration; and a diminished Type I MHC content accumulation at 3, 5, and 7 days relative to non– heat-stressed animals. These data suggest that a prior heat stress and/or the consequent accumulation of Hsps may inhibit increases in muscle mass, total muscle protein content, and Type I MHC in muscles undergoing hypertrophy.</description><subject>Animal physiology</subject><subject>Animals</subject><subject>Body Temperature</subject><subject>Body Weight</subject><subject>Gels</subject><subject>Heat stress disorders</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Histocompatibility Antigens Class I - metabolism</subject><subject>Homogenization</subject><subject>HSP27 Heat-Shock Proteins</subject><subject>HSP72 Heat-Shock Proteins - metabolism</subject><subject>Hyperthermia, Induced</subject><subject>Hypertrophy</subject><subject>Male</subject><subject>Muscle fibers</subject><subject>Muscle proteins</subject><subject>Muscle, Skeletal - pathology</subject><subject>Muscles</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Organ Size</subject><subject>Original</subject><subject>Original s</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Skeletal muscle</subject><subject>Transcriptional regulatory elements</subject><issn>1355-8145</issn><issn>1466-1268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</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>eNp9kctLAzEQxoMoVqsXzyKLBxFha2azm2wughRfUBB8nEN2O2u3bjc1yQr9701pqY-DpyR8v8x8Mx8hR0AHwIS8HD4P44SxpwFskT1IOY8h4fl2uLMsi3NIsx7Zd25KKRVCwC7pgeB5DjLZI_QetY-ct-hcVLeTuqi9i9w7Nuh1E806VzYYTRZztN6a-WRxQHYq3Tg8XJ998np78zK8j0ePdw_D61FcpJnwsYSqQpnKcZEjFQA0x3GZ4ZilKYKUOUIhkJWa00xXKZdjVnFZCI0lVjxBZH1ytao774pZ-Iutt7pRc1vPtF0oo2v1W2nriXoznwpCV8aSUOBsXcCajw6dV7Paldg0ukXTOcWXi0kgD-DpH3BqOtuG4VQClAbrbAldrKDSGucsVhsnQNUyBRVSUMsUwqtPTn56_0bXaw_A8QqYOm_sRk8zJkUmg3y-kovamBb_a_UFiReZ6Q</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Frier, Bruce C.</creator><creator>Locke, Marius</creator><general>Churchill Livingstone</general><general>Springer Nature B.V</general><general>Cell Stress Society International</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>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</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>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070601</creationdate><title>Heat stress inhibits skeletal muscle hypertrophy</title><author>Frier, Bruce C. ; Locke, Marius</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b457t-91ffe949db8e071108edc5ed344e1998e1b7e3ca605af469d3f69b7aecef62ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animal physiology</topic><topic>Animals</topic><topic>Body Temperature</topic><topic>Body Weight</topic><topic>Gels</topic><topic>Heat stress disorders</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Histocompatibility Antigens Class I - metabolism</topic><topic>Homogenization</topic><topic>HSP27 Heat-Shock Proteins</topic><topic>HSP72 Heat-Shock Proteins - metabolism</topic><topic>Hyperthermia, Induced</topic><topic>Hypertrophy</topic><topic>Male</topic><topic>Muscle fibers</topic><topic>Muscle proteins</topic><topic>Muscle, Skeletal - pathology</topic><topic>Muscles</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Organ Size</topic><topic>Original</topic><topic>Original s</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Skeletal muscle</topic><topic>Transcriptional regulatory elements</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Frier, Bruce C.</creatorcontrib><creatorcontrib>Locke, Marius</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids 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>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>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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell stress & chaperones</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Frier, Bruce C.</au><au>Locke, Marius</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat stress inhibits skeletal muscle hypertrophy</atitle><jtitle>Cell stress & chaperones</jtitle><addtitle>Cell Stress Chaperones</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>12</volume><issue>2</issue><spage>132</spage><epage>141</epage><pages>132-141</pages><issn>1355-8145</issn><eissn>1466-1268</eissn><abstract>Heat shock proteins (Hsps) are molecular chaperones that aid in protein synthesis and trafficking and have been shown to protect cells/tissues from various protein damaging stressors. To determine the extent to which a single heat stress and the concurrent accumulation of Hsps influences the early events of skeletal muscle hypertrophy, Sprague-Dawley rats were heat stressed (42°C, 15 minutes) 24 hours prior to overloading 1 plantaris muscle by surgical removal of the gastrocnemius muscle. The contralateral plantaris muscles served as controls. Heat-stressed and/or overloaded plantaris muscles were assessed for muscle mass, total muscle protein, muscle protein concentration, Type I myosin heavy chain (Type I MHC) content, as well as Hsp72 and Hsp25 content over the course of 7 days following removal of the gastrocnemius muscle. As expected, in non–heat-stressed animals, muscle mass, total muscle protein and MHC I content were significantly increased (P < 0.05) following overload. In addition, Hsp25 and Hsp72 increased significantly after 2 and 3 days of overload, respectively. A prior heat stress–elevated Hsp25 content to levels similar to those measured following overload alone, but heat stress–induced Hsp72 content was increased significantly greater than was elicited by overload alone. Moreover, overloaded muscles from animals that experienced a prior heat stress showed a lower muscle mass increase at 5 and 7 days; a reduced total muscle protein elevation at 3, 5, and 7 days; reduced protein concentration; and a diminished Type I MHC content accumulation at 3, 5, and 7 days relative to non– heat-stressed animals. These data suggest that a prior heat stress and/or the consequent accumulation of Hsps may inhibit increases in muscle mass, total muscle protein content, and Type I MHC in muscles undergoing hypertrophy.</abstract><cop>Netherlands</cop><pub>Churchill Livingstone</pub><pmid>17688192</pmid><doi>10.1379/CSC-233R.1</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animal physiology Animals Body Temperature Body Weight Gels Heat stress disorders Heat-Shock Proteins - metabolism Histocompatibility Antigens Class I - metabolism Homogenization HSP27 Heat-Shock Proteins HSP72 Heat-Shock Proteins - metabolism Hyperthermia, Induced Hypertrophy Male Muscle fibers Muscle proteins Muscle, Skeletal - pathology Muscles Neoplasm Proteins - metabolism Organ Size Original Original s Rats Rats, Sprague-Dawley Skeletal muscle Transcriptional regulatory elements |
title | Heat stress inhibits skeletal muscle hypertrophy |
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