Elevated core and muscle temperature to levels comparable to exercise do not increase heat shock protein content of skeletal muscle of physically active men.

Saved in:
Bibliographic Details
Title: Elevated core and muscle temperature to levels comparable to exercise do not increase heat shock protein content of skeletal muscle of physically active men.
Authors: Morton, J. P., MacLaren, D. P. M., Cable, N. T., Campbell, I. T., Evans, L., Bongers, T., Griffiths, R. D., Kayani, A. C., McArdle, A., Drust, B.
Source: Acta Physiologica. Aug2007, Vol. 190 Issue 4, p319-327. 9p. 4 Graphs.
Subjects: Muscles, Heat shock proteins, Body temperature, Physiological effects of heat, Men, Oxidative stress, Superoxide dismutase, Molecular chaperones
Abstract: Aim: Exercise-associated hyperthermia is routinely cited as the signal responsible for inducing an increased production of heat shock proteins (HSPs) following exercise. This hypothesis, however, has not been tested in human skeletal muscle. The aim of the present study was to therefore investigate the role of increased muscle and core temperature in contributing to the exercise-induced production of the major HSP families in human skeletal muscle. Methods: Seven physically active males underwent a passive heating protocol of 1 h duration during which the temperature of the core and vastus lateralis muscle were increased to similar levels to those typically occurring during moderately demanding aerobic exercise protocols. One limb was immersed in a tank containing water maintained at approximately 45 °C whilst the contra-lateral limb remained outside the tank and was not exposed to heat stress. Muscle biopsies were obtained from the vastus lateralis of both legs immediately prior to and at 48 h and 7 days post-heating. Results: The heating protocol induced significant increases ( P < 0.05) in rectal (1.5 ± 0.2 °C) and muscle temperature of the heated leg (3.6 ± 0.5 °C). Muscle temperature of the non-heated limb showed no significant change ( P > 0.05) following heating (pre: 36.1 ± 0.5, post: 35.7 ± 0.2 °C). Heating failed to induce a significant increase ( P > 0.05) in muscle content of HSP70, HSC70, HSP60, HSP27, αB-crystallin, MnSOD protein content or in the activity of superoxide dismutase and catalase. Conclusions: These data demonstrate that increases in both systemic and local muscle temperature per se do not appear to mediate the exercise-induced production of HSPs in human skeletal muscle and suggest that non-heat stress factors associated with contractile activity are of more importance in mediating this response. [ABSTRACT FROM AUTHOR]
Copyright of Acta Physiologica is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: pbh
DbLabel: Psychology and Behavioral Sciences Collection
An: 25736546
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Elevated core and muscle temperature to levels comparable to exercise do not increase heat shock protein content of skeletal muscle of physically active men.
– Name: Author
  Label: Authors
  Group: Au
  Data: &lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Morton%2C+J%2E+P%2E%22&quot;&gt;Morton, J. P.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22MacLaren%2C+D%2E+P%2E+M%2E%22&quot;&gt;MacLaren, D. P. M.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Cable%2C+N%2E+T%2E%22&quot;&gt;Cable, N. T.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Campbell%2C+I%2E+T%2E%22&quot;&gt;Campbell, I. T.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Evans%2C+L%2E%22&quot;&gt;Evans, L.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Bongers%2C+T%2E%22&quot;&gt;Bongers, T.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Griffiths%2C+R%2E+D%2E%22&quot;&gt;Griffiths, R. D.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Kayani%2C+A%2E+C%2E%22&quot;&gt;Kayani, A. C.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22McArdle%2C+A%2E%22&quot;&gt;McArdle, A.&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;AR&quot; term=&quot;%22Drust%2C+B%2E%22&quot;&gt;Drust, B.&lt;/searchLink&gt;
– Name: TitleSource
  Label: Source
  Group: Src
  Data: &lt;searchLink fieldCode=&quot;JN&quot; term=&quot;%22Acta+Physiologica%22&quot;&gt;Acta Physiologica&lt;/searchLink&gt;. Aug2007, Vol. 190 Issue 4, p319-327. 9p. 4 Graphs.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: &lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Muscles%22&quot;&gt;Muscles&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Heat+shock+proteins%22&quot;&gt;Heat shock proteins&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Body+temperature%22&quot;&gt;Body temperature&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Physiological+effects+of+heat%22&quot;&gt;Physiological effects of heat&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Men%22&quot;&gt;Men&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Oxidative+stress%22&quot;&gt;Oxidative stress&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Superoxide+dismutase%22&quot;&gt;Superoxide dismutase&lt;/searchLink&gt;&lt;br /&gt;&lt;searchLink fieldCode=&quot;DE&quot; term=&quot;%22Molecular+chaperones%22&quot;&gt;Molecular chaperones&lt;/searchLink&gt;
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Aim: Exercise-associated hyperthermia is routinely cited as the signal responsible for inducing an increased production of heat shock proteins (HSPs) following exercise. This hypothesis, however, has not been tested in human skeletal muscle. The aim of the present study was to therefore investigate the role of increased muscle and core temperature in contributing to the exercise-induced production of the major HSP families in human skeletal muscle. Methods: Seven physically active males underwent a passive heating protocol of 1 h duration during which the temperature of the core and vastus lateralis muscle were increased to similar levels to those typically occurring during moderately demanding aerobic exercise protocols. One limb was immersed in a tank containing water maintained at approximately 45 &#176;C whilst the contra-lateral limb remained outside the tank and was not exposed to heat stress. Muscle biopsies were obtained from the vastus lateralis of both legs immediately prior to and at 48 h and 7 days post-heating. Results: The heating protocol induced significant increases ( P &lt; 0.05) in rectal (1.5 &#177; 0.2 &#176;C) and muscle temperature of the heated leg (3.6 &#177; 0.5 &#176;C). Muscle temperature of the non-heated limb showed no significant change ( P &gt; 0.05) following heating (pre: 36.1 &#177; 0.5, post: 35.7 &#177; 0.2 &#176;C). Heating failed to induce a significant increase ( P &gt; 0.05) in muscle content of HSP70, HSC70, HSP60, HSP27, αB-crystallin, MnSOD protein content or in the activity of superoxide dismutase and catalase. Conclusions: These data demonstrate that increases in both systemic and local muscle temperature per se do not appear to mediate the exercise-induced production of HSPs in human skeletal muscle and suggest that non-heat stress factors associated with contractile activity are of more importance in mediating this response. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: &lt;i&gt;Copyright of Acta Physiologica is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder&#39;s express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.&lt;/i&gt; (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=25736546
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1111/j.1748-1716.2007.01711.x
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 9
        StartPage: 319
    Subjects:
      – SubjectFull: Muscles
        Type: general
      – SubjectFull: Heat shock proteins
        Type: general
      – SubjectFull: Body temperature
        Type: general
      – SubjectFull: Physiological effects of heat
        Type: general
      – SubjectFull: Men
        Type: general
      – SubjectFull: Oxidative stress
        Type: general
      – SubjectFull: Superoxide dismutase
        Type: general
      – SubjectFull: Molecular chaperones
        Type: general
    Titles:
      – TitleFull: Elevated core and muscle temperature to levels comparable to exercise do not increase heat shock protein content of skeletal muscle of physically active men.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Morton, J. P.
      – PersonEntity:
          Name:
            NameFull: MacLaren, D. P. M.
      – PersonEntity:
          Name:
            NameFull: Cable, N. T.
      – PersonEntity:
          Name:
            NameFull: Campbell, I. T.
      – PersonEntity:
          Name:
            NameFull: Evans, L.
      – PersonEntity:
          Name:
            NameFull: Bongers, T.
      – PersonEntity:
          Name:
            NameFull: Griffiths, R. D.
      – PersonEntity:
          Name:
            NameFull: Kayani, A. C.
      – PersonEntity:
          Name:
            NameFull: McArdle, A.
      – PersonEntity:
          Name:
            NameFull: Drust, B.
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 08
              Text: Aug2007
              Type: published
              Y: 2007
          Identifiers:
            – Type: issn-print
              Value: 17481708
          Numbering:
            – Type: volume
              Value: 190
            – Type: issue
              Value: 4
          Titles:
            – TitleFull: Acta Physiologica
              Type: main
ResultId 1