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.
abstract: OBJECTIVE
  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 degrees 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 degrees C) and muscle temperature of the heated leg (3.6 +/- 0.5 degrees 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 degrees C). Heating failed to induce a significant increase (P > 0.05) in muscle content of HSP70, HSC70, HSP60, HSP27, alphaB-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.
authors.affiliation: Research Institute for Sport and Exercise Sciences, Liverpool John Moores University, Liverpool, UK. j.p.morton@ljmu.ac.uk
authors.forename: J P
authors.initials: JP
authors.lastname: Morton
authors.forename: D P M
authors.initials: DP
authors.lastname: Maclaren
authors.forename: N T
authors.initials: NT
authors.lastname: Cable
authors.forename: I T
authors.initials: IT
authors.lastname: Campbell
authors.forename: L
authors.initials: L
authors.lastname: Evans
authors.forename: T
authors.initials: T
authors.lastname: Bongers
authors.forename: R D
authors.initials: RD
authors.lastname: Griffiths
authors.forename: A C
authors.initials: AC
authors.lastname: Kayani
authors.forename: A
authors.initials: A
authors.lastname: McArdle
authors.forename: B
authors.initials: B
authors.lastname: Drust
mesh_terms: D000328:Adult; D001706:Biopsy; D001831:Body Temperature / Q000502:physiology*; D001833:Body Temperature Regulation / Q000502:physiology; D002374:Catalase / Q000378:metabolism; D015444:Exercise / Q000502:physiology*; D006339:Heart Rate / Q000502:physiology; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006361:Heating; D006801:Humans; D006979:Hyperthermia, Induced; D008297:Male; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000473:pathology; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D006360:Heat-Shock Proteins; D002374:Catalase; D013482:Superoxide Dismutase