title: Stress proteins: the exercise response.
abstract: A class of proteins that undergoes preferential synthesis following a variety of stressors has been demonstrated to carry out important cellular functions under both stressed and nonstressed conditions. These so-called heat shock (HSP) or stress (SP) proteins have been termed "molecular chaperones" and play important roles in cellular transportation, assembly/degradation, and cell survival. This review provides a basic introduction to the function and regulation of these proteins. Emphasis is placed on members of the HSP 70 family of proteins (especially HSP 72) and their role in cellular protection, their pattern of distribution in skeletal muscle, and changes in their expression following exercise and exercise training.
authors.affiliation: Deborah Research Institute, Browns Mills, NJ 08015-1799, USA.
authors.forename: M
authors.initials: M
authors.lastname: Locke
authors.forename: E G
authors.initials: EG
authors.lastname: Noble
mesh_terms: D000818:Animals; D015444:Exercise / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000502:physiology*; D006801:Humans; D018482:Muscle, Skeletal / Q000737:chemistry; D018384:Oxidative Stress / Q000502:physiology
chemical_list: D018840:HSP70 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins; D006360:Heat-Shock Proteins