Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance.
Cells from virtually all organisms respond to a variety of stresses by the rapid synthesis of a highly conserved set of polypeptides termed heat shock proteins (HSPs). The precise functions of HSPs are unknown, but there is considerable evidence that these stress proteins are essential for survival at both normal and elevated temperatures. HSPs also appear to play a critical role in the development of thermotolerance and protection from cellular damage associated with stresses such as ischemia, cytokines, and energy depletion. These observations suggest that HSPs play an important role in both normal cellular homeostasis and the stress response. This mini-review examines recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging.
Kregel
Kevin C
KC
Integrative Physiology Laboratory, Department of Exercise Science, The University of Iowa, Iowa City 52242, USA. kevin-kregel@uiowa.edu
D000222:Adaptation, Physiological / Q000502:physiology; D000375:Aging / Q000502:physiology; D000818:Animals; D001833:Body Temperature Regulation / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology*; D018869:Heat-Shock Response; D006801:Humans; D015398:Signal Transduction / Q000502:physiology; D013312:Stress, Physiological / Q000503:physiopathology*
D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins