Heat shock proteins: endogenous modulators of apoptotic cell death

Biochem Biophys Res Commun. 2001 Aug 24;286(3):433-42. doi: 10.1006/bbrc.2001.5427.


The highly conserved heat shock proteins (HSPs) accumulate in cells exposed to heat and a variety of other stressful stimuli. HSPs, which function mainly as molecular chaperones, allow cells to adapt to gradual changes in their environment and to survive in otherwise lethal conditions. The events of cell stress and cell death are linked and HSPs induced in response to stress appear to function at key regulatory points in the control of apoptosis. HSPs include antiapoptotic and proapoptotic proteins that interact with a variety of cellular proteins. Their expression level can determine the fate of the cell in response to a death stimulus, and apoptosis-inhibitory HSPs, in particular HSP27 and HSP70, may participate in carcinogenesis. This review summarizes apoptosis-regulatory function of HSPs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Apoptosis*
  • Chaperonin 60 / physiology
  • HSP70 Heat-Shock Proteins / physiology
  • HSP90 Heat-Shock Proteins / physiology
  • Heat-Shock Proteins / physiology*
  • Models, Biological
  • Molecular Chaperones / physiology
  • Neoplasms / metabolism
  • Neoplasms / pathology
  • Stress, Physiological / metabolism


  • Chaperonin 60
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones