Heat shock proteins: Endogenous modulators of apoptotic cell death

Carmen Garrido, Sandeep Gurbuxani, Luigi Ravagnan, Guido Kroemer

Research output: Contribution to journalReview articlepeer-review

689 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)433-442
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume286
Issue number3
DOIs
Publication statusPublished - 1 Jan 2001
Externally publishedYes

Keywords

  • Apoptosis
  • Apoptosis-inducing factor
  • Cytochrome c
  • Heat shock proteins
  • Mitochondria

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