Heat shock proteins: Endogenous modulators of apoptotic cell death

Citation
C. Garrido et al., Heat shock proteins: Endogenous modulators of apoptotic cell death, BIOC BIOP R, 286(3), 2001, pp. 433-442
Citations number
93
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
286
Issue
3
Year of publication
2001
Pages
433 - 442
Database
ISI
SICI code
0006-291X(20010824)286:3<433:HSPEMO>2.0.ZU;2-1
Abstract
The highly conserved heat shock proteins (HSPs) accumulate in cells exposed to heat and a variety of other stressful stimuli. HSPs, which function mai nly as molecular chaperones, allow cells to adapt to gradual changes in the ir environment and to survive in otherwise lethal conditions. The events of cell stress and cell death are linked and HSPs induced in response to stre ss appear to function at key regulatory points in the control of apoptosis. HSPs include anti-apoptotic and proapoptotic proteins that interact with a variety of cellular proteins. Their expression level can determine the fat e of the cell in response to a death stimulus, and apoptosis-inhibitory HSP s, in particular HSP27 and HSP70, may participate in carcinogenesis. This r eview summarizes apoptosis-regulatory function of HSPs. (C) 2001 Academic P ress.