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Heat shock proteins, cellular chaperones that modulate mitochondrial cell death pathways

Authors :
Carmen Garrido
Elise Schmitt
Sandeep Gurbuxani
Arnaud Parcellier
Eric Solary
Source :
Biochemical and Biophysical Research Communications. 304:505-512
Publication Year :
2003
Publisher :
Elsevier BV, 2003.

Abstract

Stress or heat shock proteins (HSPs) are ubiquitous and highly conserved proteins whose expression is induced in response to a wide variety of physiological and environmental insults. They allow the cells to survive to otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of HSPs. These proteins play an essential role in intracellular "house-keeping" by assisting the correct folding of nascent and stress-accumulated misfolded proteins and preventing their aggregation. Several HSPs have also demonstrated to directly interact with various components of the tightly regulated programmed cell death machinery, upstream, and downstream of the mitochondrial events. Finally, HSPs could play a role in the proteasome-mediated degradation of selected proteins under stress conditions. Altogether, these properties could make HSPs appropriate targets for modulating cell death pathways.

Details

ISSN :
0006291X
Volume :
304
Database :
OpenAIRE
Journal :
Biochemical and Biophysical Research Communications
Accession number :
edsair.doi.dedup.....044dc04be7036ac55fb1e25788896b18
Full Text :
https://doi.org/10.1016/s0006-291x(03)00623-5