Heat shock proteins: endogenous modulators of apoptotic cell death.
Fiche publication
Date publication
janvier 2006
Auteurs
Membres identifiés du Cancéropôle Est :
Dr GARRIDO Carmen, Dr MIRJOLET Céline
Tous les auteurs :
Didelot C, Schmitt E, Brunet M, Maingret L, Parcellier A, Garrido C
Lien Pubmed
Résumé
The highly conserved heat shock proteins (Hsps) accumulate in cells exposed to heat and a variety of other stressful stimuli. Hsps, that 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 anti-apoptotic and pro-apoptotic proteins that interact with a variety of cellular proteins involved in apoptosis. 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 the apoptosis-regulatory function of Hsps.
Référence
Handb Exp Pharmacol. 2006;(172):171-98.