Small heat shock proteins HSP27 and alphaB-crystallin: cytoprotective and oncogenic functions.
Heat shock protein-27 (HSP27) and alphaB-crystallin are ubiquitous small heat shock proteins whose expression is induced in response to a wide variety of physiological and environmental insults. They allow the cells to survive in otherwise lethal conditions. Various mechanisms have been proposed to account for the cytoprotective functions of these small heat shock proteins. First, these proteins are powerful molecular chaperones whose main function is to prevent the aggregation of nascent and stress-accumulated misfolded proteins. Second, they interact directly with various components of the tightly regulated programmed cell death machinery, upstream and downstream of the mitochondrial events. Third, they appear to play a role in the proteasome-mediated degradation of selected proteins. Both HSP27 and alphaB-crystallin were also proposed to participate in the development of neurodegenerative diseases and malignant tumors in which their overexpression could induce drug resistance. Altogether, these properties suggest that these small heat shock proteins are appropriate targets for modulating cell death pathways.
Parcellier
Arnaud
A
INSERM U-517, IFR-100, Faculty of Medicine and Pharmacy, 7 boulevard Jeanne d'Arc, 21033 Dijon, France.
Schmitt
Elise
E
Brunet
Mathilde
M
Hammann
Arlette
A
Solary
Eric
E
Garrido
Carmen
C
D017209:Apoptosis; D002470:Cell Survival; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D009369:Neoplasms / Q000209:etiology*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D038203:alpha-Crystallin B Chain / Q000502:physiology*
D006360:Heat-Shock Proteins; D038203:alpha-Crystallin B Chain; D046988:Proteasome Endopeptidase Complex