TY - JOUR
T1 - Small heat shock proteins HSP27 and αB-crystallin
T2 - Cytoprotective and oncogenic functions
AU - Parcellier, Arnaud
AU - Schmitt, Elise
AU - Brunet, Mathilde
AU - Hammann, Arlette
AU - Solary, Eric
AU - Garrido, Carmen
PY - 2005/3/1
Y1 - 2005/3/1
N2 - Heat shock protein-27 (HSP27) and αB-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 αB-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.
AB - Heat shock protein-27 (HSP27) and αB-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 αB-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.
UR - http://www.scopus.com/inward/record.url?scp=14044272999&partnerID=8YFLogxK
U2 - 10.1089/ars.2005.7.404
DO - 10.1089/ars.2005.7.404
M3 - Review article
C2 - 15706087
AN - SCOPUS:14044272999
SN - 1523-0864
VL - 7
SP - 404
EP - 413
JO - Antioxidants and Redox Signaling
JF - Antioxidants and Redox Signaling
IS - 3-4
ER -