Small heat shock proteins HSP27 and αB-crystallin: Cytoprotective and oncogenic functions

Arnaud Parcellier, Elise Schmitt, Mathilde Brunet, Arlette Hammann, Eric Solary, Carmen Garrido

    Résultats de recherche: Contribution à un journalArticle 'review'Revue par des pairs

    152 Citations (Scopus)

    Résumé

    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.

    langue originaleAnglais
    Pages (de - à)404-413
    Nombre de pages10
    journalAntioxidants and Redox Signaling
    Volume7
    Numéro de publication3-4
    Les DOIs
    étatPublié - 1 mars 2005

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