Hsp27 negatively regulates cell death by interacting with cytochrome c

Jean Marie Bruey, Cécile Ducasse, Philippe Bonniaud, Luigi Ravagnan, Santos A. Susin, Chantal Diaz-Latoud, Sandeep Gurbuxani, André Patrick Arrigo, Guido Kroemer, Eric Solary, Carmen Garrido

    Résultats de recherche: Contribution à un journalArticleRevue par des pairs

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    Résumé

    Mammalian cells respond to stress by accumulating or activating a set of highly conserved proteins known as heat-shock proteins (HSPs). Several of these proteins interfere negatively with apoptosis. We show that the small HSP known as Hsp27 inhibits cytochrome-c-mediated activation of caspases in the cytosol. Hsp27 does not interfere with granzyme-B-induced activation of caspases, nor with apoptosis-inducing factor-mediated, caspase-independent, nuclear changes. Hsp27 binds to cytochrome c released from the mitochondria to the cytosol and prevents cytochrome-c-mediated interaction of Apaf-1 with procaspase-9. Thus, Hsp27 interferes specifically with the mitochondrial pathway of caspase-dependent cell death.

    langue originaleAnglais
    Pages (de - à)645-652
    Nombre de pages8
    journalNature Cell Biology
    Volume2
    Numéro de publication9
    Les DOIs
    étatPublié - 1 sept. 2000

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