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2000:
Bruey J M; Ducasse C; Bonniaud P; Ravagnan L; Susin S A; Diaz-Latoud C; Gurbuxani S; Arrigo A P; Kroemer G; Solary E; Garrido C
Hsp27 negatively regulates cell death by interacting with cytochrome c.
Nature cell biology 2000;
2(
9):.
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.
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