Author: ["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"]
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Abstract
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.Cite this article
Bruey, JM., Ducasse, C., Bonniaud, P. et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2, 645–652 (2000). https://doi.org/10.1038/35023595 