@article{8726c543100c44839a991014575f4db8,
title = "Hsp27 negatively regulates cell death by interacting with cytochrome c",
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.",
author = "Bruey, \{Jean Marie\} and C{\'e}cile Ducasse and Philippe Bonniaud and Luigi Ravagnan and Susin, \{Santos A.\} and Chantal Diaz-Latoud and Sandeep Gurbuxani and Arrigo, \{Andr{\'e} Patrick\} and Guido Kroemer and Eric Solary and Carmen Garrido",
note = "Funding Information: ACKNOWLEDGEMENTS The authors wish to thank Elisabeth Bates, Olivier Sordet and C{\'e}dric R{\'e}b{\'e} for technical help, and Alena Pance and Kathryn Nason-Burchenal for helpful advices. This work was supported by grants from INSERM, Conseil R{\'e}gional de Bourgogne, ARC (6515 and 5204), Comit{\'e}s de C{\^o}te d{\textquoteright}Or, Sa{\^o}ne et Loire, Ni{\`e}vre de la Ligue Nationale Contre le Cancer et ARERS (E.S.), as well as special grants from the Ligue Nationale contre le Cancer (G.K. and E.S.).",
year = "2000",
month = sep,
day = "1",
doi = "10.1038/35023595",
language = "English",
volume = "2",
pages = "645--652",
journal = "Nature Cell Biology",
issn = "1465-7392",
number = "9",
}