Hsp27 negatively regulates cell death by interacting with cytochrome c.
Nat Cell Biol
; 2(9): 645-52, 2000 Sep.
Article
em En
| MEDLINE
| ID: mdl-10980706
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Apoptose
/
Grupo dos Citocromos c
/
Proteínas de Choque Térmico
/
Proteínas de Neoplasias
Limite:
Humans
Idioma:
En
Revista:
Nat Cell Biol
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
França