Hsp27 negatively regulates cell death by interacting with cytochrome c.

Date publication

septembre 2000

Journal

Nature cell biology

Auteurs

Membres identifiés du Cancéropôle Est :
Dr GARRIDO Carmen , Pr BONNIAUD Philippe

Tous les auteurs :
Bruey JM, Ducasse C, Bonniaud P, Ravagnan L, Susin SA, Diaz-Latoud C, Gurbuxani S, Arrigo AP, Kroemer G, Solary E, Garrido C

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/10980706

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.

Mots clés

Apoptosis, Apoptosis Inducing Factor, Caspases, metabolism, Cytochrome c Group, metabolism, Cytosol, metabolism, Enzyme Activation, Flavoproteins, metabolism, HSP27 Heat-Shock Proteins, Heat-Shock Proteins, metabolism, Humans, Membrane Proteins, metabolism, Neoplasm Proteins, genetics, U937 Cells

Référence

Nat. Cell Biol.. 2000 Sep;2(9):645-52