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Titolo:
Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
Autore:
Byun, Y; Chen, F; Chang, R; Trivedi, M; Green, KJ; Cryns, VL;
Indirizzi:
Northwestern Univ, Div Endocrinol, Ctr Endocrinol Metab & Mol Med, Dept Med, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 d, Dept Med, Chicago, IL 60611 USA Northwestern Univ, Sch Med, Dept Pathol, Chicago, IL 60611 USA Northwestern Univ Chicago IL USA 60611 Dept Pathol, Chicago, IL 60611 USA
Titolo Testata:
CELL DEATH AND DIFFERENTIATION
fascicolo: 5, volume: 8, anno: 2001,
pagine: 443 - 450
SICI:
1350-9047(200105)8:5<443:CCOVDI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLY(ADP-RIBOSE) POLYMERASE; LAMIN-A; SUBSTRATE; PROTEASES; REORGANIZATION; IDENTIFICATION; SPECIFICITIES; PROTEOLYSIS; ACTIVATION; PROTEINASE;
Keywords:
caspases; proteases; cytoskeleton; intermediate filaments; vimentin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Cryns, VL Northwestern Univ, Div Endocrinol, Ctr Endocrinol Metab & Mol Med, Dept Med,Sch Med, Tarry 15-755,303 E Chicago Ave, Chicago, IL 60611 USA Northwestern Univ Tarry 15-755,303 E Chicago Ave Chicago IL USA 60611
Citazione:
Y. Byun et al., "Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis", CELL DEAT D, 8(5), 2001, pp. 443-450

Abstract

Caspases are key mediators of apoptosis, Using a novel expression cloning strategy we recently developed to identify cDNAs encoding caspase substrates, we isolated the intermediate filament protein vimentin as a caspase substrate, vimentin is preferentially cleaved by multiple caspases at distinct sites in vitro, including Asp(85) by caspases-3 and -7 and Asp(259) by caspase-6, to yield multiple proteolytic fragments. Vimentin is rapidly proteolyzed by multiple caspases into similar sized fragments during apoptosis induced by many stimuli. Caspase cleavage of vimentin disrupts its cytoplasmicnetwork of intermediate filaments and coincides temporally with nuclear fragmentation. Moreover, caspase proteolysis of vimentin at Asp(85) generatesa pro apoptotic amino-terminal fragment whose ability to induce apoptosis is dependent on caspases, Taken together, our findings suggest that caspaseproteolysis of vimentin promotes apoptosis by dismantling intermediate filaments and by amplifying the cell death signal via a pro-apoptotic cleavageproduct.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 15:57:11