Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The temporal relationship between protein phosphatase, mitochondrial cytochrome c release, and caspase activation in apoptosis
Autore:
Wolf, CM; Eastman, A;
Indirizzi:
Dartmouthcol,l, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Pharmacol & Toxi Dartmouth Coll Hanover NH USA 03755 tmouth Med Sch, Dept Pharmacol & Toxi
Titolo Testata:
EXPERIMENTAL CELL RESEARCH
fascicolo: 2, volume: 247, anno: 1999,
pagine: 505 - 513
SICI:
0014-4827(19990315)247:2<505:TTRBPP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGRAMMED CELL-DEATH; DNA FRAGMENTATION; ICE/CED-3 PROTEASE; INTRACELLULAR ACIDIFICATION; OKADAIC ACID; PHOSPHORYLATION; BCL-2; ELEGANS; ENDONUCLEASE; INHIBITION;
Keywords:
HL-60 cells; Jurkat cells; staurosporine; Fas receptor; z-VAD-FMK; calyculin A; zinc;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Eastman, A Dartmouthcol,l, Hitchcock Med Ctr, Dartmouth Med Sch, Dept Pharmacol & Toxi Dartmouth Coll 7650 Remsen Hanover NH USA 03755 harmacol & Toxi
Citazione:
C.M. Wolf e A. Eastman, "The temporal relationship between protein phosphatase, mitochondrial cytochrome c release, and caspase activation in apoptosis", EXP CELL RE, 247(2), 1999, pp. 505-513

Abstract

Apoptosis is mediated by members of the caspase family of proteases which can be activated by release of mitochondrial cytochrome c. Additional members of the caspase family are activated at the cell surface in response to direct stimulus from the external environment such as by activation of the Fas receptor. It has been suggested that these upstream caspases directly activate the downstream caspases which would obviate a role for cytochrome c in apoptosis induced by the Fas receptor. We demonstrate that cytochrome c is released from mitochondria of Jurkat cells in response to both staurosporine and an agonistic anti-Fas antibody and that only the latter is inhibited by the caspase inhibitor z-VAD-FMK. This suggests that an upstream caspase such as caspase-8 is required for the Fas-mediated release of mitochondrial cytochrome c. The protein phosphatase inhibitor calyculin A prevented cytochrome c release and apoptosis induced by both agents, suggesting that release of cytochrome c is required in both models. Zinc, once thought of asan endonuclease inhibitor, has previously been shown to prevent the activation of caspase-3. We show that zinc prevents the activation of downstream caspases and apoptosis induced by both insults, yet does not prevent release of mitochondrial cytochrome c. The ability of calyculin A and zinc to prevent DNA digestion implies that the mitochondrial pathway is important for induction of apoptosis by both agents. These results do not support an alternative pathway in which caspase-8 directly activates caspase-3. These results also demonstrate that a critical protein phosphatase regulates the release of cytochrome c and apoptosis induced by both insults. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 16:22:46