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Titolo:
Bcl-x(L) blocks activation of related adhesion focal tyrosine kinase proline-rich tyrosine kinase 2 and stress-activated protein kinase c-Jun N-terminal protein kinase in the cellular response to methylmethane sulfonate
Autore:
Pandey, P; Avraham, S; Place, A; Kumar, V; Majumder, PK; Cheng, KD; Nakazawa, A; Saxena, S; Kharbanda, S;
Indirizzi:
Harvard02115, Sch Med, Dana Farber Canc Inst, Dept Adult Oncol, Boston, MAHarvard Univ Boston MA USA 02115 Canc Inst, Dept Adult Oncol, Boston, MA Harvardolniv, Inst Med, Beth Israel Deaconess Med Ctr, Div Expt Med & Hemat Harvard Univ Boston MA USA 02115 Deaconess Med Ctr, Div Expt Med & Hemat Univ Manitoba, Manitoba Inst Cell Biol, Winnipeg, MB R3E 0V9, Canada Univ Manitoba Winnipeg MB Canada R3E 0V9 ol, Winnipeg, MB R3E 0V9, Canada
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 13, volume: 274, anno: 1999,
pagine: 8618 - 8623
SICI:
0021-9258(19990326)274:13<8618:BBAORA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-NECROSIS-FACTOR; KAPPA-B ACTIVATION; INDUCED APOPTOSIS; DEATH PATHWAY; POLY(ADP-RIBOSE) POLYMERASE; PROTEOLYTIC ACTIVATION; JNK ACTIVATION; BCL-2; CELLS; INDUCTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Kharbanda, S Harvardt,niv, Sch Med, Dana Farber Canc Inst, Dept Adult Oncol, 44 Binney S Harvard Univ 44 Binney St Boston MA USA 02115 ol, 44 Binney S
Citazione:
P. Pandey et al., "Bcl-x(L) blocks activation of related adhesion focal tyrosine kinase proline-rich tyrosine kinase 2 and stress-activated protein kinase c-Jun N-terminal protein kinase in the cellular response to methylmethane sulfonate", J BIOL CHEM, 274(13), 1999, pp. 8618-8623

Abstract

The stress-activated protein kinase/c-Jun N-terminal protein kinase (JNK) is induced in response to ionizing radiation and other DNA-damaging agents. Recent studies indicate that activation of JNK is necessary for induction of apoptosis in response to diverse agents. Here we demonstrate that methylnethane sulfonate (MMS)-induced activation of JNK is inhibited by overexpression of the anti-apoptotic protein Bcl-x(L), but not by caspase inhibitorsCrmA and p35, By contrast, UV-induced JNK activity is insensitive to Bcl-x(L). The results demonstrate that treatment with MMS is associated with an increase in tyrosine phosphorylation of related adhesion focal tyrosine kinase (RAFTK)/proline-rich tyrosine kinase 2 (PYK2), an upstream effector of JNK and that this phosphorylation is inhibited by overexpression of Bcl-x(L). Furthermore, overexpression of a dominant-negative mutant of RAFTK (RAFTK K-M) inhibits MMS-induced JNK activation, The results indicate that inhibition of RAFTK phosphorylation by MMS in Bcl-x(L) cells is attributed to anincrease in tyrosine phosphatase activity in these cells. Hence, treatmentof Bcl-x(L) cells with sodium vanadate, a tyrosine phosphatase inhibitor, restores MMS-induced activation of RAFTK and JNK. These findings indicate that RAFTK-dependent induction of JNK in response to MMS is sensitive to Bcl-x(L), but not to CrmA. and p35, by a mechanism that inhibits tyrosine phosphorylation and thereby activation of RAFTK. Taken together, these findingssupport a novel role for Bcl-x(L) that is independent of the caspase cascade.

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Documento generato il 03/07/20 alle ore 16:14:45