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Titolo:
Tyrosine phosphorylation of the p85 subunit of phosphatidylinositol 3-kinase correlates with high proliferation rates in sublines derived from the Jurkat leukemia
Autore:
Martinez-Lorenzo, MJ; Anel, A; Monleon, I; Sierra, JJ; Pineiro, A; Naval, J; Alava, MA;
Indirizzi:
Univ Zaragoza, Fac Ciencias, Dept Bioquim & Biol Mol & Celular, E-50009 Zaragoza, Spain Univ Zaragoza Zaragoza Spain E-50009 & Celular, E-50009 Zaragoza, Spain
Titolo Testata:
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
fascicolo: 4, volume: 32, anno: 2000,
pagine: 435 - 445
SICI:
1357-2725(200004)32:4<435:TPOTPS>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-CELL ACTIVATION; SIGNAL-TRANSDUCTION; PHOSPHOINOSITIDE 3-KINASE; KINASE; PROTEIN; INHIBITOR; STIMULATION; ASSOCIATION; PATHWAY; ANTIGEN;
Keywords:
leukemia; tyrosine phosphorylation; proliferation; p85 subunit of P13K;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Alava, MA Univ Zaragoza, Fac Ciencias, Dept Bioquim & Biol Mol & Celular, E-50009 Zaragoza, Spain Univ Zaragoza Zaragoza Spain E-50009 , E-50009 Zaragoza, Spain
Citazione:
M.J. Martinez-Lorenzo et al., "Tyrosine phosphorylation of the p85 subunit of phosphatidylinositol 3-kinase correlates with high proliferation rates in sublines derived from the Jurkat leukemia", INT J BIO C, 32(4), 2000, pp. 435-445

Abstract

A prominent tyrosine phosphorylated protein of 85 kDa (p85) was detected in highly proliferative sublines derived from the Jurkat T cell leukemia. Weundertook a study to characterize the identity of this protein and its possible role in the hyperproliferative phenotypes observed. Using immunoblot and immunoprecipitation techniques, this protein was characterized as the p85 regulatory subunit of phosphatidylinositol 3-kinase. Cell proliferation and p85 tyrosine phosphorylation was not affected by tyrphostin AG-490, an inhibitor of Jak kinases, wortmannin or LY294002, inhibitors of the activity of the catalytic phosphatidylinositol 3-kinase subunit. Herbimycin-A and PPI, inhibitors of ac-like protein tyrosine kinases, and genistein, a general tyrosine kinase inhibitor, inhibited p85 tyrosine phosphorylation and induced cell death in the sublines, PD98059, an inhibitor of Mek, inhibited cell growth of the sublines, but not that of the parental cells. It was concluded that tyrosine phosphorylation of p85 is associated with highly proliferative tumoral phenotypes. at least in T cell leukemias, independent of the phosphatidylinositol 3-kinase activity of the catalytic subunit, (C) 2000Elsevier Science Ltd. All rights reserved.

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Documento generato il 26/09/20 alle ore 05:13:00