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Titolo:
ASSOCIATION OF PHOSPHATIDYLINOSITOL 3-KINASE WITH THE PROTOONCOGENE PRODUCT CBL UPON CD38 LIGATION BY A SPECIFIC MONOCLONAL-ANTIBODY IN THP-1 CELLS
Autore:
MATSUO T; HAZEKI K; TSUJIMOTO N; INOUE SI; KUROSU H; KONTANI K; HAZEKI O; UI M; KATADA T;
Indirizzi:
UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM TOKYO 113 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM TOKYO 113 JAPAN INST PHYS & CHEM RES,UI LAB WAKO SAITAMA 35101 JAPAN
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 397, anno: 1996,
pagine: 113 - 116
SICI:
0014-5793(1996)397:1<113:AOP3WT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE ANTIGEN CD38; TYROSINE PHOSPHORYLATION; SIGNAL TRANSDUCTION; NAD GLYCOHYDROLASE; C-CBL; EXPRESSION; GLYCOPROTEIN; KINASE; ACID; GRB2;
Keywords:
CD38; PHOSPHATIDYLINOSITOL 3-KINASE; PROTOONCOGENE PRODUCT CBL; TYROSINE PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
T. Matsuo et al., "ASSOCIATION OF PHOSPHATIDYLINOSITOL 3-KINASE WITH THE PROTOONCOGENE PRODUCT CBL UPON CD38 LIGATION BY A SPECIFIC MONOCLONAL-ANTIBODY IN THP-1 CELLS", FEBS letters, 397(1), 1996, pp. 113-116

Abstract

We reported that ecto-NAD(+) glycohydrolase activity induced upon differentiation of HL-60 cells with retinoic acid is localized on the extracellular domain of CD38 and that CD38 ligation by a specific monoclonal antibody, HB-7, is followed by rapid tyrosine phosphorylation of cellular proteins including a proto-oncogene product, Cbl. In the present study, we investigated intracellular signaling linked to the HB-7-induced Cbl phosphorylation in dibutyryl cAMP-treated THP-1 cells. The 85-kDa regulatory subunit (p85) of phosphatidylinositol (PT) 3-kinase was immunoprecipitated with anti-Cbl antibody in a manner dependent onthe tyrosine phosphorylation of Cbl. PI 3-kinase activity was also observed in the immunoprecipitated fractions containing tyrosine-phosphorylated Cbl. The phosphorylated form of Cbl, which had been separated from the CD38-stimulated cells, was capable of directly binding to a recombinant p85 fused to glutathione S-transferase. Thus, the direct association of tyrosine-phosphorylated Cbl with PI 3-kinase, possibly leading to the kinase activation, appeared to be involved in intracellular signaling caused by the CD38 ligation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:28:45