ASSOCIATION OF PROTEIN-TYROSINE KINASE WITH PHOSPHOLIPASE C-GAMMA-1 IN BONE MARROW-DERIVED MOUSE MAST-CELLS

被引：40

作者：

FUKAMACHI, H ^{[1
]}

KAWAKAMI, Y ^{[1
]}

TAKEI, M ^{[1
]}

ISHIZAKA, T ^{[1
]}

ISHIZAKA, K ^{[1
]}

KAWAKAMI, T ^{[1
]}

机构：

[1] LA JOLLA INST ALLERGY & IMMUNOL, DIV ALLERGY, LA JOLLA, CA 92037 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 20期

关键词：

SIGNAL TRANSDUCTION; FC-EPSILON-RI;

D O I：

10.1073/pnas.89.20.9524

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bone marrow-derived mouse mast cells contain phospholipase C-gamma1 (PLC-gamma1), which is phosphorylated at tyrosine residues upon cross-linking of cell-bound IgE antibodies with multivalent antigen. It was found that immune complexes formed from digitonin lysates of the mast cells by monoclonal anti-PLC-gamma1 antibodies contained protein-tyrosine kinase (PTK), which phosphorylated PLC-gamma1 in vitro. The tyrosine kinase activity coprecipitated with PLC-gamma1-anti-PLC-gamma1 complexes markedly increased when the cell lysates were obtained immediately after antigen challenge. The results indicate that PTK is associated with PLC-gamma1 in the mast cells and that the kinase is activated upon cross-linking of Fc(epsilon)RI. Neither beta nor gamma subunit of Fc(epsilon)RI nor src family PTK was coprecipitated with the PLC-gamma1-anti-PLC-gamma1 complexes. In situ denaturation/renaturation experiments, which detect autophosphorylated kinases, indicated that the PTK associated with PLC-gamma1 was a 44-kDa protein.

引用

页码：9524 / 9528

页数：5

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