PROTEIN-TYROSINE-PHOSPHATASE ACTIVITY ENHANCEMENT IS INDUCED UPON FC-EPSILON, RECEPTOR ACTIVATION OF MAST-CELLS

被引：15

作者：

HAMPE, CS ^{[1
]}

PECHT, I ^{[1
]}

机构：

[1] WEIZMANN INST SCI, DEPT CHEM IMMUNOL, IL-76100 REHOVOT, ISRAEL

来源：

FEBS LETTERS | 1994年 / 346卷 / 2-3期

关键词：

RBL-2H3; LINE; IMMUNOLOGICAL SIGNAL TRANSDUCTION; RAT MUCOSAL MAST CELL;

D O I：

10.1016/0014-5793(94)00471-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Immunological stimulation of rat mucosal type mast cells (line RBL-2H3) by clustering the type I Fc(epsilon) receptor (Fc(epsilon)RI) causes a fast and transient tyrosine phosphorylation of several proteins. This implied the involvement of both, protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPases) in that process. In order to identify the PTPases involved in these very early steps coupling Fc(epsilon)RI stimulus to cell response, we undertook the purification and characterization of PTPases present in RBL-2H3 cells. In one of the cells' membranal fractions, a PTPase activity was found to be enhanced 2- to 3-fold upon cell stimulation by Fc(epsilon)RI clustering. Characterization of this activity implies its involvement in control of the Fc,RI signalling cascade.

引用

页码：194 / 198

页数：5

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