THE LECTIN WHEAT-GERM-AGGLUTININ INDUCES RAPID PROTEIN-TYROSINE PHOSPHORYLATION IN HUMAN PLATELETS

被引：21

作者：

INAZU, T ^{[1
]}

TANIGUCHI, T ^{[1
]}

OHTA, S ^{[1
]}

MIYABO, S ^{[1
]}

YAMAMURA, H ^{[1
]}

机构：

[1] FUKUI MED SCH,DEPT INTERNAL MED 3,FUKUI 91011,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 174卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)91541-J

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：

In response to wheat germ agglutinin (WGA), platelet aggregation and stimulation of protein-tyrosine phosphorylation were observed in a dose dependent manner. These reactions were completely inhibited by coexistence of N-acetyl-D-glucosamine with WGA. Upon stimulation by this agonist, protein-tyrosine phosphorylation of seven bands with molecular masses of 140-, 130-, 80-, 76-, 53-, 38- and 35-kDa proteins was observed by immunoblot. These protein-tyrosine phosphorylations were divided into three groups by kinetics. Considering the previous report from our laboratory that thrombin and collagen induced tyrosine phosphorylation in 135-, 124- and 76-kDa proteins (Nakamura, S. and Yamamura, H. (1989) J. Biol. Chem. 264, 7089-7091.), there may be another signal transduction pathway in tyrosine phosphorylation of human platelets. © 1991.

引用

页码：1154 / 1158

页数：5

共 20 条

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