THE LECTIN WHEAT-GERM-AGGLUTININ STIMULATES A PROTEIN-TYROSINE KINASE-ACTIVITY OF P72SYK IN PORCINE SPLENOCYTES

被引：26

作者：

YAMADA, T ^{[1
]}

TANIGUCHI, T ^{[1
]}

NAGAI, K ^{[1
]}

SAITOH, H ^{[1
]}

YAMAMURA, H ^{[1
]}

机构：

[1] FUKUI MED SCH,DEPT OTORHINOLARYNGOL,FUKUI 91011,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 03期

关键词：

D O I：

10.1016/S0006-291X(05)81340-3

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：

We previously reported a molecular cloning of porcine gene syk encoding a non-receptor type 72-kDa protein-tyrosine kinase and a generation of anti-CPTK40 antibodies which could immunoprecipitate the activity of p72syk(Taniguchi et al. (1991) J. Biol. Chem. 266, 15790-15796). In this study, we have demonstrated that wheat germ agglutinin caused an increase in the autophosphorylation activity of p72syk which preceded an increase of protein-tyrosine phosphorylation observed at the same time in porcine splenocyte. The increase of p72syk activity was dose dependent and was inhibited by the coexistence of N-acetyl-D-glucosamine. Upon stimulation by the combination of 4β-phorbol 12-myristate 13-acetate and ionophore A23187, we could not detect the increase of activity of p72syk suggesting that the activation of p72syk was independent of protein kinase C and calcium ions. © 1991 Academic Press, Inc.

引用

页码：1325 / 1329

页数：5

共 23 条

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