Activation of protein kinase C by tyrosine phosphorylation in response to H2O2

被引：519

作者：

Konishi, H

Tanaka, M

Takemura, Y

Matsuzaki, H

Ono, Y

Kikkawa, U

Nishizuka, Y

机构：

[1] KOBE UNIV, BIOSIGNAL RES CTR, NADA KU, KOBE, HYOGO 657, JAPAN

[2] KOBE UNIV, FAC SCI, DEPT BIOL, KOBE, HYOGO 657, JAPAN

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1997年 / 94卷 / 21期

关键词：

D O I：

10.1073/pnas.94.21.11233

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：

Protein kinase C (PKC) isoforms, alpha, beta I, and gamma of cPKC subgroup, delta and epsilon of nPKC subgroup, and zeta of aPKC subgroup, were tyrosine phosphorylated in COS-7 cells in response to H2O2. These isoforms isolated from the H2O2-treated cells showed enhanced enzyme activity to various extents. The enzymes, PKC alpha and delta, recovered from the cells were independent of lipid cofactors for their catalytic activity. Analysis of mutated molecules of PKC delta showed that tyrosine residues, which are conserved in the catalytic domain of the PKC family, are critical for PKC activation induced by H2O2. These results suggest that PKC isoforms can be activated through tyrosine phosphorylation in a manner unrelated to receptor-coupled hydrolysis of inositol phospholipids.

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收藏

页码：11233 / 11237

页数：5

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