A suppressive role of p125FAK protein tyrosine kinase hydrogen peroxide-induced apoptosis of T98G cells

被引：59

作者：

Sonoda, Y ^{[1
]}

Kasahara, T ^{[1
]}

Yokota-Aizu, E ^{[1
]}

Ueno, M ^{[1
]}

Watanabe, S ^{[1
]}

机构：

[1] Kyoritsu Coll Pharm, Minato Ku, Tokyo, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1997年 / 241卷 / 03期

关键词：

D O I：

10.1006/bbrc.1997.7895

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：

Protein tyrosine phosphorylation was examined on a human glioblastoma cell line, T98G, after exposure to oxidative stress in vitro. Hydrogen peroxide (1 mM) markedly induced tyrosine phosphorylation of a 125 kDa protein at 30 min after stimulation. The 125-kDa molecule phosphorylated was revealed to be a focal adhesion kinase (FAK). Tyrosine phosphorylation of p125FAK continued at least up to 5h, and decreased after 8h concomitant with apoptosis. Tyrosine phosphorylation of p125FAK was blocked by herbimycin A, a potent inhibitor of protein tyrosine kinases, while apoptosis was accelerated. When T98G cells were incubated with FAK antisense oligonucleotide, apoptosis was also accelerated. These results suggest that tyrosine phosphorylation of p125FAK plays a suppressive role in hydrogen peroxide-induced apoptosis. (C) 1997 Academic Press.

引用

页码：769 / 774

页数：6

共 31 条

[21] AUTOPHOSPHORYLATION OF THE FOCAL ADHESION KINASE, PP125(FAK), DIRECTS SH2 DEPENDENT BINDING OF PP60(SRC) [J].