p70 S6 kinase is activated by sodium arsenite in adult rat cardiomyocytes: Roles for phosphatidylinositol 3-kinase and p38 MAP kinase

被引:44
作者
Wang, XM [1 ]
Proud, CG [1 ]
机构
[1] UNIV KENT, RES SCH BIOSCI, CANTERBURY CT2 7NJ, KENT, ENGLAND
关键词
D O I
10.1006/bbrc.1997.7273
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
p70 S6 kinase (p70 S6k) is important in regulating a variety of cellular functions including mRNA translation and cell cycle progression and is activated by mitogens and hormones, Unexpectedly, we have found that, in adult rat cardiomyocytes, arsenite, which generally induces stress responses, markedly and rapidly activates p70 S6k, This activation of p70 S6k is completely blocked by rapamycin but only partially prevented by inhibitors of phosphatidylinositol 3-kinase. In trying to delineate the mechanism underlying this effect, we found that arsenite did not activate protein kinase B, JNK or MAP kinase, but did activate p38 MAP kinase in cardiac myocytes. A specific inhibitor of p38 MAP kinase (SB203580) partially attenuated the stimulation of p70 S6k by arsenite. These data indicate that the activation of p70 S6k by arsenite involves p38 MAP kinase and phosphatidylinositol 3-kinase but not PKB. (C) 1997 Academic Press.
引用
收藏
页码:207 / 212
页数:6
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