Activation of p70 S6 protein kinase is necessary for angiotensin II‐induced hypertrophy in neonatal rat cardiac myocytes

FEBS Letters

Yazaki, Yoshio¹  Zuu, Yunzeng¹  Kudoh, Sumiyo¹  Takano, Hiroyuki¹  Yamazaki, Tsutomu¹  Komuro, Issei¹ 

[1] Department of Medicine III, University of Tokyo School of Medicine, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Angiotensin II;    p70 S6 protein kinase;    Rat cardiomyocyte;    Cardiac hypertrophy;    MAP kinase;    c-fos;    Ang II;    angiotensin II;    PKC;    protein kinase C;    MAP;    mitogen-activated protein;    p90rsk;    90 kDa S6 kinase;    ACE;    angiotensin-converting enzyme;    p70S6K;    70 Dka S6 kinase;    MBP;    myelin basic protein;    FKBP;    FK506-binding protein;   

DOI  :  10.1016/0014-5793(95)01523-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Although many lines of evidence have suggested that angiotensin II (Ang II) plays an important role in development of cardiac hypertrophy, the mechanism by which Ang II increases protein synthesis in cardiac myocytes remains unclear. It has been reported that the phosphorylation of S6 protein in 40 S ribosome is correlated to the efficiency of protein synthesis. In the present study, we have examined whether Ang II activates p70 S6 kinase (p70^S6K), which has been reported to phosphorylate S6 protein. Ang II activated p70^S6K through AT1 receptor. An immunosuppressant agent, rapamycin, inhibited Ang II-induced p70^S6K activation but not the activation of MAP kinases or the induction of c-fos gene expression. Rapamycin also abolished Ang II-induced increase in protein synthesis. These results suggest that Ang II induces cardiac hypertrophy by activating p70^S6K.

【 授权许可】

Unknown