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Activation of p70 S6 protein kinase is necessary for angiotensin II‐induced hypertrophy in neonatal rat cardiac myocytes
Author(s) -
Takano Hiroyuki,
Komuro Issei,
Zuu Yunzeng,
Kudoh Sumiyo,
Yamazaki Tsutomu,
Yazaki Yoshio
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01523-x
Subject(s) - angiotensin ii , p70 s6 kinase 1 , medicine , muscle hypertrophy , angiotensin ii receptor type 1 , phosphorylation , endocrinology , chemistry , kinase , protein kinase a , protein biosynthesis , myocyte , renin–angiotensin system , microbiology and biotechnology , receptor , biology , protein kinase b , biochemistry , blood pressure
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 .