Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9012912 | Life Sciences | 2005 | 12 Pages |
Abstract
We previously reported that p38 MAP kinase takes part in thrombin-induced HSP27 phosphorylation in aortic smooth muscle A10 cells. In the present study, we investigated whether Akt is involved in the phosphorylation of HSP27 and the role of adenylyl cyclase-cAMP system. Thrombin time-dependently induced the phosphorylation of heat shock protein 27 (HSP27) and Akt in aortic smooth muscle A10 cells. SB203580, a p38 MAP kinase inhibitor, significantly suppressed the thrombin-induced phosphorylation of Akt and the Akt inhibitor suppressed the phosphorylation of HSP27. Furthermore, the thrombin-induced phosphorylation of HSP27, p38 MAP kinase and Akt were decreased by dibutyryl-cAMP (DBcAMP). These results strongly suggest that Akt functions the thrombin-induced phosphorylation of HSP27 at a point downstream from p38 MAP kinase in aortic smooth muscle cells and the adenylyl cyclase-cAMP system is upstream regulator of the HSP27 phosphorylation in these cells.
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Authors
Keiichi Nakajima, Kouseki Hirade, Akira Ishisaki, Hiroyuki Matsuno, Hidetaka Suga, Yosuke Kanno, En Shu, Yasuo Kitajima, Yoshihiro Katagiri, Osamu Kozawa,