## Abstract We previously showed that vasopressin stimulates the induction of heat shock protein (HSP) 27, a low molecular‐weight HSP, through protein kinase C activation in aortic smooth muscle A10 cells. In the present study, we examined the effects of midazolam, an intravenous anesthetic, on the
Vasopressin phosphorylates HSP27 in aortic smooth muscle cells
✍ Scribed by Shigeru Akamatsu; Keiichi Nakajima; Akira Ishisaki; Hiroyuki Matsuno; Kumiko Tanabe; Mariko Takei; Motoki Takenaka; Kouseki Hirade; Naoki Yoshimi; Hidetaka Suga; Yutaka Oiso; Kanefusa Kato; Osamu Kozawa
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 482 KB
- Volume
- 92
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
Administration of arginine vasopressin (AVP) time‐dependently induced the phosphorylation of heat shock protein 27 (HSP27) at Ser‐15 and Ser‐85 in smooth muscle of aorta in vivo. The AVP‐induced phosphorylation of HSP27 at Ser‐15 and Ser‐85 was inhibited by a V1a receptor antagonist but not by a V2 receptor antagonist. In cultured aortic smooth muscle A10 cells, AVP markedly stimulated the phosphorylation of HSP27 at Ser‐15 and Ser‐85. The AVP‐induced phosphorylation of HSP27 was attenuated by SB203580 and PD169316, inhibitors of p38 mitogen‐activated protein (MAP) kinase, but not by PD98059, a MEK inhibitor. These results strongly suggest that AVP phosphorylates HSP27 via p38 MAP kinase in aortic smooth muscle cells. © 2004 Wiley‐Liss, Inc.
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