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Platelet-derived growth factor-BB phosphorylates heat shock protein 27 in cardiac myocytes

✍ Scribed by Motoki Takenaka; Hiroyuki Matsuno; Akira Ishisaki; Keiichi Nakajima; Kouseki Hirade; Mariko Takei; Eisuke Yasuda; Shigeru Akamatsu; Naoki Yoshimi; Kanefusa Kato; Osamu Kozawa

Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
353 KB
Volume
91
Category
Article
ISSN
0730-2312

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✦ Synopsis

Abstract

It is recognized that heat shock protein 27 (HSP27) is highly expressed in heart. In the present study, we investigated whether platelet‐derived growth factor (PDGF) phosphorylates HSP27 in mouse myocytes, and the mechanism underlying the HSP27 phosphorylation. Administration of PDGF‐BB induced the phosphorylation of HSP27 at Ser‐15 and ‐85 in mouse cardiac muscle in vivo. In primary cultured myocytes, PDGF‐BB time dependently phosphorylated HSP27 at Ser‐15 and ‐85. PDGF‐BB stimulated the phosphorylation of p44/p42 mitogen‐activated protein (MAP) kinase, p38 MAP kinase, and stress‐activated protein kinase/c‐Jun N‐terminal kinase (SAPK/JNK) among the MAP kinase superfamily. SB203580, a specific inhibitor of p38 MAP kinase, reduced the PDGF‐BB‐stimulated phosphorylation of HSP27 at both Ser‐15 and ‐85, and phosphorylation of p38 MAP kinase. However, PD98059, a specific inhibitor of MEK, or SP600125, a specific inhibitor of SAPK/JNK, failed to affect the HSP27 phosphorylation. These results strongly suggest that PDGF‐BB phosphorylates HSP27 at Ser‐15 and ‐85 via p38 MAP kinase in cardiac myocytes. © 2003 Wiley‐Liss, Inc.

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