Platelet-derived growth factor-BB phosphorylates heat shock protein 27 in cardiac myocytes |
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Authors: | Takenaka Motoki Matsuno Hiroyuki Ishisaki Akira Nakajima Keiichi Hirade Kouseki Takei Mariko Yasuda Eisuke Akamatsu Shigeru Yoshimi Naoki Kato Kanefusa Kozawa Osamu |
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Institution: | Department of Pharmacology, Gifu University School of Medicine, Gifu 500-8705, Japan. |
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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. |
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Keywords: | HSP27 PDGF‐BB phosphorylation MAP kinase cardiac myocytes |
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