cAMP regulates ADP-induced HSP27 phosphorylation in human platelets

Yukiko Enomoto, Seiji Adachi, Tomoaki Doi, Hideo Natsume, Kenji Kato, Rie Matsushima-Nishiwaki, Shigeru Akamatsu, Haruhiko Tokuda, Shinichi Yoshimura, Takanobu Otsuka, Shinji Ogura, Osamu Kozawa*, Toru Iwama

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

9 被引用数 (Scopus)

抄録

Elevation of cAMP in platelets is recognized to play a suppressive role in platelet functions. We have previously shown that adenosine diphosphate (ADP)-induced phosphorylation of heat shock protein 27 (HSP27) via p38 mitogen-activated protein (MAP) kinase is correlated with platelet-derived growth factor (PDGF)-AB secretion and soluble CD40 ligand (sCD40L) release. In the present study, we investigated the relationship between cAMP and HSP27 phosphorylation in platelet function. 8-Bromoadenosine-3′,5′-cyclic monophosphate (8-bromo-cAMP), a plasma membrane-permeable cAMP analogue, or cilostazol, an inhibitor of cAMP phosphodiesterase, markedly attenuated the ADP-induced phosphorylation levels of p38 MAP kinase. In addition, the ADP-induced HSP27 phosphorylation was suppressed by 8-bromo-cAMP or cilostazol. 8-Bromo-cAMP, forskolin and cilostazol remarkably reduced the ADP-stimulated PDGF-AB secretion and sCD40L release. These results strongly suggest that cAMP regulates ADP-stimulated platelet activation due to inhibition of HSP27 phosphorylation via p38 MAP kinase.

本文言語英語
ページ(範囲)695-700
ページ数6
ジャーナルInternational Journal of Molecular Medicine
27
5
DOI
出版ステータス出版済み - 2011/05

ASJC Scopus 主題領域

  • 遺伝学

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