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HSP27 phosphorylation is correlated with ADP-induced platelet granule secretion |
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| Authors: | Kato Hisaaki Takai Shinji Matsushima-Nishiwaki Rie Adachi Seiji Minamitani Chiho Otsuka Takanobu Tokuda Haruhiko Akamatsu Shigeru Doi Tomoaki Ogura Shinji Kozawa Osamu |
| Affiliation: | a Department of Pharmacology, Gifu University Graduate School of Medicine, Yanagido1-1, Gifu 501-1194, Japan b Department of Emergency and Disaster Medicine, Gifu University Graduate School of Medicine, Gifu, Japan c Department of Clinical Laboratory, National Hospital for Geriatric Medicine, National Center for Geriatrics and Gerontology, Obu, Aichi, Japan d Department of Orthopedic Surgery, Nagoya City University Graduate School of Medical Sciences, Nagoya, Aichi, Japan e Department of Intensive Care Medicine, Matsunami General Hospital, Gifu, Japan |
| Abstract: | Adenosine diphosphate (ADP) plays a crucial role in hemostasis and thrombosis by activating platelets. ADP has been reported to induce heat-shock protein (HSP) 27 phosphorylation in human platelets. However, the exact role of HSP27 phosphorylation in human platelets has not yet been clarified. In the present study, we investigated the mechanisms and the roles of ADP-induced HSP27 phosphorylation in human platelets. We showed for the first time that both of decreased phosphorylation levels of HSP27 by PD98059, a MEK1/2 inhibitor and SB203580, a p38 MAPK inhibitor were correlated with the suppressed levels of platelet granule secretion but not with platelet aggregation. Furthermore, the inhibition of either the p44/p42 MAPK or p38 MAPK pathways had no effect on ADP-induced platelet aggregation. These results strongly suggest that the ADP-induced phosphorylation of HSP27 via p44/p42 MAPK and/or p38 MAPK is therefore sufficient for platelet granule secretion but not for platelet aggregation in humans. |
| Keywords: | HSP27 Platelet Phosphorylation ADP Granule secretion |
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