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αB‐crystallin extracellularly suppresses ADP‐induced granule secretion from human platelets
Author(s) -
Enomoto Yukiko,
Adachi Seiji,
Matsushima-Nishiwaki Rie,
Niwa Masayuki,
Tokuda Haruhiko,
Akamatsu Shigeru,
Doi Tomoaki,
Kato Hisaaki,
Yoshimura Shinichi,
Ogura Shinji,
Iwama Toru,
Kozawa Osamu
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.036
Subject(s) - secretion , phosphorylation , platelet , hsp27 , adenosine diphosphate , protein kinase a , chemistry , microbiology and biotechnology , p38 mitogen activated protein kinases , mapk/erk pathway , kinase , heat shock protein , granule (geology) , adenosine , biochemistry , biology , hsp70 , platelet aggregation , immunology , paleontology , gene
αB‐crystallin, a low‐molecular‐weight heat shock protein (HSP), has binding sites on platelets. However, the exact role of αB‐crystallin is not clarified. In this study, we investigated the effect of αB‐crystallin on platelet granule secretion. αB‐crystallin attenuated the adenosine diphosphate (ADP)‐induced phosphorylation of p44/p42 mitogen‐activated protein kinase (MAPK) and p38 MAPK. The ADP‐stimulated HSP27 phosphorylation was markedly reduced by αB‐crystallin. αB‐crystallin significantly suppressed the ADP‐induced secretions of both platelet‐derived growth factor (PDGF)‐AB and serotonin. Therefore, our results strongly suggest that αB‐crystallin extracellularly suppresses platelet granule secretion by inhibition of HSP27 phosphorylation via p44/p42 MAPK and p38 MAPK.