αB-crystallin extracellularly suppresses ADP-induced granule secretion from human platelets

Yukiko Enomoto, Seiji Adachi, Rie Matsushima-Nishiwaki, Masayuki Niwa, Haruhiko Tokuda, Shigeru Akamatsu, Tomoaki Doi, Hisaaki Kato, Shinichi Yoshimura, Shinji Ogura, Toru Iwama, Osamu Kozawa*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)2464-2468
Number of pages5
JournalFEBS Letters
Volume583
Issue number15
DOIs
StatePublished - 2009/08/06

Keywords

  • Adenosine diphosphate
  • Heat shock protein
  • Platelet
  • Platelet-derived growth factor-AB
  • Serotonin
  • αB-crystallin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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