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 language | English |
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Pages (from-to) | 2464-2468 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 15 |
DOIs | |
State | Published - 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