Journal
CURRENT PHARMACEUTICAL DESIGN
Volume 12, Issue 7, Pages 887-892Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138161206776056047
Keywords
heat shock protein; platelets; thrombin
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Some low molecular mass heat shock proteins (HSPs) appear to act as molecular chaperones, but their exact physiological roles have not been fully elucidated. We reported on a physiological role of HSP20, HSP27 and alpha B-crystallin on platelet function in vitro and ex vivo. HSP20 and alpha B-crystallin inhibited platelet aggregation using human Platelets dose-dependently induced by thrombin or botrocetin. On the other hand, HSP27, the other type of low molecular mass HSP, did not affect platelet aggregation. When HSP20 or alpha B-crystallin was injected intravenously as a bolus in hamsters, the development of thrombus after endothelial injury was prevented. Moreover, 9 amino-acid sequences isolated from HSP20 or alpha B-crystallin significantly reduced platelet aggregation induced by TRAP, but not a PAR-4 agonist. These findings strongly suggest that HSP20 or alpha B-crystallin can act intercellularly to regulate platelet functions. Our results may provide the basis for a novel defensive system to thrombus formation in vivo.
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