The Possibility of Novel Antiplatelet Peptides: The Physiological Effects of Low Molecular Weight HSPs on Platelets

Author(s): Yosuke Kanno, Hiroyuki Matsuno

Journal Name: Current Pharmaceutical Design

Volume 12 , Issue 7 , 2006

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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 αBcrystallin on platelet function in vitro and ex vivo. HSP20 and αB-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 αB-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 αB-crystallin significantly reduced platelet aggregation induced by TRAP, but not a PAR-4 agonist. These findings strongly suggest that HSP20 or αB-crystallin can act intercellularly to regulate platelet functions. Our results may provide the basis for a novel defensive system to thrombus formation in vivo.

Keywords: Heat shock protein, platelets, thrombin

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Article Details

Year: 2006
Published on: 01 March, 2012
Page: [887 - 892]
Pages: 6
DOI: 10.2174/138161206776056047
Price: $65

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