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

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

Volume: 12 Issue: 7

Author(s): Yosuke Kanno and Hiroyuki Matsuno

Affiliation:

Keywords: Heat shock protein, platelets, thrombin

Abstract: 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.

Cite this article as:

Kanno Yosuke and Matsuno Hiroyuki, The Possibility of Novel Antiplatelet Peptides: The Physiological Effects of Low Molecular Weight HSPs on Platelets, Current Pharmaceutical Design 2006; 12 (7) . https://dx.doi.org/10.2174/138161206776056047