The possibility of novel antiplatelet peptides: the physiological effects of low molecular weight HSPs on platelets

Current Pharmaceutical Design
Yosuke Kanno, Hiroyuki Matsuno

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

Citations

Oct 10, 2008·Transfusion clinique et biologique : journal de la Société française de transfusion sanguine·F CognasseO Garraud
Mar 22, 2014·Biochemical Society Transactions·Tamara P MartinGeorge S Baillie
Nov 1, 2017·Cell Stress & Chaperones·V Sudhakar ReddyG Bhanuprakash Reddy
Oct 21, 2011·Physiological Reviews·Evgeny V MymrikovNikolai B Gusev
May 28, 2011·Cellular Signalling·H V EdwardsG S Baillie

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