The Possibility of Novel Antiplatelet Peptides: the Physiological Effects of Low Molecular Weight Hsps on Platelets.
From: Institute of Biological Science, University of Tsukuba, Iabaraki, Japan.
Current pharmaceutical design
- Publish Date: 2006
- ISSN: 1381-6128
- Volume: 12
- Issue: 7
- Pages: 887-92
- Medium: Print
- Language: English
- Citation (JAMA): Kanno Yosuke, Matsuno Hiroyuki, et al. The Possibility of Novel Antiplatelet Peptides: the Physiological Effects of Low Molecular Weight Hsps on Platelets.. Curr. Pharm. Des. 2006;12:887-92
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.
Mesh Headings (Keywords): Animals, Blood Platelets, Heat-Shock Proteins, Small, Humans, Models, Biological, Peptides, Platelet Aggregation, Platelet Aggregation Inhibitors, alpha-Crystallin B Chain
Check for Full Text / PubMed Unique Identifier (PMID): 16515504
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