[Novel physiological roles of low molecular weight HSPs].
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 the physiological roles of HSP20, HSP27, and alpha B-crystallin in platelet function in vitro and ex vivo. HSP20 and alpha B-crystallin dose-dependently inhibited the aggregation of human platelets 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 defense system against thrombus formation in vivo.
Matsuno
Hiroyuki
H
Department of Pharmacology, Gifu University, School of Medicine, Tsukasa-machi 40, Gifu 500-8705, Japan.
Kozawa
Osamu
O
D000818:Animals; D006224:Cricetinae; D003864:Depression, Chemical; D004195:Disease Models, Animal; D004305:Dose-Response Relationship, Drug; D050886:HSP20 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000494:pharmacology / Q000502:physiology*; D006801:Humans; D008970:Molecular Weight; D010750:Phosphoproteins / Q000494:pharmacology / Q000502:physiology*; D010973:Platelet Adhesiveness / Q000187:drug effects; D010974:Platelet Aggregation / Q000187:drug effects*; D013927:Thrombosis / Q000517:prevention & control; D038203:alpha-Crystallin B Chain / Q000494:pharmacology / Q000502:physiology*
D050886:HSP20 Heat-Shock Proteins; C494382:HSPB6 protein, human; D006360:Heat-Shock Proteins; D010750:Phosphoproteins; D038203:alpha-Crystallin B Chain