Investigation of p20, a heat shock protein, in platelet function

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We investigated the effects of p20, a low molecular weight heat shock protein, on platelet aggregation and the mechanism. We obtained the results as follows:1. p38 mitogen-activated protein kinase is required for vasopressin-stimulated HSP27 induction in vascular smooth muscle cells, and the activation of p38 mitogen-activated protein kinase is dependent on protein kinase C.2. αB-crystallin, which is discharged from vessel walls in response to endothelial injury, acts intercellularly as a regulator of platelet function. Moreover, these findings could be a part of new concept of antiplatelet therapy in the treatment of cardiovascular diseases.