Showing papers by "Robert E. Gerszten published in 1992"

Thrombin receptor structure and function.

Abstract: Thrombin is a multifunctional serine protease generated at sites of vascular injury. While it is best known for its ability to cleave fibrinogen and trigger fibrin formation, thrombin is also a powerful agonist for a variety of cellular responses. First and foremost, thrombin is the most potent activator of platelets in vitro. Thrombin is also chemotactic for monocytes, and is mitogenic for lymphocytes, fibroblasts, and vascular smooth muscle cells. Thrombin acts on the vascular endothelium to stimulate production of prostacyclin, plasminogen activator inhibitor, and the potent smooth muscle cell mitogen platelet-derived growth factor. Thrombin also induces neutrophil adherence to the vessel wall by an endothelial-dependent mechanism, probably by causing surface expression of GMP-140 on the endothelial cell and directly activates neutrophils themselves. Teleologically, these disparate functions of thrombin may be unified by viewing thrombin as an orchestrator of the response to vascular injury or wounding, mediating not only hemostatic but inflammatory and proliferative or reparative responses.1