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If you cut yourself, your hemostatic system will recruit circulating platelets and plasma fibrinogen/fibrin to staunch the loss of blood. These two arms of hemostasis combine to produce the hemostatic plug, comprised of aggregated platelets and deposited fibrin. “Plug” formation is regulated in terms of time, place, and extent so as to minimize bleeding from injured arteries/veins, while avoiding any obstruction of nearby uninjured vessels. Such finely tuned regulation entails cross-talk between the platelet and the fibrin pathways, and nature has chosen the plasma protease, thrombin, acting on platelet thrombin receptor(s) as the vital link between the two systems. This linkage is the topic of studies by Ramakrishnan and colleagues (1) in this issue of PNAS, who have applied “knockout-mouse” technology to identify a heretofore unappreciated platelet thrombin receptor, glycoprotein (GP) Ib–IX–V (1). A main conclusion is that GP Ib–IX–V acts as a thrombin receptor only after it jettisons its GP V chain/inhibitor, either through thrombin cleavage or knockout. Thrombin is the major product of the plasma coagulation “cascade” of sequential “zymogen-to-protease” steps. As the culmination of a series of proteolytic cleavages, thrombin converts fibrinogen to fibrin, which deposits at sites of bleeding or thrombosis as the fibrinous portion of a hemostatic plug or a thrombotic mass. However, thrombin plays an alternate role in platelet function as …

A new “kid” on the platelet thrombin receptor “block”: Glycoprotein Ib–IX–V