Protease activated receptors 1 and 4 govern the responses of human platelets to thrombin.
Studies carried out in the past 12 years have established that activation of protease-activated receptor (PAR)-1 and PAR-4 by thrombin essentially drives human platelet activation. Thrombin is the most potent physiologic agonist of platelets. PAR-1 and PAR-4 are found on human platelets and are half of the family of the four known 7-transmembrane receptors that are activated by a single proteolytic cleavage within the amino terminal extracellular domain of these receptors. This review will consider the direct and indirect evidence that apparently support the idea that PAR-1 and PAR-4 activation by thrombin drives platelet activation
Department of Pathology and Molecular Medicine, Faculty of Health Sciences, McMaster University, 1200 Main Street West, 3N26, Hamilton, Ont., Canada L8N 3Z5. ofosuf@mcmaster.ca
Frederick A
FA
Ofosu
D001792:Blood Platelets / Q000502:physiology*; D006801:Humans; D015539:Platelet Activation; D044463:Receptor, PAR-1; D018179:Receptors, Thrombin / Q000378:metabolism / Q000502:physiology*; D013917:Thrombin / Q000378:metabolism / Q000502:physiology*
D044463:Receptor, PAR-1; D018179:Receptors, Thrombin; D013917:Thrombin; C112908:protease-activated receptor 4