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Overview
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Background
CD62P (P-selectin) is an adhesion glycoprotein that is expressed on platelets and endothelial cells upon their activation. Interaction between CD62P and its mucin-like ligand PSGL-1 (P-selectin glycoprotein ligand-1) expressed on the microvilli of most leukocytes supports leukocyte rolling along postkapillary venules at the earliest time of inflammation. Both CD62P and PSGL-1 are extended glycoproteins that form homodimers. CD62P dimerization is probably mediated through interactions of the transmembrane domains and stabilizes leukocyte tethering and rolling, probably by increasing rebinding within a bond cluster.
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