PEC AM-1 (CD31) is a 130 kDa glycoprotein expressed on endothelial cells, platelets and some leukocytes. CD31 is constitutively expressed on endothelial cells, and its expression is nor increased by cytokines. Molecular cloning studies have shown that CD31 is composed of six extracellular Ig-superfamily domains, a short transmembrane region, and a relatively long cytoplasmic tail of 118 amino acids containing potential sites for post-translational modifications. Alternative splicing of the cytoplasmic tail can generate multiple CD31 isoforms that may differ in phosphorylation, cytoskeletal association and ligand affinity. CD31 is heavily glycosylated and glycosylation accounts for 40% of the mass of CD31. PECAM-1 appears to be able to interact both with itself in an homophilic interaction and with other molecules in an heterophilic interaction. In endothelial cells, CD31 is localized at intercellular junctions, and plays an important role in adhesion of endothelial cells. Its function might be regulated via phosphorylation of the cytoplasmic domain. PECAM-1 is directly involved in the process of leukocyte diapedesis between endothelial cells, as demonstrated by inhibition studies using PECAM-1 -specific mAbs and soluble recombinant PECAM-1. Leukocytes blocked in transmigration by anti-PECAM-1 remained attached to the endothelium, clearly implicating PECAM-1 in diapedesis rather than in adhesion.

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