PECAM1 (platelet and endothelial cell adhesion molecule 1), a member of the Ig (immunoglobulin) superfamily, is a multifunctional vascular cell adhesion and signaling molecule. It is a surface molecule found on circulating leukocytes, endothelial cells, and platelets. It is a glycoprotein with a molecular weight of 130kDa, and is composed of a single-chain of six Ig-like extracellular homology domains (total 574-residues), a transmembrane portion of 19 residues, and a cytoplasmic tail containing 118 amino acids. This gene is localized to human chromosome 17q23, and is a 75kb gene composed of 16 exons.
Monomeric glycosylated PECAM-1 migrates at an apparent molecular weight of approximately 80.0-95.0kDa by SDS-PAGE analysis under reducing conditions.
PECAM1 (platelet and endothelial cell adhesion molecule 1) forms an essential part of the endothelial cell intercellular junctions in vascular beds. Its extracellular domain is involved in homo- and heterophilic interactions, and its cytosolic domain is involved in the transduction of a variety of cellular signaling. It controls vascular inflammatory response as it functions as both pro-inflammatory and anti-inflammatory molecule. Its capacity for hemophilic interactions renders it essential for leukocyte transmigration, interendothelial cell bindings, and vascular permeability regulation. This molecule is thought to be involved in the pathogenesis of various disorders such as thrombosis, cardiovascular disease, inflammation, and cancer.
