Platelet endothelial cell adhesion molecule (PECAM-1 (CD31))

Platelet endothelial cell adhesion molecule (PECAM-1/CD31) is a highly glycosylated cell adhesion protein of approximately 130 kDa, encoded by the PECAM1 gene on human chromosome 17q23.3[1][2]. It is mainly expressed on platelets, leukocytes, and concentrated at the intercellular junctions of endothelial cells[2][6]. Structurally, it contains six extracellular immunoglobulin-like domains, a single transmembrane region, and a cytoplasmic tail with immunoreceptor tyrosine-based inhibitory motifs (ITIMs)[3][5]. PECAM-1 mediates cell-cell interactions through its homophilic binding, playing critical roles in leukocyte transmigration, regulation of vascular permeability, mechanotransduction, and immune cell inhibition. It is implicated in angiogenesis, inflammation, cardiovascular disease, and cancer. PECAM-1 can be targeted experimentally with antibodies, with serum levels used as biomarkers in cancer prognosis[1][4]. Therapeutic targeting of PECAM-1 is challenged by its fundamental role in vascular integrity and immune regulation[4][6].

Other names

Cluster of differentiation 31CD31PECAM1Platelet-endothelial cell adhesion molecule-1

Inhibition of homophilic or heterophilic PECAM-1 interactions (e.g., antibody-mediated) Modulation of leukocyte or neutrophil trafficking Antibody binding to membrane-proximal extracellular domain leads to conformational changes and affinity modulation[4]