PECAM-1 is a highly glycosylated protein with a molecular mass of approximately 130 kDa. It consists of an N-terminal domain with 574 amino acids, a transmembrane domain with 19 amino acids, and a C-terminal cytoplasmic domain with 118 amino acids . The PECAM1 gene is located on chromosome 17q23.3 in humans .
PECAM-1 is expressed on the surface of platelets, monocytes, neutrophils, and certain types of T-cells. It constitutes a significant portion of endothelial cell intercellular junctions . This protein is involved in several key functions:
PECAM-1 mediates its functions through both homophilic and heterophilic interactions. Homophilic interactions involve PECAM-1 binding to itself on adjacent cells, which is important for endothelial cell-cell adhesion . Heterophilic interactions, such as with CD177, facilitate the transendothelial migration of neutrophils .
PECAM-1 is implicated in various diseases and conditions. For instance, it is associated with angiosarcoma, a type of cancer that originates in the lining of blood vessels . Additionally, PECAM-1 plays a role in the immune response and has been linked to conditions involving inflammation and immune cell migration .
Recombinant PECAM-1 is produced using recombinant DNA technology, which involves inserting the PECAM1 gene into a suitable expression system to produce the protein in vitro. This recombinant form is used in research to study the protein’s structure, function, and role in various physiological and pathological processes.