|Detection of CD31/PECAM‑1 in Mouse Splenocytes by Flow Cytometry. Mouse splenocytes were stained with Goat Anti-Mouse CD31/PECAM‑1 Biotinylated Antigen Affinity‑purified Polyclonal Antibody (Catalog # BAF3628, filled histogram) or control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Phycoerythrin (Catalog # F0040).|
PECAM-1 (platelet-endothelial cell adhesion molecule-1; also known as CD31) is a 130 kDa type I transmembrane glycoprotein adhesion molecule in the immunoglobulin superfamily (1, 2). Expression is restricted to cells involved in circulation, especially endothelial cells, platelets, monocytes, neutrophils and lymphocyte subsets. PECAM-1 is concentrated at cell-cell junctions and is required for transendothelial migration (TEM) (1-3). The extracellular domain (ECD) of PECAM-1 has ten potential N-linked glycosylation sites and six C2-type Ig-like domains, the first of which is critical for adhesion and extravasation (3, 4). The cytoplasmic domain contains immunoregulatory tyrosine-based inhibitory and switch motifs (ITIM, ITSM) that mediate both inhibition and activation via phosphotyrosine-mediated engagement of SH2-containing signaling molecules (1, 5). Metalloproteinase-mediated ectodomain shedding occurs during apoptosis (6) but increased serum PECAM-1 ectodomain in HIV and active multiple sclerosis occurs independent of apoptosis (7, 8). In humans, expression of six isoforms with exon deletions in the cytoplasmic domain is tissue- and stage-specific, but full-length PECAM-1 is predominant. A form lacking the ITSM predominates in mouse (9). Mouse PECAM-1 ECD shows 77%, 63%, 63%, 63%, and 61% amino acid (aa) identity with rat, human, canine, porcine, and bovine PECAM-1, respectively. PECAM-1 participates with other adhesion molecules in some functions, but is the critical molecule for TEM. Homotypic PECAM-1 adhesion in trans, combined with cycling of PECAM-1 to and from surface-connected endothelial cell vesicles, leads leukocytes across endothelial tight junctions (3, 10). Homotypic adhesion and signaling functions also strongly suppress mitochondria-dependent apoptosis (11). In platelets, PECAM-1 is necessary for limiting thrombus formation (12) and promoting integrin-mediated clot retraction and platelet spreading (13), but mechanisms for these phenomena are unclear. PECAM-/- mice are deficient in chemokine-mediated chemotaxis (14).
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