The family of juctional adhesion molecules (JAM), comprising at least three members, are type I transmembrane receptors belonging to the immunoglobulin (Ig) superfamily (1, 2). These proteins are localized in the tight junctions between endothelial cells or epithelial cells. Some family members are also found on blood leukocytes and platelets. Human JAM-C cDNA predicts a 310 amino acid (aa) residue precursor protein with a putative 31 aa signal peptide, a 210 aa extracellular region containing two Ig domains, a 23 aa transmembrane domain and a 46 aa cytoplasmic domain containing a PDZ-binding motif and a PKC phosphorylation site (3, 4). Human JAM-C shares 86% aa sequence identity with its mouse homologue. It also shares approximately 36% and 32% aa sequence homology with human JAM-B and JAM-A, respectively (3‑5). Human JAM-C shows widespread tissue expression and the highest levels are found in the placenta, brain, kidney and heart. JAM-C is expressed on endothelial cells of high endothelial venules in human tonsil. It is also expressed on platelets, T-cells and NK cells (3‑5). Unlike other JAM family members, JAM-C forms only weak homotypic interactions. JAM-C binds to JAM-B to facilitate the interactions between JAM-B and the integrin alpha4beta1 (6). This heterotypic interaction between leukocyte JAM-C and endothelial JAM-B may play a role in regulating leukocyte transmigration (5). On platelets, JAM-C is a counter-receptor for the leukocyte integrin Mac-1(CD11b/CD18) (7). JAM-C has also been identified as a strong candidate gene for hypoplastic left heart syndrome (8).
The nomenclature used for the JAM family proteins is confusing. VE-JAM has been referred to in the literature variously as JAM-B or JAM-C. Until further clarification, R&D Systems has adopted the nomenclature where both mouse and human VE-JAM are referred to as JAM-B. Under this system, JAM-C refers to the protein encoded by the gene localized to human chromosome 11.
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