Junctional adhesion molecule-A (JAM-A)

Junctional adhesion molecule-A (JAM-A) is a transmembrane glycoprotein and a member of the immunoglobulin superfamily, broadly expressed in epithelial and endothelial cells, leukocytes, platelets, and other tissues[2][6]. It is composed of two extracellular immunoglobulin-like domains, a single transmembrane segment, and a short cytoplasmic tail with a PDZ-binding motif[1][3][6]. JAM-A is localized at tight junctions where it mediates homophilic and heterophilic cell-cell adhesion, playing essential roles in maintaining barrier integrity, regulating leukocyte transmigration, and orchestrating intracellular signaling through protein-protein interactions[1][2][6]. JAM-A participates in diverse processes including immune homeostasis, hemostasis, angiogenesis, and cell migration. It is implicated in various diseases, especially those involving barrier dysfunction and aberrant leukocyte infiltration, such as inflammation, atherosclerosis, cancer, and cardiovascular disease[1][3][7].

Other names

JAM-AJAM1CD321F11 receptorJAMAJunctional adhesion molecule 1

Antibody blockade can inhibit JAM-A-mediated leukocyte transmigration and modulate endothelial/epithelial barrier integrity[5][1]. Some research compounds may modulate JAM-A to alter immune or barrier functions.