Basal cell adhesion molecule (BCAM)

Basal cell adhesion molecule (BCAM), also known as Lutheran antigen and CD239, is a transmembrane glycoprotein of the immunoglobulin superfamily that functions as both an adhesion molecule and a receptor for extracellular matrix proteins, most notably laminin alpha-5. BCAM plays a crucial role in cell adhesion, motility, migration, and invasion, and is involved in physiological processes such as erythrocyte and epithelial cell adhesion. It is implicated in the pathogenesis of several diseases, including the promotion of metastasis in cancers (notably ovarian and bladder cancer), vaso-occlusion in sickle cell disease, and immune-related conditions like glomerulonephritis. BCAM polymorphisms define Lutheran blood group antigens and variants. The molecule contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short cytoplasmic tail, and can signal intracellularly via pathways such as JAK2/Rap1/AKT[1][2][3][5][6].

Other names

Basel cell adhesion moleculeLutheran antigenLUCD239MSK19B-CAMAuberger B antigenLutheran blood group glycoproteinF8/G253 antigenAU

Not directly established for approved drugs; potential blocking of BCAM-laminin interaction could disrupt cell adhesion and migration in cancer or sickle cell disease (inferred)