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Description
CD49d (Anti-VLA-alpha-4) recognizes the 150-kDa alpha-chain of very-late antigen (VLA)-4, a member of the integrin family of cell adhesion molecules. VLA-4, like other integrins, is a noncovalently associated heterodimeric glycoprotein composed of alpha and beta subunits and is involved in cell-cell and cell-extracellular matrix interactions. The beta-chain of the VLA-4 complex is the CD29 antigen, a 130-kDa glycoprotein. The CD29 antigen, also known as the beta-1 subunit, is common to the VLA family of integrins. When acting as a matrix receptor, the CD49d antigen binds to CS-1, an alternatively spliced domain of fibronectin. When functioning as a cell receptor, the CD49d antigen binds to the vascular cell-adhesion molecule-1 (VCAM-1). The interaction between the CD49d antigen and VCAM-1 is known to play an important role in stabilizing the adhesion of lymphocytes to endothelial cells and in mediating B- lymphocyte precursor/bone marrow stromal cell adhesion. The CD49d antigen, when associated with the beta integrin, forms a lymphocyte homing receptor for Peyer's patch, binding to the mucosal vascular addressin MAdCAM-1. The CD49d antigen is also involved in CD3- dependent CD4+ T-lymphocyte activation via its interaction with fibronectin.