Integrins are a family of dimeric proteins that mediate cell-to-cell and extracellular matrix adhesion. They consist of a large α chain that is non-covalently associated with a smaller β chain which is used to define integrin subfamilies. These molecules exhibit a wide range of expression throughout development and adulthood. VLA-2 (very late antigen), a member of the integrin superfamily, was identified on activated T cells, but has since been reported to be on various cell types. VLA-2 is reported to be a heterodimer of integrin α2 (CD49b) and integrin β1 (CD29) subunits. The α2 chain contains a large extracellular domain, a transmembrane domain, and a short cytoplasmic tail. VLA-2 functions as a collagen receptor on platelets and fibroblasts, as well as a collagen and laminin receptor on endothelial and epithelial cells. On activated T cells, VLA-2, like LFA-1, exhibits increased number and affinity of ligand binding. Interactions of these molecules with their extracellular matrix ligands is important for directing effector T cells to their target tissues and to provide co-stimulatory signals. Thus, VLA-2 not only plays an important role in cellular adhesion, but may function in intracellular signal transmission.