| Modification Notes |
Integrins are heterodimers composed of noncovalently associated transmembrane å and ∫ subunits. The 16 å and 8 ∫ subunits heterodimerize to produce more than 20 different receptors. Most integrin receptors bind ligands that are components of the extracellular matrix, including fibronectin, collagen and vitronectin. Certain integrins can also bind to soluble ligands such as fibrinogen, or to counterreceptors on adjacent cells such as the intracellular adhesion molecules (ICAMs), leading to aggregation of cells. Ligands serve to cross-link or cluster integrins by binding to adjacent integrin receptors; both receptor clustering and ligand occupancy are necessary for the activation of integrin-mediated responses. In addition to mediating cell adhesion and cytoskeletal organization, integrins function as signaling receptors. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis. The Integrin å3 chain, also known as very late (activation) antigen 3 (VLA-3), very common antigen 2 (VCA-2), extracellular matrix receptor 1 (ECMR1) and galactoprotein b3 (GAPB3), undergoes posttranslational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with ∫1 to form an integrin that interacts with many extracellular-matrix proteins. |
