| Modification Notes |
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. Integrin ∫L1 (integrin, beta-like 1), also known as OSCP (osteoblast-specific cysteine-rich protein), TIED (ten integrin EGF-like repeat domain-containing protein) or ITGBL1, is a 494 amino acid secreted protein that is widely expressed in many tissues, but readily detectable only in aorta. Integrin ∫L1 contains ten tandem EGF-like repeats that are similar to those found in the cysteine rich 'stalk-like' structure of integrin beta-subunits. |