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Description

"Integrins are a family of dimeric, transmembrane proteins that mediate cell-cell and extracellular matrix adhesion. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis. The integrin family is composed of at least 15 alpha and 8 beta subunits that may form over twenty different alpha-beta non-covalently bound dimeric combinations on the cell surface. The alpha subunits all have some homology to each other, as do the beta subunits. Both of the subunits contribute to the binding of the ligand. Integrin alpha subunits contain seven weak sequence repeats in the N-terminal region, which may be important in ligand binding, and have been predicted to fold cooperatively into a single beta-propeller domain with seven beta-sheets. The alpha-3 subunit (CD49c) is highly concentrated in epithelial cells where it strongly adheres to Laminin-5 and Laminin-5 induced rapid adhesion can be blocked by antibodies against the alpha-3 integrin subunit. The alpha-3 subunit exists in two different splice variants, denoted as ""A"" and ""B"". The only difference that results from this differential splicing is a total change in the cytoplasmic domain, while the extracellular domain stays the same. Knock-out mice lacking this subunit show prenatal lethality and abnormalities in the kidneys."