Integrin alpha V beta 6

Integrin alpha V beta 6 is an epithelium-restricted heterodimer of CD51 and beta-6 whose principal function is activation of latent TGF-beta-1. Binding of the RGD motif in the TGF-beta latency-associated peptide, together with cytoskeletal tension transmitted through the short beta-6 tail, releases active TGF-beta-1 at the cell surface. This mechanism controls wound repair and mucosal immunity and, when overactive, drives organ fibrosis; alpha V beta 6 antagonists are in clinical development for idiopathic pulmonary fibrosis. The receptor is normally scarce in adult airway epithelium but induced during injury, and it is overexpressed in pancreatic and other carcinomas. ITGB6 mutations cause amelogenesis imperfecta, a dental enamel defect.