Integrin alpha-V beta-6 receptor (Integrin αvβ6)

Integrin alpha-V beta-6 (αvβ6 integrin) is a heterodimeric cell-surface receptor composed of the alpha-V (ITGAV) and beta-6 (ITGB6) subunits, both of which are type I transmembrane glycoproteins in the integrin superfamily[1][2][4]. The β6 subunit only associates with the αv subunit, creating a receptor highly specific for epithelial cells, and it is upregulated during development, wound healing, and in a wide range of cancers and tissue fibrosis[1][4][9]. Integrin αvβ6 binds extracellular matrix proteins containing the RGD motif (e.g., fibronectin, tenascin C) and is unique for its high-affinity, force-dependent activation of latent TGF-β, a crucial regulator of tissue homeostasis, fibrosis, and tumor progression[1][2][6][7][9]. Aberrant expression or activation of αvβ6 is implicated in pathological remodeling processes in cancer and fibrosis, making it a focus for targeted therapies, imaging, and biomarker strategies.

Other names

αvβ6 integrinIntegrin alpha V beta 6ITGAV-ITGB6

Antagonism of ligand binding (e.g., blocking αvβ6 interaction with the latency-associated peptide of TGF-β, preventing TGF-β activation) Inhibition of downstream profibrotic and pro-tumorigenic signaling pathways Imaging agents bind selectively for diagnostic visualization of αvβ6 expression