αvβ1

The integrin αvβ1 is a heterodimeric transmembrane receptor that mediates cell adhesion and extracellular matrix interactions, playing a critical role in tissue remodeling and fibrotic processes^[1][2][3]. Mechanistically, αvβ1 directly binds the latency-associated peptide of transforming growth factor-β1 (TGFβ1), facilitating TGFβ1 activation and promoting fibroblast differentiation in fibrotic tissues^[1][2]. In disease models, selective αvβ1 inhibition attenuates bleomycin-induced pulmonary fibrosis and carbon tetrachloride-induced liver fibrosis, demonstrating its therapeutic potential in fibrosis-associated pathologies^[1][3]. Compared with related isoforms such as αvβ3 and αvβ6, αvβ1 exhibits distinct ligand specificity and higher expression on activated fibroblasts, highlighting its unique functional profile^[4][1][2]. Structurally optimized small-molecule inhibitors, including azabenzimidazolone derivatives, achieve potent αvβ1 selectivity without substantially affecting other integrins, providing precise tools for experimental modulation of TGFβ1-mediated fibrotic signaling^[3]. Dual antagonists targeting αvβ1 and related integrins like α5β1 further enable the dissection of overlapping integrin pathways and the evaluation of combinatorial therapeutic strategies in airway hyperresponsiveness and fibrotic disease models^[5]. Collectively, these studies establish αvβ1 as a critical regulator of fibrotic signaling, distinguishable from other RGD-binding integrins, and underscore the utility of selective inhibitors in preclinical research and potential clinical translation^[1][2][3][5].