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Integrin alpha 5 beta 1 (α5β1), also known as the fibronectin receptor, is a heterodimeric cell surface receptor composed of two subunits: α5 (ITGA5/CD49e) and β1 (ITGB1/CD29). It mediates cell-extracellular matrix (ECM) adhesion and plays critical roles in cellular signaling, migration, proliferation, survival, and differentiation. It primarily binds fibronectin via the RGD motif and is implicated in cancer metastasis, angiogenesis, and wound healing. It functions by triggering downstream signalling cascades involving kinases, leading to cytoskeletal reorganisation.
Inhibition of α5β1 binding to fibronectin, disruption of focal adhesion signaling, modulation of downstream kinase activity (e.g., FAK/Src), interference with actin cytoskeleton reorganization
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