Integrin alpha-5 (ITGA5)

Integrin alpha-5 (ITGA5) is a cell surface receptor protein encoded by the ITGA5 gene, belonging to the integrin alpha chain family. Integrins are transmembrane heterodimeric proteins composed of alpha and beta subunits; integrin alpha-5 primarily pairs with beta-1 (ITGB1) to form the fibronectin receptor (also known as very late activation protein 5, VLA-5)[2][4]. This complex recognizes RGD-motif ligands such as fibronectin and fibrinogen, mediating cell–extracellular matrix adhesion and intracellular signaling events. ITGA5 regulates essential functions including cell migration, proliferation, differentiation (notably in bone and adipose tissues), and angiogenesis, and is implicated in various pathologies including cancer progression, cardiovascular remodeling, and infectious disease mechanisms[1][3][4]. High ITGA5 expression correlates with tumor invasiveness and poor prognosis in certain cancers[1][4]. Therapeutically, ITGA5 is being investigated as a drug target for conditions ranging from cancer to tissue repair, but clinical translation faces challenges due to roles in normal tissue functions and potential safety concerns.

Other names

Integrin alpha-5 heavy chainIntegrin alpha-5 light chainFNRACD49eCD49 antigen-like family member EFibronectin receptor subunit alphaIntegrin alpha-FVLA-5fibronectin receptor, alpha polypeptideVLA5AITGA5/SLC9B1 fusionvery late activation protein 5, alpha subunit

Inhibition of integrin–ligand binding (blocking RGD-motif ligand recognition, e.g., fibronectin, fibrinogen), Interference with adhesion signaling, Modulation of cell migration and survival