Integrin alpha-V

Integrin alpha-V (ITGAV) is a transmembrane adhesion receptor that recognizes the R-G-D motif across multiple extracellular ligands including vitronectin, fibronectin, osteopontin, and thrombospondin (UniProt: P06756). In heterodimeric complexes with various beta integrins, ITGAV mediates cell adhesion, migration, and signaling. Notably, ITGAV:ITGB6 and ITGAV:ITGB8 heterodimers play a key role in transforming growth factor beta-1 (TGF-β1) activation by releasing it from latency-associated peptide, a process relevant to immune and fibrotic responses (UniProt: P06756).

ITGAV is broadly expressed across tissues and participates in developmental and vascular remodeling pathways. The protein also serves as an entry receptor for multiple viral pathogens including adenovirus, coxsackievirus, and herpes simplex virus, reflecting its widespread tissue distribution (UniProt: P06756).

In Alzheimer's disease, ITGAV shows elevated abundance in post-mortem AD brain tissue compared to age-matched controls, with a mean log2 fold-change of +0.80 (Chaparral AD proteomics). This upregulation suggests potential involvement in AD-related neuroinflammatory or neurovascular pathways, though the specific contribution to disease pathogenesis requires further investigation.