ITGAV+ITGB3

Integrins are heterodimeric transmembrane receptors, formed from 18 alpha- and 8 beta subunits, capable of dimerizing to form 24 different heterodimer combinations that can bind to numerous extracellular ligands including a variety of extracellular matrix (ECM) proteins.

Integrin alpha V (ITGAV) is a protein-coding gene and is located on chromosome 2q31-q32. In mammals, ITGAV can form a heterodimer with b chains 1,3,5,6, and 8. ITGAV also binds to Arg–Gly–Asp (RGD) motif of fibronectin, vitronectin, osteopontin as well as latency-associated peptide (LAP) of transforming growth factor (TGF)-β1 or -β3.

ITGAV has been shown to play an important role in the regulation of cancer growth and metastasis. Especially the ITGAV/ITGB3 heterodimer has been connected with tumor neoangiogenesis via high levels of bFGF and tumor-necrosis factor α (TNFA) whereas the ITGAV/ITGB1 receptor is implicated in tumor cell proliferation via BCL2 and p53 activity.

The integrin alpha V beta 3, also known as the vitronectin receptor, consists of a 125 kDa alpha V subunit and a 105 kDa beta 3 subunit. It has been the focus of intensive research because of its major role in several distinct processes, particularly osteoclast-mediated bone resorption, angiogenesis and pathological neovascularisation, and tumour metastasis.