Integrin alpha V beta 8 is one of five alpha V integrins, is expressed in yolk sac, placenta, brain perivascular astrocytes, Schwann cells, renal glomerular mesangial cells and pulmonary epithelial cells. Unlike other alpha V integrins, ITGAVB8 does not appear to assume different activation states, and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif, including vitronectin, fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP, which releases active TGF-beta. This mechanism differs from that of alpha V beta 6, the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms. Downstream effects of TGF-beta activation include control of cell growth and associated vascularization. Deletion of either alpha V or beta 8 reveals that alpha V beta 8 is required for vascular morphogenesis in the embryonic brain and yolk sac.
Greater than 95% as determined by reducing SDS-PAGE
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