Regulation of the VLA integrin-ligand interactions through the beta 1 subunit.

• DOI: 10.1083/jcb.117.3.659
• Publication Date: 2004-05-15T00:22:22Z
• Authors: A G Arroyo; P Sánchez-Mateos; M R Campanero; I Martín-Padura; E Dejana; F Sánchez-Madrid
• Keywords: CD49c; BETA (programming language)

Integrins from the very late activation antigen (VLA) subfamily are involved in cellular attachment to extracellular matrix (ECM) proteins and intercellular adhesions. It is known that interaction of integrin with their ligands can be regulated during activation. We have investigated regulation different VLA-mediated adhesive interactions through common beta 1 chain. found certain anti-beta antibodies strongly enhance binding myelomonocytic U-937 cells fibronectin. This 1-mediated regulatory effect both VLA-4 VLA-5 fibronectin receptors. Moreover, mAb also induced VLA-4-mediated a recombinant soluble form its endothelial cell ligand VCAM-1. Non-activated peripheral blood T lymphocytes, unable mediate or VCAM-1, acquired ability bind these presence mAb. The changes affinities for were comparable those triggered by lymphocyte agents such as anti-CD3 phorbol ester. Adhesion melanoma other ECM laminin collagen well alpha 2-transfected K-562 collagen, was enhanced These effects on VLA-ligand do not involve surface membrane expression VLA heterodimers. functional required an active metabolism, cytoskeleton integrity existence physiological levels intracellular calcium Na+/H+ antiporter. Beta only increased but promoted spreading cytoplasmic extension plates coated either fibronectin, rapid appearance microspikes cytoskeletal protein talin colocalized microspikes. results emphasize central role chain regulating functions mediated integrins morphology.