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PMID: 1374069 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Journal of cell biology ·Vol. 117 ·No. 3 ·1992-05-00 ·Pages 659-70

Arroyo AG, Sánchez-Mateos P, Campanero MR, Martín-Padura I, Dejana E, Sánchez-Madrid F

Abstract

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

MeSH Terms
Animals Antibodies, Monoclonal/metabolism Antigens, Surface/immunology,metabolism Antiporters Carrier Proteins/metabolism Cell Adhesion/physiology Cell Adhesion Molecules/metabolism Cell Communication/physiology Collagen/metabolism Cytoskeleton/ultrastructure Fibronectins/metabolism Integrins/immunology,metabolism Ligands Morphogenesis/physiology T-Lymphocytes/physiology Tumor Cells, Cultured Up-Regulation Vascular Cell Adhesion Molecule-1
Chemicals
Antibodies, Monoclonal Antigens, Surface Antiporters Carrier Proteins Cell Adhesion Molecules Fibronectins Integrins Ligands Vascular Cell Adhesion Molecule-1 Collagen
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Arroyo A G
Hospital de la Princesa, Universidad Autónoma de Madrid, Spain.
Sánchez-Mateos P
Campanero M R
Martín-Padura I
Dejana E
Sánchez-Madrid F
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.117.3.659
Published
1992-05-00
Pages
659-70
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289434
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.117.3.659 PMC Full Text View journal details
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