Abstract
Integrins are a family of alpha beta heterodimeric receptors that mediate cell-cell and cell-substratum interactions. Integrin binding to extracellular ligands regulates cell adhesion, shape, motility, intracellular signalling and gene expression. Mechanisms that regulate integrin function are, therefore, central to the participation of integrins in a diverse set of cellular events. Here we report the identification of TASC, a monoclonal antibody to a novel epitope on the integrin beta 1 subunit, which inhibits cell adhesion to vitronectin but promotes adhesion to laminin and collagen types I and IV. We show that developing retinal neurons that have lost responsiveness to laminin regain the ability to bind laminin in the presence of TASC. Thus, beta 1-class integrins are likely to occupy multiple affinity states that can be modulated at the cell surface.
MeSH Terms
Amino Acid Sequence
Animals
Antibodies, Monoclonal/immunology,pharmacology
Cattle
Cell Adhesion/drug effects
Chick Embryo
Collagen/metabolism
Epitopes/immunology
Glycoproteins/metabolism
Immunoblotting
Integrins/immunology,metabolism
Laminin/metabolism
Molecular Sequence Data
Molecular Weight
Neurons/metabolism
Peptide Fragments/pharmacology
Retina/cytology,embryology
Vitronectin
Chemicals
Antibodies, Monoclonal
Epitopes
Glycoproteins
Integrins
Laminin
Peptide Fragments
Vitronectin
Collagen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Neugebauer K M
Howard Hughes Medical Institute, San Francisco, California 94143-0724.
Reichardt L F
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