Premium
Functional regulation of the human integrin VLA‐1 (CD49a/CD29) by divalent cations and stimulatory β1 antibodies
Author(s) -
Alfonso Luque,
Francisco SánchezMadrid,
Carlos Cabañas
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00490-0
Subject(s) - integrin , monoclonal antibody , chemistry , divalent , adhesion , extracellular , cell adhesion , microbiology and biotechnology , collagen receptor , antibody , biochemistry , cell , biology , immunology , organic chemistry
We have investigated the regulation by divalent cations Mg 2+ , Ca 2+ and Mn 2+ of the functional activity of the human integrin VLA‐1 expressed on neuroblastoma NB100 cells. VLA‐1‐mediated adhesion of NB100 cells to ligand collagen type I was supported by either mM concentrations of extracellular Mg 2+ or μM levels of Mn 2+ . In contrast, Ca 2+ alone did not induce activation of VLA‐1 but exerted a potent inhibitory effect on the Mg 2+ ‐supported cell adhesion. We have also demonstrated that VLA‐1 can be directly activated by the stimulatory monoclonal antibody TS2/16 specific for the integrin β1 subunit, resulting in effective adhesion of NB100 cells to type I collagen. This study has been possible by using a novel blocking VLA‐α1 specific monoclonal antibody, 5E8D9.