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J. Biol. Chem., Vol. 269, Issue 6, 4005-4011, 02, 1994
R Makarem, P Newham, JA Askari, LJ Green, J Clements, M Edwards, MJ Humphries and AP Mould
The integrin receptor alpha 4 beta 1 binds to two different ligands, the
extracellular matrix glycoprotein fibronectin and the endothelial cell
surface protein vascular cell adhesion molecule-1 (VCAM-1). Using probes
derived from each ligand and a variety of cell adhesion and ligand-receptor
binding assays, we have investigated the relationship between the
mechanisms of fibronectin and VCAM-1 interaction with alpha 4 beta 1. CS1
peptide, which represents the dominant active site from the HepII/IIICS
recognition domain in fibronectin, was found to inhibit VCAM-1-dependent
adhesion in three different assays: MOLT-4 T lymphoblastic leukaemia cell
attachment to immobilized recombinant soluble VCAM-1 (rsVCAM-1), MOLT-4
cell attachment to monolayers of VCAM- 1-transfected COS-1 cells, and
A375-SM melanoma cell spreading on immobilized rs VCAM-1. Half-maximal
inhibition required CS1 concentrations of 1.7-3.0 mg/ml, some 3-7-fold
higher than that needed to autoinhibit adhesion to CS1-IgG conjugate. Using
a more sensitive solid-phase receptor-ligand binding assay, CS1 was found
to be a potent inhibitor of the binding of rsVCAM-1 to alpha 4 beta 1
(half-maximal inhibition at 13 micrograms/ml). In agreement with cell-based
assays, severalfold lower concentrations of CS1 were required to inhibit
binding of recombinant HepII/IIICS region of fibronectin (half-maximal
inhibition at 3 micrograms/ml). VCAM-1-alpha 4 beta 1 binding was blocked
not only by CS1 peptide but also by the recombinant HepII/IIICS region of
fibronectin. Kinetic analysis of CS1 inhibition of VCAM-1 binding revealed
that it was directly competitive in nature, indicating that VCAM-1 and
fibronectin recognize either identical or spatially overlapping binding
sites on alpha 4 beta 1. The implications of these results for the future
design of VCAM-1 antagonists are discussed.
Competitive binding of vascular cell adhesion molecule-1 and the HepII/IIICS domain of fibronectin to the integrin alpha 4 beta 1
Department of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, United Kingdom.
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