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Vol. 8, Issue 12, 2449-2461, December 1997
v
3 Integrin Mediates the
Cell-adhesive Capacity and Biological Activity of Basic Fibroblast
Growth Factor (FGF-2) in Cultured Endothelial Cells
Unit of General Pathology and Immunology, Department of
Biomedical Sciences and Biotechnology, School of Medicine, University
of Brescia, 25123 Brescia, Italy
Fibroblast growth factor-2 (FGF-2) immobilized on
non-tissue culture plastic promotes adhesion and spreading of bovine
and human endothelial cells that are inhibited by anti-FGF-2 antibody. Heat-inactivated FGF-2 retains its cell-adhesive activity despite its
incapacity to bind to tyrosine-kinase FGF receptors or to cell-surface
heparan sulfate proteoglycans. Recombinant
glutathione-S-transferase-FGF-2 chimeras and synthetic
FGF-2 fragments identify two cell-adhesive domains in FGF-2
corresponding to amino acid sequences 38-61 and 82-101. Both regions
are distinct from the FGF-receptor-binding domain of FGF-2 and contain
a DGR sequence that is the inverse of the RGD cell-recognition
sequence. Calcium deprivation, RGD-containing eptapeptides, soluble
vitronectin (VN), but not fibronectin (FN), inhibit cell adhesion to
FGF-2. Conversely, soluble FGF-2 prevents cell adhesion to VN but not
FN, thus implicating VN receptor in the cell-adhesive activity of
FGF-2. Accordingly, monoclonal and polyclonal
anti-
v
3 antibodies prevent cell adhesion
to FGF-2. Also, purified human v3 binds
to immobilized FGF-2 in a cation-dependent manner, and this interaction
is competed by soluble VN but not by soluble FN. Finally,
anti-v3 monoclonal and polyclonal
antibodies specifically inhibit mitogenesis and urokinase-type
plasminogen activator (uPA) up-regulation induced by free FGF-2 in
endothelial cells adherent to tissue culture plastic. These data
demonstrate that FGF-2 interacts with v3
integrin and that this interaction mediates the capacity of the
angiogenic growth factor to induce cell adhesion, mitogenesis, and uPA
up-regulation in endothelial cells.
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