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Clustering of vitronectin and RGD peptides on microspheres leads to
engagement of integrins on the luminal aspect of endothelial cell membrane
A Zanetti, G Conforti, S Hess, I Martin-Padura, E Ghibaudi, KT Preissner and E Dejana
Instituto di Ricerche Farmacologiche Mario Negri, Milano, Italy.
In previous work (Conforti et al, Blood 80:437, 1992), we have shown that
integrins in endothelial cells (EC) are not polarized to the basal cell
membrane, but are also exposed on the apical cell surface, in contact with
blood. Therefore, endothelial integrins might be available for binding
circulating plasma proteins. However soluble plasma vitronectin (vn) bound
very poorly to EC apical surface and this interaction was unaffected by
Arg-Gly-Asp (RGD) peptides or an anti- alpha v beta 3 serum. In contrast,
beads (diameter, 4.5 microns) coupled with plasma vn associated to EC
apical surface in a time- and concentration-dependent way. Addition of
antibodies directed to vn, alpha v beta 3, and RGD-containing peptides
blocked the interaction of vn beads with EC. In contrast, heparin and
antibodies directed to alpha v beta 5 and beta 1 integrin chain had no
effect. Beads coupled with Gly-Arg-Gly-Asp-Ser-Pro bound to the EC surface,
but not those coupled with Gly-Arg-Gly-Glu-Ser-Pro. This interaction was
blocked by alpha v beta 3 antibodies and RGD peptides, but not by alpha v
beta 5 antibody. Overall, these results indicate that luminal alpha v beta
3 retains its binding capacity for surface-linked vn and RGD-containing
ligands, but binding is observed only when the ligand is offered in a
clustered, multivalent form. We propose that when vn or RGD-containing
proteins are bound to circulating cells, they can act as bridging molecules
by promoting adhesion of the cells to the endothelium via apical integrins.
Volume 84,
Issue 4,
pp. 1116-1123,
08/15/1994
Copyright © 1994 by The American Society of Hematology
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