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Interaction of fibronectin with cultured human endothelial cells:
characterization of the specific receptor
G Conforti, A Zanetti, S Colella, M Abbadini, PC Marchisio, R Pytela, F Giancotti, G Tarone, LR Languino and E Dejana
Istituto di Ricerche Farmacologiche "Mario Negri," Milano, Italy.
In this study we provide a characterization of the fibronectin (FN) binding
to endothelial cells (EC), and we identify the FN binding site on these
cells. 125I-FN binding to EC in suspension was time dependent and reached a
plateau at 4 h. Cold FN inhibited this interaction in a
concentration-dependent way, but vitronectin, fibrinogen, and IgG were
poorly effective. About 80% of the total FN associated to EC at the
equilibrium was specifically bound; of this, 60% was reversibly bound,
while 20% appeared to be internalized. The FN binding was saturable and an
apparent dissociation constant of about 0.23 x 10(-6) mol/L and a maximal
number of binding sites of about 9.8 x 10(5) was estimated from binding
isotherms. Autoradiography data showed that EC-associated 125I- FN was all
in high mol wt form that did not enter the gel. We then characterize the FN
receptor (FNR) in EC. An antiserum to the FNR isolated from human placenta
inhibited FN binding to EC by 89%, and using the immunoblotting technique,
it recognized two bands in the EC detergent extract of mol wt 125/160 Kd.
This antiserum also recognized the EC membrane protein complex eluted from
the FN affinity column by an arg-gly-asp (RGD) peptide. When this complex
was included into liposomes, it poorly bound to FN. However, the binding
was strikingly increased by addition of Mn in the buffer and was specific
for FN in respect to other substrata. These data define the FN binding site
in EC and indicate that it is functionally and structurally related to that
isolated from human placenta.
Volume 73,
Issue 6,
pp. 1576-1585,
05/01/1989
Copyright © 1989 by The American Society of Hematology
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