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Fibrinogen-endothelial cell interaction in vitro: a pathway mediated by an
Arg-Gly-Asp recognition specificity
LR Languino, S Colella, A Zanetti, A Andrieux, JJ Ryckewaert, MH Charon, PC Marchisio, EF Plow, MH Ginsberg and G Marguerie
Institute of Pharmacological Research Mario Negri, Milan, Italy.
It has been previously shown that fibrinogen (FG) associates specifically
with human umbilical vein and bovine aortic endothelial cells (EC) in
culture and induces EC migration. In the present study, we have
investigated whether the FG-EC interaction is mediated by an Arg-Gly-Asp
(RGD) recognition specificity and whether EC membrane proteins related to
platelet GPIIb-IIIa are involved. Highly purified radioiodinated human FG,
containing no detectable fibronectin, interacted with cultured human and
bovine EC in suspension in a time- dependent and specific manner. The
binding was inhibited by EDTA. Two polyclonal antibodies to platelet
GPIIb-IIIa, which immunoprecipitated a heterodimer molecule from EC,
inhibited FG binding to EC. These same antibodies inhibited FG-induced EC
migration in a dose-dependent manner as measured in a Boyden chamber.
Preabsorption of the antibodies with purified platelet GPIIb-IIIa markedly
reduced both inhibitory activities. A series of synthetic RGD-containing
peptides inhibited FG binding to EC and FG-induced EC migration.
Gly-Arg-Gly-Asp (GRGD) was the most active peptide tested in inhibiting FG
binding and EC migration (ID50 of 30 microM), and conservative
substitutions in the RGD sequence markedly reduced inhibitory activity
(ID50 greater than 1,000 microM). These results indicate that FG binding
and EC migration are events mediated by an RGD recognition specificity and
that EC surface proteins immunologically related to the GPIIb-IIIa complex
on platelets are involved in this recognition.
Volume 73,
Issue 3,
pp. 734-742,
02/15/1989
Copyright © 1989 by The American Society of Hematology
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