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(Received for publication, June 6, 1996, and in revised form, December 10, 1996)
From the Previous studies have shown that fibrinogen can
associate with endothelial cells via an Arg-Gly-Asp (RGD) recognition
specificity. In the present study, we have characterized the
specificity of fibrinogen binding to endothelial cells under different
cation conditions. Fibrinogen binding to suspended endothelial cells was selectively supported by Mn2+ and was suppressed by
Ca2+. The Mn2+-supported interaction was
completely inhibited by RGD peptides but not by
Volume 272, Number 8,
Issue of February 21, 1997
pp. 5360-5366
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
5
1 on Endothelial Cells
,
Joseph J. Jacobs Center for Thrombosis and
Vascular Biology, Department of Molecular Cardiology, The Cleveland
Clinic Foundation, Cleveland, Ohio 44195 and the
§ Department of Dermatology, State University of New York,
Stony Brook, New York 11794-8165
v
3 blocking monoclonal antibodies. In
contrast, the interaction was completely blocked by two
51 monoclonal antibodies. This
interaction was not mediated by fibronectin bound to the integrin;
could be demonstrated with purified 51;
and also was observed with a second
51-bearing cell type, platelets. The binding of fibrinogen to 51 on
endothelial cells in the presence of Mn2+ was
time-dependent, specific, saturable, and of high affinity (Kd = 65 nM). By employing anti-peptide
monoclonal antibodies, the carboxyl-terminal RGD sequence at A
572-574 was implicated in fibrinogen recognition by
51. Two circumstances were identified in
which 51 interacted with fibrinogen in
the presence of Ca2+: when the receptor was activated with
monoclonal antibody (8A2) or when the fibrinogen was presented as an
immobilized substratum. These results identify fibrinogen as a ligand
for 51 on endothelial and other cells, an
interaction which may have broad biological implications.
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