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Studies on the mechanism of expression of secreted fibrinogen on the
surface of activated human platelets
C Legrand, V Dubernard and AT Nurden
Laboratoire d'Hemostase et de Thrombose Experimentale, Hopital
Lariboisiere, Paris, France.
Affinity purified anti-fibrinogen (anti-Fg) Fab fragments were used to
study the mechanism of expression of alpha-granule fibrinogen on activated
platelets. Low amounts of the radiolabeled anti-Fg Fab bound to
unstimulated or adenosine diphosphate (ADP)-stimulated cells. They readily
bound to platelets stimulated with collagen, alpha-thrombin or
gamma-thrombin in the presence of divalent cations. At 1 n mol/L alpha-
thrombin or 25 nmol/L gamma-thrombin, platelet fibrinogen was expressed on
the surface of the cells notwithstanding the presence of AP-2, a monoclonal
antibody to the glycoprotein (GP) IIb-IIIa complex, or the synthetic
peptides Arg-Gly-Asp-Ser and gamma 400-411, all substances that prevented
the binding of plasma fibrinogen to platelets. These results suggest that
platelet fibrinogen may interact with its receptors during its
translocation from the alpha-granules to the plasma membrane and, thus, not
occupy the same sites as those available for plasma fibrinogen on the
surface of the cell. Furthermore, we found that platelet fibrinogen was
expressed on the thrombin-stimulated platelets of a Glanzmann's
thrombasthenia variant that failed to bind plasma fibrinogen. Normal
platelets stimulated with 5 nmol/L alpha- thrombin bound increased amounts
of the anti-fg Fab, the additional expression being inhibited by the
anti-GP IIb-IIIa monoclonal antibody or by Gly-Pro-Arg-Pro, an inhibitor of
fibrin polymer formation. This suggests that rebinding to externally
located GP IIb-IIIa complexes becomes important once fibrin is formed.
Volume 73,
Issue 5,
pp. 1226-1234,
04/01/1989
Copyright © 1989 by The American Society of Hematology
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