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Correlation between fibrinogen binding to human platelets and platelet
aggregability
EI Peerschke, MB Zucker, RA Grant, JJ Egan and MM Johnson
Fibrinogen is essential for aggregating platelets with adenosine
diphosphate (ADP) and was recently shown to bind to platelets stimulated
with ADP. The present work confirms the specific and saturable nature of
the platelet-fibrinogen interaction. Binding of 125iodine-labeled
fibrinogen to human gel-filtered platelts was maximal at 1 min, and the
receptors were saturated when the fibrinogen concentration in the
suspending medium approached 0.8 mg/ml. Assuming that one fibrinogen
molecule interacts with a single receptor, experiments with 9 normal donors
revealed the presence of 12,896 +/- 2456 receptors per platelet. Much of
the bound material dissociated from platelets after incubation with apyrase
or EDTA. Binding was markedly inhibited at pH 6.5, in the presence of EDTA,
and with platelets from 3 thrombasthenic patients but not with those from a
patient with the Bernard-Soulier syndrome. Fibrinogen binding was also
virtually absent with platelets that had been incubated with EDTA for 8 min
at 37 degrees C and pH 7.8. These platelets could not aggregate when mixed
with ADP and adequate CaCl2 and fibrinogen, although they could still
change their shape. Thus, ADP-induced binding of fibrinogen correlates with
platelet aggregability.
Volume 55,
Issue 5,
pp. 841-847,
05/01/1980
Copyright © 1980 by The American Society of Hematology
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