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Thromb Haemost 1986; 56(03): 323-327
DOI: 10.1055/s-0038-1661676
Original Article
Schattauer GmbH Stuttgart

Further Characterization of Wheat Germ Agglutinin Interaction with Human Platelets: Exposure of Fibrinogen Receptors

Marilyne Lebret
The Laboratoire de Thrombose expérimentale et Hémostase, INSERM U 150, LA 334 CNRS, Hôpital Lariboisière, Paris, France
,
Francine Rendu
The Laboratoire de Thrombose expérimentale et Hémostase, INSERM U 150, LA 334 CNRS, Hôpital Lariboisière, Paris, France
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Publikationsverlauf

Received 21. Februar 1986

Accepted 05. September 1986

Publikationsdatum:
18. Juli 2018 (online)

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Summary

It was previously shown that (i) Wheat germ agglutinin, (WGA)-induced platelet activation occurred when only 17% of the lectin binding sites were occupied on the platelet surface and (ii) WGA caused the release of a platelet constituent which in turn participates in the observed effect. We now further define the platelet activation induced by WGA: the lectin induces a binding of fibrinogen to specific surface receptors. 125I-fibrinogen binding increases with the WGA concentration from 5 to 15 ug/ ml. Binding occurs without addition of exogenous calcium; its analysis demonstrated 54000 sites with a Ka = 0.8 × 106 M-1, Addition of 1 mM Ca2+ enhances the 125I-fibrinogen binding and reveals a second class of sites with higher affinity (9200 sites, Ka = 0.17 x 108 M-1). This 125I-fibrinogen binding is totally abolished by EDTA, ATP and arginine, and inhibited by 75% by CP/CPK; cyclooxygenase inhibitors and PGE1 also reduce the fibrinogen binding. Thus the WGA-induced fibrinogen binding is (1) release-dependent and (2) responsible for the aggregation process but not for the agglutinating effect of the lectin.

Key words

WGA - Platelets - Release - Fibrinogen - Binding - Aggregation - Receptor
 

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