Abstract Title:

Interaction of wheat germ agglutinin and concanavalin A with platelets. Stimulation of platelet functional reactions and binding with membrane glycoproteins.

Abstract Source:

Biochemistry (Mosc). 1998 Jun;63(6):710-8. PMID: 9668212

Abstract Author(s):

I V Smirnova, S G Khaspekova, V V Ignatov, A V Mazurov

Article Affiliation:

Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, Saratov, 410015, Russia.


Effects of two lectins, wheat germ agglutinin (WGA) and concanavalin A (Con A), on platelet functional reactions and interaction of lectins with the platelet membrane glycoproteins (GPs) have been studied. Both lectins stimulated platelet aggregation and secretion of serotonin from platelet dense granules. The effects of WGA and Con A were blocked by specific sugars, N-acetyl-D-glucosamine and alpha-methyl-D-mannopyranoside, respectively, by adenylate cyclase activator prostaglandin E1, and by anti-GP IIb-IIIa monoclonal antibody (monAB), CRC64, that inhibits platelet interaction with fibrinogen. The data indicate that both lectins interacting with the carbohydrate moiety on the platelet surface stimulated not passive agglutination but fibrinogen--GP IIb-IIIa-dependent platelet aggregation which is coupled with the secretion from granules and activation of the intracellular systems of signal transduction. However, there were significant differences between the stimulatory effects of WGA and Con A. WGA induced more pronounced and quick platelet aggregation and stimulated several times higher serotonin secretion than Con A. In addition, adhesion studies showed that plastic-adsorbed WGA appeared to be a nonadhesive substrate, whereas Con A effectively stimulated platelet adhesion. Unlike Con A-induced platelet aggregation, adhesion to Con A substrate was not inhibited by monAB CRC64, i.e., was not dependent on GP IIb-IIIa--fibrinogen interaction. Binding of lectins with major platelet GPs was studied using immobilized WGA and Con A and platelet lysate as a source of GPs. Platelet lysate was incubated with immobilized lectins and then binding of individual GPs was evaluated using specific mono- and polyclonal antibodies. WGA binds with GP Ib and P-selectin but not with other GPs tested. Interaction of Con A with platelet GPs was less specific. This lectin binds with GP IIb-IIIa, GP Ib, GP IV, and P-selectin. Although GP Ib appeared to be the main protein which bound WGA on platelet surface, anti-GP Ib antibodies failed to affect WGA-induced platelet aggregation, but inhibited WGA-induced agglutination of fixed platelets. Thus, interaction of the WGA with GP Ib could not be considered as a major stimulus initiating WGA-dependent platelet activation and aggregation.

Study Type : In Vitro Study

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