Galactose-specific lectin from VISCUM ALBUM as a mediator of aggregation and priming of human platelets

Journal/Book: Anticancer Res. 15 (2), 361-367. 1995;

Abstract: Galactose-specific lectin from Viscum album (VAA) was found to induceaggregation of human platelets in a dose- and sugar-dependent manner.Small nonaggregating concentrations of VAA primed the response ofplatelets to known aggregants (ADP, arachidonic acid, thrombin,ristocetin, and A23187). VAA-induced platelet aggregation was completelyreversible by addition of the sugar inhibitor lactose and the plateletsfrom disrupted aggregates maintained the response to other aggregants.The lectin-induced aggregation of washed platelets was more resistant tometabolic inhibitors than thrombin- or arachidonic acid-dependent cellinteraction. In contrast to the related galactose-specific lectin fromRicinus communis and the soy bean agglutinin, the lectin did notaggregate liposomes prepared from total platelet lipids, indicatingdifferent affinities of aggregation-mediating lectins to plateletglycolipids. Author.

Keyword(s): ARACHIDONIC-ACID/PD (pharmacology)

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