Interaction of β₂-Glycoprotein-I with Human Blood Platelets: Influence Upon the ADP-Induced Aggregation

Summary

The interaction of β₂-glycoprotein-I (β₂-G-I), a plasma constituent of unknown function, with blood platelets was studied. The following results were obtained: 1) β₂-G-I binds to washed human platelets isolated by centrifugation (WP) at one kind of specific, saturable binding sites. The dissociation constant was found to be approx. 1 × 10⁻⁶M.

2) In the presence of physiological concentrations of Ca⁺⁺ (2.5 mM), this specific binding is markedly reduced. Unspecific binding of β₂-G-I to platelets, however, is not influenced by Ca⁺⁺.

3) Platelets prepared by gel filtration (GFP), differing in their in vitro aggregability from WP, exhibit no specific binding of β₂-G-I. Binding to GFP is also not induced by activation with thrombin, collagen or ADP.

4) β₂-G-I causes significant alteration of the ADP-induced aggregation of GFP. Aggregation induced by thrombin, collagen, arachidonic acid or PAF-acether, however is not altered by β₂G-I.

It is suggested, that pelleting during centrifugation causes irreversible rearrangements in the membrane of platelets.

Keywords

β₂-glycoprotein-I - Platelets - ADP-aggregation

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