Key result
α1-acid glycoprotein completely inhibits thrombin-induced human platelet aggregation at physiological concentrations.
α1-acid glycoprotein acts as an inhibitor of platelet aggregation induced by thrombin, epinephrine, and collagen in vitro.
Should not yet influence antiplatelet strategies; leaves open any in vivo antithrombotic role for α1-acid glycoprotein.
α1‐acid glycoprotein (α1‐acid GP) isolated from human plasma was found to inhibit thrombin‐induced aggregation of washed human platelets (final thrombin concentration 0.05 NIH U/ml), and inhibition was complete with physiological concentrations of the glycoprotein (1.0–1.5 g/l final conc.). The inhibitory effect seemed to occur immediately on thrombin addition, thus being similar to the effect of heparin previously observed. As opposed to heparin, however, α1‐acid GP did not affect spontaneous platelet aggregation. Furthermore, α1‐acid GP (in optimal concentrations) reduced the combined inhibitory effect of heparin and antithrombin III on thrombin‐induced platelet aggregation, thus being consistent with the previous findings using heparin thrombin clotting time. Snyder & Coodley (1976) found α1‐acid GP to inhibit platelet aggregation induced by epinephrine and adenosine diphosphate in platelet‐rich plasma. As we also found α1‐acid GP to inhibit collagen‐induced platelet aggregation, this acid glycoprotein may possibly act as an inhibitor of the release reaction although fairly high concentrations (10 mg/ml final conc.) were needed for complete inhibition.
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Andersen et al. (1980) studied In vitro platelet aggregation. α1-acid glycoprotein was evaluated on Thrombin-, epinephrine-, and collagen-induced platelet aggregation. α1-acid glycoprotein completely inhibited thrombin-induced human platelet aggregation at physiological concentrations (1.0–1.5 g/l) and also inhibited collagen-induced aggregation at higher doses.
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