Thromb Haemost 1983; 50(02): 560-562
DOI: 10.1055/s-0038-1665255
Original Article
Schattauer GmbH Stuttgart

Interaction of Heparin with Histidine-Rich Glycoprotein and with Antithrombin III

H R Lijnen
The Center for Thrombosis and Vascular Research, Department of Medical Research, University of Leuven, Belgium
,
B van Hoef
The Center for Thrombosis and Vascular Research, Department of Medical Research, University of Leuven, Belgium
,
D Collen
The Center for Thrombosis and Vascular Research, Department of Medical Research, University of Leuven, Belgium
› Institutsangaben
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Publikationsverlauf

Received 25. April 1983

Accepted 07. Juni 1983

Publikationsdatum:
18. Juli 2018 (online)

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Summary

The interaction between heparin, histidine-rich glycoprotein and antithrombin III was studied in purified systems. Histidine- rich glycoprotein binds heparin and thereby interferes with its interaction with antithrombin III, resulting in neutralization of the anticoagulant activity. This interaction occurs with clinical grade heparin as well as with high affinity (for antithrombin III) heparin and with a high affinity heparin fragment with Mr. 4,300.

Low affinity heparin competes with high affinity heparin for the binding to histidine-rich glycoprotein which results in an apparent increase of the anticoagulant activity of high affinity heparin.

The interaction between heparin and histidine-rich glycoprotein is counteracted by Ca2+-binding anticoagulants, indicating that it is dependent on the presence of divalent metal ions. Ethylenediaminetetraacetate is a much more potent inhibitor of the interaction between heparin and histidine-rich glycoprotein than citrate.