Histidine-Rich Glycoprotein Modulates the Anticoagulant Activity of Heparin in Human Plasma
- 1 January 1984
- journal article
- research article
- Published by Georg Thieme Verlag KG in Thrombosis and Haemostasis
- Vol. 51 (02) , 266-268
- https://doi.org/10.1055/s-0038-1661073
Abstract
Addition of 0.05 IU of heparin per ml normal plasma prolongs its thrombin time from 20 to 27s, but that of plasma specifically depleted in histidine-rich glycoprotein (by immunoadsorption) from 20 to 180s. Reconstitution of the depleted plasma with normal plasma or with purified histidine-rich glycoprotein normalizes its thrombin time. In 54 plasma samples from hospitalized patients a significant negative correlation was found between the anticoagulant activity of heparin measured by thrombin inhibition and the plasma level of histidine-rich glycoprotein (r = 0.69). It is concluded that the level of histidine-rich glycoprotein modulates the anticoagulant activity of heparin in human plasma to an extent which appears to be pharmacologically and possibly clinically relevant.Keywords
This publication has 7 references indexed in Scilit:
- Heparin binding properties of human histidine-rich glycoprotein. Mechanism and role in the neutralization of heparin in plasma.Journal of Biological Chemistry, 1983
- Physicochemical, immunochemical and functional comparison of human histidine-rich glycoprotein and autorosette inhibition factorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Interaction of Heparin with Histidine-Rich Glycoprotein and with Antithrombin IIIThrombosis and Haemostasis, 1983
- Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma.Journal of Biological Chemistry, 1982
- Fractionation of low molecular weight heparin species and their interaction with antithrombin.Journal of Biological Chemistry, 1979
- The separation of active and inactive forms of heparinBiochemical and Biophysical Research Communications, 1976
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951