Thromb Haemost 1991; 66(06): 666-671
DOI: 10.1055/s-0038-1646483
Original Article
Schattauer GmbH Stuttgart

In Vitro Studies of Antiphospholipid Antibodies and Its Cofactor, β2-Glycoprotein I, Show Negligible Effects on Endothelial Cell Mediated Protein C Activation

Janine D Oosting
1   The Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands
2   The Department of Internal Medicine (Division of Immunopathology), University Hospital Utrecht, Utrecht, The Netherlands
,
Ronald H W M Derksen
2   The Department of Internal Medicine (Division of Immunopathology), University Hospital Utrecht, Utrecht, The Netherlands
,
Tilman M Hackeng
1   The Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands
,
Marja van Vliet
1   The Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands
2   The Department of Internal Medicine (Division of Immunopathology), University Hospital Utrecht, Utrecht, The Netherlands
,
Klaus T Preissner
The Department of Haemostasis Research, Max Planck Gesellschaft, Bad Nauheim, Federal Republic of Germany
,
Bonno N Bouma
1   The Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands
,
Philip G de Groot
1   The Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands
› Author Affiliations
Further Information

Publication History

Received 26 February 1991

Accepted 10 June 1991

Publication Date:
26 July 2018 (online)

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Summary

The effect of sera and purified IgG isolated from plasma of 46 patients with systemic lupus erythematosus (SLE) and 9 healthy donors on the endothelial cell (EC) mediated protein C activation was investigated. Out of the 46 SLE sera used, 19 were antiphospholipid antibodies (aPL) positive. From 12 patients IgG was isolated, of which 6 contained aPL. EC were first incubated with IgG (7 mg/ml) or serum (1: 1 diluted) for 1 h and then tested for their ability to promote protein C activation by thrombin, with the cells either in a monolayer or in a suspension. The normal range (mean of control values ± 2 SD) of protein C activation was 80-120%. In contrast to others, we could not detect an inhibition of protein C activation by any of the patient IgG's or sera.

The recently described cofactor for binding of antiphospholipid antibodies to phospholipids, β2-glycoprotein I, was purified and added to the purified IgG's. A combination of these two components did not inhibit the EC mediated protein C activation by thrombin.

This study suggests that the inhibition of the protein C activation, mediated by EC, is not a general mechanism by which aPL related thrombosis can be explained.