Thromb Haemost 2002; 87(03): 502-508
DOI: 10.1055/s-0037-1613031
Review Article
Schattauer GmbH

Immunoglobulin G from Patients with Antiphospholipid Syndrome Impairs the Fibrin Dissolution with Plasmin

Krasimir Kolev
1   Semmelweis University, Department of Medical Biochemistry
,
Judit Gombás
1   Semmelweis University, Department of Medical Biochemistry
,
Balázs Váradi
1   Semmelweis University, Department of Medical Biochemistry
,
Judit Skopá
2   National Stroke Center
,
Katalin Mede
2   National Stroke Center
,
Ervin Pitlik
3   Semme lweis University, 2nd Department of Internal Medicine, Budapest, Hungary
,
Zoltán Nagy
2   National Stroke Center
,
Raymund Machovich
1   Semmelweis University, Department of Medical Biochemistry
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Received 12. Juni 2001

Accepted after resubmission 28. November 2001

Publikationsdatum:
14. Dezember 2017 (online)

Summary

Immunoglobulin G (IgG) isolated from normal human blood plasma stabilizes the structure of perfused crosslinked fibrin and prolongs the time for its dissolution with plasmin, when the fibrin surface is exposed to 500 s-1 shear rate flow. The IgG from patients suffering in antiphospholipid syndrome with thrombotic complications exerts even stronger antifibrinolytic effect. A patient, whose IgG does not affect the fibrin dissolution with plasmin, displays a bleeding tendency. The shear stress-induced disassembly of the fibrin clots containing IgGs with antifibrinolytic potency occurs at a much more advanced stage of fibrin digestion, as evidenced by the electrophoretic pattern of the ureatreated samples. The antifibrinolytic effects are also produced under static conditions and these are caused by the variable portion of the IgG molecules (fragment Fab), whereas the constant part (fragment Fc) has no inhibitory effect. The IgGs with antifibrinolytic properties do not affect directly the plasmin activity in amidolytic assay, but the IgGs from APS patients obliterate the competition of the fibrin and the peptidyl-p-nitroanilide for the protease in the same assay system suggesting interference of the IgGs with the plasmin action on the fibrin substrate. Thus, the correlation of the clinical symptoms with the effect of the isolated IgG on the dissolution of perfused fibrin clots supports a physiological and a pathological role of IgG in the fibrinolytic process related to the variability of the cross-reactions of immunoglobulins with fibrin, fibrin degradation products or fibrin-plasmin complexes.