Effect of Antiphospholipid Antibodies on β2Glycoprotein I-Phospholipid Interaction
Article first published online: 6 SEP 2011
American Journal of Reproductive Immunology
Volume 39, Issue 5, pages 310–315, May 1998
How to Cite
(1998), Effect of Antiphospholipid Antibodies on β2Glycoprotein I-Phospholipid Interaction. American Journal of Reproductive Immunology, 39: 310–315. doi: 10.1111/j.1600-0897.1998.tb00523.x
- Issue published online: 6 SEP 2011
- Article first published online: 6 SEP 2011
- accepted November 21, 1997
- antiphospholipid syndrome;
- recurrent fetal death;
- systemic lupus erythematosus;
PROBLEM: β2 glycoprotein I (β2GPI) physiologically binds to negatively charged phospholipids (PLs) and is a natural regulator of the coagulation cascade. Thrombotic clinical complications and recurrent fetal loss associated with autoimmune antiphospholipid (aPL) antibodies are thought to be related to their binding to β2GPI-PL complex and interference with the physiological function of β2GPI.
METHOD OF STUDY: To investigate the effect of aPL on β2GPI-PL interaction, we studied the binding of biotinylated β2GPI to cardiolipin (CL) by enzyme-linked immunosorbent assay (ELISA) in the presence and absence of purified aPL immunoglobulin G (IgG) antibodies.
RESULTS: Adding five different aPL IgG antibodies with different levels of aPL activity isolated from the sera of five patients with aPL-associated recurrent fetal death greatly increased the binding of biotinylated β2GPI to CL-coated plates. The optical densities (ODs) were 0.635, 0.890, and 1.265 in the presence of three aPL IgG antibodies, compared to 0.425 in the absence of aPL IgG. In contrast, normal human IgG had no enhancing effect. The OD was 0.480 and 0.425, respectively. The enhancement of β2GPI binding to CL by aPL IgG correlated with the titers of aPL antibodies. The use of phosphate-buffered saline with increasing salt concentrations as a washing buffer for the ELISA resulted in more stable binding of β2GPI to PL in the presence of aPL IgG.
CONCLUSIONS: These findings suggest that the binding of autoimmune aPL antibodies to β2GPI-PL complex results in abnormally tighter interaction between β2GPI and PLs, which may lead to physiological dysfunction of β2GPI as a regulator of coagulation.