β2-Glycoprotein i reactivity of monoclonal anticardiolipin antibodies from patients with the antiphospholipid syndrome
Article first published online: 9 DEC 2005
Copyright © 1994 American College of Rheumatology
Arthritis & Rheumatism
Volume 37, Issue 10, pages 1453–1461, October 1994
How to Cite
Ichikawa, K., Khamashta, M. A., Koike, T., Matsuura, E. and Hughes, G. R. V. (1994), β2-Glycoprotein i reactivity of monoclonal anticardiolipin antibodies from patients with the antiphospholipid syndrome. Arthritis & Rheumatism, 37: 1453–1461. doi: 10.1002/art.1780371008
- Issue published online: 9 DEC 2005
- Article first published online: 9 DEC 2005
- Manuscript Accepted: 21 APR 1994
- Manuscript Received: 10 SEP 1993
- Daiwa Anglo-Japanese Foundation
- Eranda Foundation
- Lupus UK
- Jean Shanks Foundation
- Yamasa Company
Objective. To elucidate the specificity of anticardiolipin antibodies (aCL) from patients with the antiphospholipid syndrome (APS) to various phospholipids (PLs), DNA, and β2-glycoprotein I (β2-GPI).
Methods. Five monoclonal aCL were established from peripheral blood lymphocytes of 3 patients with the APS. The reactivity of monoclonal aCL with various PLs, with DNA, and with β2-GPI was examined by enzyme-linked immunosorbent assay (ELISA).
Results. All of the monoclonal aCL bound to anionic PLs, only in the presence of β2-GPI. Neither monoclonal aCL nor β2-GPI bound to DNA. Monoclonal aCL bound to solid-phase β2-GPI on polystyrene ELISA plates that had carboxyl groups on their surface, but did not react with solid-phase β2-GPI on ordinary polystyrene plates. A mixture of β2-GPI and CL inhibited the binding of monoclonal aCL to β2-GPI, but CL or β2-GPI alone did not.
Conclusion. Monoclonal aCL may recognize a cryptic epitope, which appears as a result of β2-GPI binding to anionic PLs or to polystyrene with carboxyl groups.