β2-Glycoprotein i reactivity of monoclonal anticardiolipin antibodies from patients with the antiphospholipid syndrome

✍ Scribed by Kenji Ichikawa; Munther A. Khamashta; Takao Koike; Eiji Matsuura; Graham R. V. Hughes

• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 907 KB
• Volume: 37
• Category: Article
• ISSN: 0004-3591
• DOI: 10.1002/art.1780371008

✦ Synopsis

To elucidate the specificity of anticardiolipin antibodies (aCL) from patients with the antiphospholipid syndrome (APS) to various phospholipids (PLs), DNA, and &-glycoprotein I (&-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 &GPI was examined by enzyme-linked immunosorbent assay (ELISA).

Results. All of the monoclonal aCL bound to anionic PLs, only in the presence of p,-GPI. Neither monoclonal aCL nor &GPI bound to DNA. Monoclonal aCL bound to solid-phase &GPI on polystyrene ELISA plates that had carboxyl groups on their surface, but did not react with solid-phase &GPI on ordinary polystyrene plates. A mixture of &-GPI and CL inhibited the binding of monoclonal aCL to &-GPI, but CL or &GPI alone did not.

Conclusion.

Monoclonal aCL may recognize a cryptic epitope, which appears as a result of &GPI binding to anionic PLs or to polystyrene with carboxyl groups.

Antiphospholipid antibodies (aPL), including anticardiolipin antibodies (aCL), lupus anticoagulant (LA),