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Anticardiolipin antibodies recognize beta 2-glycoprotein I structure altered by interacting with an oxygen modified solid phase surface.

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Matsuura, E, Igarashi, Y, Yasuda, T, Triplett, D A, Koike, T·1994·The Journal of experimental medicine

Abstract

Anticardiolipin antibodies (aCL) derived from the sera of individuals exhibiting the antiphospholipid syndrome (APS) directly bind to beta 2-glycoprotein I (beta 2-GPI), which is adsorbed to an oxidized polystyrene surface. Oxygen atoms were introduced on a polystyrene surface by irradiation with electron or gamma-ray radiation. X-ray photoelectron spectroscopy revealed the irradiated surfaces were oxidized to generate C-O and C = O moieties. aCL derived from either APS patients or (NZW x BXSB)F1 mice bound to beta 2-GPI coated on the irradiated plates, depending on the radiation dose. Antibody binding to beta 2-GPI on the irradiated plates was competitively inhibited by simultaneous addition of cardiolipin (CL)-coated latex beads mixed together with beta 2-GPI but were unaffected by addition of excess beta 2-GPI, CL micelles, or CL-coated latex beads alone. There was a high correlation between binding values of aCL in sera from 40 APS patients obtained by the anti-beta 2-GPI enzyme-linked immunosorbent assay (ELISA) using the irradiated plates and those by the beta 2-GPI-dependent aCL ELISA. Therefore, aCL have specificity for an epitope on beta 2-GPI. This epitope is expressed by a conformational change occurring when beta 2-GPI interacts with an oxygen-substituted solid phase surface.

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Metadata

Authors
Matsuura, E., Igarashi, Y., Yasuda, T., Triplett, D. A., & Koike, T.
Venue
The Journal of experimental medicine
Published
1994-02-01
Volume
179
Issue
2
Pages
457-462
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
OpenAlex
W2160872701
Cited by
529
References
0
FWCI
31.22
Type
journal article
Language
en
Open access
bronze

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Matsuura, E., Igarashi, Y., Yasuda, T., Triplett, D. A., & Koike, T. (1994). Anticardiolipin antibodies recognize beta 2-glycoprotein I structure altered by interacting with an oxygen modified solid phase surface. The Journal of experimental medicine. https://doi.org/10.1084/jem.179.2.457

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