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ID 48121
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Author
Igarashi, Yoshiko
Yasuda, Tatsuji
Triplett, Douglas A.
Koike, Takao
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)F-1 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.
Published Date
1994-02-01
Publication Title
Journal of Experimental Medicine
Volume
volume179
Issue
issue2
Publisher
Rockefeller University Press
Start Page
457
End Page
462
ISSN
0022-1007
NCID
AA00697559
Content Type
Journal Article
Related Url
http://ousar.lib.okayama-u.ac.jp/metadata/3929
language
日本語
Copyright Holders
© 1994 Rockefeller University Press
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publisher
Refereed
True
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PubMed ID
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