期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1998
卷号：95
期号：26
页码：15542-15546
DOI：10.1073/pnas.95.26.15542
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Anticardiolipin (aCL) autoantibodies are associated with thrombosis, recurrent fetal loss, and thrombocytopenia. Only aCL found in autoimmune disease require the participation of the phospholipid binding plasma protein {beta}2 glycoprotein I ({beta}2GPI) for antibody binding and now are called anti-{beta}2GPI. The antigenic specificity of aCL affinity purified from 11 patients with high titers was evaluated in an effort to better understand the pathophysiology associated with aCL. Seven different recombinant domain-deleted mutants of human {beta}2GPI, and full length human {beta}2GPI (wild-type), were used in competition assays to inhibit the autoantibodies from binding to immobilized wild-type {beta}2GPI. Only those domain-deleted mutants that contained domain 1 inhibited the binding to immobilized wild-type {beta}2GPI from all of the patients. The domain-deleted mutants that contained domain 1 inhibited all aCL in a similar but not identical pattern, suggesting that these aCL recognize a similar, but distinguishable, epitope(s) present on domain 1.
