The molecular basis of self-association of antibodies to IgG (rheumatoid factors) in rheumatoid arthritis.
The molecular basis of self-association of antibodies to IgG (rheumatoid factors) in rheumatoid arthritis.
复制标题
类风湿关节炎中 IgG（类风湿因子）抗体自关联的分子基础。
DOI：
10.1073/pnas.71.2.517
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发表时间：
1974
影响因子：
11.1
通讯作者：
M. Mannik
中科院分区：
文献类型：
--
作者：
R. Pope;David C. TELLERt;M. Mannik
许多类风湿关节炎患者的血清和滑液中都含有由免疫球蛋白G(Ig G)组成的免疫复合体。在这项研究中，来自一名患者的这种复合体是通过免疫球蛋白抗体与免疫球蛋白(免疫球蛋白类风湿因子)的自身结合而形成的，因此每个分子既是抗体又是抗原。所有来自这些络合物的F(ab‘)(2)和Fab’片段都有与正常免疫球蛋白结合的抗体结合部位。由于这些抗体在形成环状复合体时有很高的结合常数，正常的免疫球蛋白被排除为抗原。这些研究为进一步阐明类风湿关节炎患者的血清和滑液中是否存在类似的免疫复合体提供了一个模型。
The serum and synovial fluid of many patients with rheumatoid arthritis contain immune complexes composed of immunoglobulin G (IgG). In this study such complexes from one patient are shown to be formed by self-association of IgG-antibodies to IgG (IgG-rheumatoid factors), so that each molecule serves as an antibody as well as an antigen. All F(ab')(2) and Fab' fragments derived from these complexes have antibody binding sites for normal IgG. Due to a high association constant in the formation of a cyclic complex by these antibodies, normal IgG is excluded as an antigen. These studies serve as a model for further elucidation of presence of similar immune complexes in the serum and synovial fluid of patients with rheumatoid arthritis.