Newkirk M M, Rauch J, Commerford K
Department of Medicine, McGill University, Montreal General Hospital Research Institute, Quebec, Canada.
J Rheumatol Suppl. 1992 Jan;32:54-5; discussion 55-8.
The interaction of human monoclonal rheumatoid factors (RF) with the Fc portion of IgG is complex. We have investigated the influence of the nature of the antigen (Fc) on the binding of hybridoma-generated RF derived from patients with rheumatoid arthritis or systemic lupus erythematosus. For IgM RF, the interaction is strongly influenced by the primary structure of the Fc with little or no effect of the carbohydrate, which is positioned at amino acid 297 in the gamma-2 domain. In contrast, our preliminary data suggest that IgG RF binding is affected both by the primary structure and the nature of the carbohydrate of the Fc. These results suggest that the antigen selection events which lead to the induction and production of IgG RF are likely to be different from those that induce IgM RF production.
人单克隆类风湿因子（RF）与IgG的Fc部分的相互作用很复杂。我们研究了抗原（Fc）的性质对源自类风湿性关节炎或系统性红斑狼疮患者的杂交瘤产生的RF结合的影响。对于IgM RF，这种相互作用受到Fc一级结构的强烈影响，而位于γ-2结构域第297位氨基酸处的碳水化合物影响很小或没有影响。相比之下，我们的初步数据表明，IgG RF的结合受到Fc一级结构和碳水化合物性质的影响。这些结果表明，导致IgG RF诱导和产生的抗原选择事件可能与诱导IgM RF产生的事件不同。
