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Rheumatology 2003; 42: 154-161
© 2003 British Society for Rheumatology

Autoantibodies to dsDNA cross-react with the arginine–glycine-rich domain of heterogeneous nuclear ribonucleoprotein A2 (hnRNP A2) and promote methylation of hnRNP A2

K.-H. Sun, S.-J. Tang1, Y.-S. Wang, W.-J. Lin2 and R.-I. You

Faculty of Medical Technology and Institute of Biotechnology in Medicine, National Yang-Ming University, Taipei,
1 Institute of Marine Biotechnology, National Taiwan Ocean University, Keelung and
2 Institute of Biopharmaceutical Science, National Yang-Ming University, Taiwan, ROC

Objective. This study was designed to clarify the internalization of anti-DNA antibodies (anti-DNA) into living cells in the pathogenesis of systemic lupus erythematosus (SLE) using anti-DNA monoclonal antibodies (mAbs).

Methods. Anti-DNA mAbs 9D7, 9D7D2, 9A4, 5E3F5, 12B3H2 and 6E11E3 were prepared by a standard hybridoma procedure to determine the interaction of anti-DNA with proteins in different types of cells.

Results. The anti-DNA mAbs reacted with two protein antigens (35 and 50 kDa) in the cells. The 35-kDa antigen was shown to have 100% homology with hnRNP A2. The arginine–glycine-rich domain in hnRNP A2 was found to be the reaction site, and the methylation of hnRNP A2 by PRMT1 (protein arginine methyltransferase 1) was increased by anti-DNA. Moreover, anti-DNA was demonstrated to bind and internalize into the cytoplasm and nucleus.

Conclusion. Nuclear localizing anti-DNA may cross-react with hnRNP A2 to modulate the inflammatory responses and polarize immune reactions associated with SLE.

KEY WORDS: Antigen, Autoantibody, Epitope, Systemic lupus erythematosus.

Correspondence to: K.-H. Sun, Faculty of Medical Technology and Institute of Biotechnology in Medicine, National Yang-Ming University, 155 Section 2, Lie-Nong Street, Shih-Pai, Taipei, Taiwan 112, ROC. E-mail: ksun{at}ym.edu.tw


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