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The Journal of Immunology, Vol 149, Issue 12 4067-4073, Copyright © 1992 by American Association of Immunologists
ARTICLES |
HH Guldner, C Szostecki, T Grotzinger and H Will
Heinrich-Pette-Institut fur Experimentelle Virologie und Immunologie, Universitat Hamburg, Germany.
About 30% of patients suffering from the chronic autoimmune liver disease primary biliary cirrhosis produce autoantibodies against Sp100, a protein migrating in SDS-PAGE at a position corresponding to 100 kDa and located on discrete dot-shaped nuclear structures. The human Sp100 cDNA has recently been cloned and the deduced amino acid sequence was found to contain similarities to several transcriptional regulatory proteins; the biologic function of the Sp100 protein, however, is still unknown. In this study we present data which show that infection of HEp2 cells with influenza A virus, transformation of glial cells with SV40 DNA, and stimulation of PBL with mitogens affect the expression of the Sp100 autoantigen. These observations prompted us to investigate whether expression of the Sp100 protein is modulated by the action of IFN. Immunofluorescence staining of HEp2 and HeLa cells grown in the presence of IFN-alpha, IFN-beta, or IFN-gamma revealed an increase both in size and number of the Sp100 protein-containing nuclear dots, whereas no such effect was observed with cells treated with TNF-alpha. As measured by an immunoblot-based ELISA the amount of Sp100 protein in INF-beta-treated cells (1000 IU/ml, 18 h) was eight to nine times higher than in untreated cells. The enhanced protein expression was accompanied by an accumulation of the Sp100-specific mRNA (13-fold increase of the normal level after 10 h of INF-beta treatment of HEp2 cells). These findings characterize the Sp100 protein as a new member of IFN-modulated proteins and raise the question whether cytokine- mediated increase of Sp100 protein expression plays a role in induction of anti-Sp100 autoantibodies.
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T. Sternsdorf, K. Jensen, D. Zuchner, and H. Will Cellular Localization, Expression, and Structure of the Nuclear Dot Protein 52 J. Cell Biol., July 28, 1997; 138(2): 435 - 448. [Abstract] [Full Text] [PDF]
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J. Zhu, M. H. M. Koken, F. Quignon, M. K. Chelbi-Alix, L. Degos, Z. Y. Wang, Z. Chen, and H. de The Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia PNAS, April 15, 1997; 94(8): 3978 - 3983. [Abstract] [Full Text] [PDF]
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D. B. Bloch, S. M. de la Monte, P. Guigaouri, A. Filippov, and K. D. Bloch Identification and Characterization of a Leukocyte-specific Component of the Nuclear Body J. Biol. Chem., November 15, 1996; 271(46): 29198 - 29204. [Abstract] [Full Text] [PDF]
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T. Grotzinger, K. Jensen, and H. Will The Interferon (IFN)-stimulated Gene Sp100 Promoter Contains an IFN-gamma Activation Site and an Imperfect IFN-stimulated Response Element Which Mediate Type I IFN Inducibility J. Biol. Chem., October 11, 1996; 271(41): 25253 - 25260. [Abstract] [Full Text] [PDF]
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V Doucas, A M Ishov, A Romo, H Juguilon, M D Weitzman, R M Evans, and G G Maul Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes & Dev., January 15, 1996; 10(2): 196 - 207. [Abstract] [PDF]
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J Strouboulis and A. Wolffe Functional compartmentalization of the nucleus J. Cell Sci., January 8, 1996; 109(8): 1991 - 2000. [Abstract] [PDF]
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