Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis

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Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis

C Szostecki, HH Guldner, HJ Netter and H Will
Max-Planck-Institut fur Biochemie, Martinsried, Federal Republic of Germany.

Autoantibodies to a novel nuclear Ag, Sp100, have recently been described that recognize a nuclear protein with an apparent molecular mass of 95 to 100 kDa and a dot-like distribution within cell nuclei. By immunoscreening of a lambda gt11 cDNA expression library derived from HeLa cells with an anti-Sp100 autoimmune serum a 0.7-kb cDNA (Sp26) coding for a fragment of Sp100 was isolated. Expression of this cDNA and use of the recombinant protein in ELISA revealed that the fragment carries major Sp100 autoepitopes and that anti-Sp100 autoantibodies predominantly occur in patients suffering from primary biliary cirrhosis (50/184). The Sp26 cDNA was used as hybridization probe for isolation of longer cDNA from human liver- and placenta- derived lambda gt10 cDNA libraries. Overlapping fragments were assembled to generate a full length cDNA coding for a protein with a molecular mass of 53 kDa and an isoelectric point of 4.7. The Sp100 autoantigen expressed in vitro from this cDNA and authenticated by a capture immunoblot assay, comigrated in SDS-PAGE with the authentic HeLa autoantigen of 95 to 100 kDa and thus showed an aberrant electrophoretic mobility. Computer based protein sequence analysis of the Sp100 autoantigen revealed regions of striking sequence similarities to the alpha 1 and alpha 2 domains of various human and non-human MHC class I Ag and to several transacting transcriptional regulatory proteins.

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				C. Shiels, S. A. Islam, R. Vatcheva, P. Sasieni, M. J. E. Sternberg, P. S. Freemont, and D. Sheer PML bodies associate specifically with the MHC gene cluster in interphase nuclei J. Cell Sci., March 12, 2002; 114(20): 3705 - 3716. [Abstract] [Full Text] [PDF]

				M. M. Shareef, C. King, M. Damaj, R. Badagu, D. W. Huang, and R. Kellum Drosophila Heterochromatin Protein 1 (HP1)/Origin Recognition Complex (ORC) Protein Is Associated with HP1 and ORC and Functions in Heterochromatin-induced Silencing Mol. Biol. Cell, June 1, 2001; 12(6): 1671 - 1685. [Abstract] [Full Text] [PDF]

				J.-S. Seeler, A. Marchio, R. Losson, J. M. P. Desterro, R. T. Hay, P. Chambon, and A. Dejean Common Properties of Nuclear Body Protein SP100 and TIF1{alpha} Chromatin Factor: Role of SUMO Modification Mol. Cell. Biol., May 15, 2001; 21(10): 3314 - 3324. [Abstract] [Full Text]

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				D Negorev, A. Ishov, and G. Maul Evidence for separate ND10-binding and homo-oligomerization domains of Sp100 J. Cell Sci., January 1, 2001; 114(1): 59 - 68. [Abstract] [PDF]

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Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis

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				F.-M. Boisvert, M. J. Hendzel, and D. P. Bazett-Jones Promyelocytic Leukemia (Pml) Nuclear Bodies Are Protein Structures That Do Not Accumulate RNA J. Cell Biol., January 24, 2000; 148(2): 283 - 292. [Abstract] [Full Text] [PDF]

				A. M. Ishov, A. G. Sotnikov, D. Negorev, O. V. Vladimirova, N. Neff, T. Kamitani, E. T.H. Yeh, J. F. Strauss III, and G. G. Maul Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1 J. Cell Biol., October 18, 1999; 147(2): 221 - 234. [Abstract] [Full Text] [PDF]

				T. Sternsdorf, E. Puccetti, K. Jensen, D. Hoelzer, H. Will, O. G. Ottmann, and M. Ruthardt PIC-1/SUMO-1-Modified PML-Retinoic Acid Receptor alpha �Mediates Arsenic Trioxide-Induced Apoptosis in Acute Promyelocytic Leukemia Mol. Cell. Biol., July 1, 1999; 19(7): 5170 - 5178. [Abstract] [Full Text] [PDF]

				S. Müller and A. Dejean Viral Immediate-Early Proteins Abrogate the Modification by SUMO-1 of PML and Sp100 Proteins, Correlating with Nuclear Body Disruption J. Virol., June 1, 1999; 73(6): 5137 - 5143. [Abstract] [Full Text]

				D. B. Bloch, J.-D. Chiche, D. Orth, S. M. de la Monte, A. Rosenzweig, and K. D. Bloch Structural and Functional Heterogeneity of Nuclear Bodies Mol. Cell. Biol., June 1, 1999; 19(6): 4423 - 4430. [Abstract] [Full Text] [PDF]

				A. Melnick and J. D. Licht Deconstructing a Disease: RAR{alpha}, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia Blood, May 15, 1999; 93(10): 3167 - 3215. [Full Text] [PDF]

				T. Sternsdorf, K. Jensen, B. Reich, and H. Will The Nuclear Dot Protein Sp100, Characterization of Domains Necessary for Dimerization, Subcellular Localization, and Modification by Small Ubiquitin-like Modifiers J. Biol. Chem., April 30, 1999; 274(18): 12555 - 12566. [Abstract] [Full Text] [PDF]