The specificity of disease-associated anti-fibrillarin autoantibodies compared with that of HgCl2-induced autoantibodies

Molecular Biology Reports
B LübbenR Lührmann

Abstract

Autoantibodies against nucleolar components are a common serological feature of patients suffering from scleroderma, a collagen vascular autoimmune disease. An important target of these autoantibodies is a protein with an apparent molecular weight of 36 kDa and a pI value of 8.5, located in the dense fibrillar component of the nucleolus and therefore termed fibrillarin. Animal models in which abundant anti-nucleolar antibodies appear spontaneously have not yet been described; however, high levels of anti-fibrillarin antibodies can be induced by treating susceptible strains of mice with sub-toxic amounts of mercuric chloride. In this study, we have analysed the specificity of anti-fibrillarin autoantibodies of human and murine origin. Our results suggest that both species have similar, if not identical conformational epitopes that are the target of anti-fibrillarin autoantibodies; these epitopes require the presence of a 30-kDa fragment of the fibrillarin molecule. Post-translational modifications such as the dimethylation of arginines in the N terminus of the protein are not essential for antibody recognition.

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Citations

May 13, 2003·Environmental Toxicology·Paul B TchounwouDwayne Sutton
Dec 1, 1995·Current Opinion in Immunology·P Griem, E Gleichmann
Dec 1, 1995·Journal of Autoimmunity·P HultmanF Dagnaes-Hansen
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Sep 1, 1997·Clinical Immunology and Immunopathology·G A HanleyE S Sobel
Sep 25, 1999·Protein Expression and Purification·D L PearsonK M Pollard

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