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Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody

An autoantibody known as PL-7 was found in the serum of four patients with myositis and one with a systemic lupus erythematosus-like syndrome. The PL-7 antigen is an 80,000 dalton polypeptide that coprecipitates with transfer RNA. In aminoacylation reactions, PL-7 IgG inhibited the charging of tRNA...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1984
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187452/
https://www.ncbi.nlm.nih.gov/pubmed/6206177
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description An autoantibody known as PL-7 was found in the serum of four patients with myositis and one with a systemic lupus erythematosus-like syndrome. The PL-7 antigen is an 80,000 dalton polypeptide that coprecipitates with transfer RNA. In aminoacylation reactions, PL-7 IgG inhibited the charging of tRNA with threonine but had little or no effect on charging with other amino acids. Experimental antibodies raised against purified threonyl-tRNA synthetase recognized the same 80,000 dalton polypeptide, but tRNA was not coprecipitated. We conclude that PL-7 antibody is directed at threonyl-tRNA synthetase, and that different antigenic sites are recognized by the human and experimental autoantibodies. Our findings emphasize the link between myositis and autoimmunity to tRNA-related structures.
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spelling pubmed-21874522008-04-17 Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody J Exp Med Articles An autoantibody known as PL-7 was found in the serum of four patients with myositis and one with a systemic lupus erythematosus-like syndrome. The PL-7 antigen is an 80,000 dalton polypeptide that coprecipitates with transfer RNA. In aminoacylation reactions, PL-7 IgG inhibited the charging of tRNA with threonine but had little or no effect on charging with other amino acids. Experimental antibodies raised against purified threonyl-tRNA synthetase recognized the same 80,000 dalton polypeptide, but tRNA was not coprecipitated. We conclude that PL-7 antibody is directed at threonyl-tRNA synthetase, and that different antigenic sites are recognized by the human and experimental autoantibodies. Our findings emphasize the link between myositis and autoimmunity to tRNA-related structures. The Rockefeller University Press 1984-08-01 /pmc/articles/PMC2187452/ /pubmed/6206177 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title_full Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title_fullStr Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title_full_unstemmed Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title_short Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody
title_sort anti-threonyl-trna synthetase, a second myositis-related autoantibody
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187452/
https://www.ncbi.nlm.nih.gov/pubmed/6206177