Cargando…
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...
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 |
_version_ | 1782146178032336896 |
---|---|
collection | PubMed |
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. |
format | Text |
id | pubmed-2187452 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1984 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |