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

Abstract

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.

• Authors: M B Mathews, M Reichlin, G R Hughes, R M Bernstein
• Journal: The Journal of experimental medicine (J Exp Med) Vol. 160 Issue 2 Pg. 420-34 (Aug 01 1984) ISSN: 0022-1007 [Print] United States
• PMID: 6206177 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Autoantibodies
• Autoantigens
• Epitopes
• RNA
• Amino Acyl-tRNA Synthetases
• Threonine-tRNA Ligase

Topics

• Adult
• Amino Acyl-tRNA Synthetases (immunology)
• Animals
• Antibody Specificity
• Autoantibodies (analysis, physiology)
• Autoantigens (analysis)
• Binding, Competitive
• Epitopes
• Female
• Humans
• Male
• Middle Aged
• Myositis (immunology)
• Precipitin Tests
• RNA (analysis)
• Rabbits
• Threonine-tRNA Ligase (immunology, isolation & purification)