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PMID: 6712685 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Rat liver histidyl-tRNA synthetase. Purification and inhibition by the myositis-specific anti-Jo-1 autoantibody.

Biochemical and biophysical research communications ·Vol. 120 ·No. 1 ·1984-04-16 ·Pages 15-21

Yang DC, Dang CV, Arnett FC

Abstract

Myositis is an autoimmune inflammatory muscle disease of unknown etiology. We demonstrate directly that the antigen to the myositis-specific anti-Jo-1 antibody is histidyl-tRNA synthetase. The anti-Jo-1 antibody inhibits human HeLa and rat liver histidyl-tRNA synthetase. Using conventional and immunoaffinity chromatography with immobilized anti-Jo-1 antibody, we have purified rat liver histidyl-tRNA synthetase which has a subunit Mr 64,000 and an estimated native Mr suggesting an alpha 2 structure. The evidence indicates that the Jo-1 antigen is histidyl-tRNA synthetase, and that some of the histidyl-tRNA synthetase structure are conserved across species.

MeSH Terms
Amino Acyl-tRNA Synthetases/isolation & purification Animals Autoantibodies/pharmacology Chromatography, Affinity HeLa Cells Histidine-tRNA Ligase/antagonists & inhibitors,isolation & purification Humans Immunochemistry Liver/enzymology Myositis/immunology Rats
Chemicals
Autoantibodies Amino Acyl-tRNA Synthetases Histidine-tRNA Ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yang D C
Dang C V
Arnett F C
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1984-04-16
Pages
15-21
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NCRR NIH HHS · 5M01RR00722 · United States
NIGMS NIH HHS · GM25848 · United States
NIADDK NIH HHS · T60 AM20558 · United States
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