Linked Life Data

11311235

Source:http://linkedlifedata.com/resource/pubmed/id/11311235

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pubmed-article:11311235pubmed:abstractTextAutoantibodies directed against specific human aminoacyl-tRNA synthetases have been associated with a clinical picture including myositis, arthritis, interstitial lung disease and other features that has been referred to as the "anti-synthetase syndrome". Anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS), the most recently described anti-synthetase autoantibodies, are directed against human cytosolic asparaginyl-tRNA synthetase and neutralize specifically its activity. Here we show that these antibodies recognize two epitopes on the human enzyme, an N-terminal epitope reactive in immunoblot experiments and a heat-labile epitope in the catalytic domain. In contrast to the well studied anti-Jo-1 autoantibodies anti-KS when bound to the synthetase increase the affinity of the synthetase for its tRNA substrate and prevent aminoacylation without interfering with the amino acid activation step.lld:pubmed
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pubmed-article:11311235pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:11311235pubmed:articleTitleHuman anti-asparaginyl-tRNA synthetase autoantibodies (anti-KS) increase the affinity of the enzyme for its tRNA substrate.lld:pubmed
pubmed-article:11311235pubmed:affiliationEMBL, Grenoble Outstation, P.O. Box 156, F-38042 Grenoble Cedex 9, France.lld:pubmed
pubmed-article:11311235pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11311235pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:11311235pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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