Autoantibodies in primary biliary cirrhosis: Analysis of reactivity against eukaryotic and prokaryotic 2-oxo acid dehydrogenase complexes
Autor: | C. Fuller, S. Dale, S. P. M. Fussey, R. N. Perham, O.F.W. James, J. G. Lindsay, Margaret F. Bassendine, Stephen J. Yeaman |
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Rok vydání: | 1991 |
Předmět: |
Primary biliary cirrhosis
Hepatology Biochemistry 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Pyruvate Dehydrogenase (Lipoamide) medicine Dehydrogenase Bacterial antigen Biology Pyruvate dehydrogenase complex medicine.disease Branched-chain alpha-keto acid dehydrogenase complex Oxoglutarate dehydrogenase complex |
Zdroj: | Hepatology. 13:467-474 |
ISSN: | 1527-3350 0270-9139 |
DOI: | 10.1002/hep.1840130314 |
Popis: | Six components of the mammalian 2-oxo acid dehydrogenase complexes have previously been identified as M2 autoantigens in primary biliary cirrhosis. In this report, we present data showing that both polypeptide-specific and cross-reacting antibodies are present in patients' sera. Antibodies reacting with E2 of the pyruvate dehydrogenase complex cross-react with protein X but not with any other mammalian antigen. The main immunogenic region on protein X has been localized to within its single lipoyl domain. Polypeptide-specific antibodies bind to E1 alpha and E1 beta of the pyruvate dehydrogenase complex. Antibodies reacting with the E2 polypeptides of the 2-oxoglutarate dehydrogenase complex and branched-chain 2-oxo acid dehydrogenase complex show some cross-reactivity but do not recognize any of the antigens of the pyruvate dehydrogenase complex. Antibodies against the E2 component of the mammalian pyruvate dehydrogenase complex cross-react effectively with the corresponding protein from yeast but not with E2 from Escherichia coli. Antibody titer against mammalian antigens is significantly higher than against the bacterial antigens, arguing against a bacterial origin for primary biliary cirrhosis. |
Databáze: | OpenAIRE |
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