NDLI: Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis.

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Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis.

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Identification and analysis of the major M2 autoantigens in primary biliary cirrhosis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	James, O. F. Guest, J. R. Bassendine, M. F. Fussey, S. P. Yeaman, S. J.
Description	Author Affiliation: Fussey SP ( Department of Biochemistry, Medical School, University of Newcastle upon Tyne, United Kingdom.);
Abstract	Primary biliary cirrhosis (PBC) is a chronic cholestatic liver disease characterized by the presence of antimitochondrial antibodies in the serum. It is possible that the PBC-specific immunoreactive trypsin-sensitive antigens on the inner mitochondrial membrane, termed M2, are important in the pathogenesis of this autoimmune disease. We have previously shown that a major M2'a' antigen is the E2 component of the pyruvate dehydrogenase multienzyme complex located within mitochondria. Analysis of the primary structure of the E2 components of all three 2-oxo acid dehydrogenase complexes reveals a high degree of homology with a similar highly segmented structure including lipoyl domains, E3-binding domains, C-terminal catalytic domains, and interdomain linker sequences. Immunoblotting of PBC patients' sera against purified E2 protein from 2-oxoglutarate dehydrogenase complex and branched-chain 2-oxo acid dehydrogenase complex reveals that these polypeptides are also autoantigens in this disease. Sera from 29 of 40 (72.5%) PBC patients gave a positive response against bovine 2-oxoglutarate dehydrogenase complex E2 and from 25 of 40 (62.5%) PBC patients gave a positive response against bovine branched-chain 2-oxo acid dehydrogenase complex E2. All 40 PBC patients (100%) have autoantibodies directed against at least one of the E2 components of the family of 2-oxo acid dehydrogenase complexes. Identification of these M2 mitochondrial autoantigens and detailed knowledge of their structure will allow important questions concerning this autoimmune disease to be addressed.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	85
Language	English
Publisher	National Academy of Sciences
Publisher Date	1988-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyltransferases Immunology Autoantigens Intracellular Membranes Liver Cirrhosis, Biliary Mitochondria, Liver Pyruvate Dehydrogenase Complex Amino Acid Sequence Animals Dihydrolipoyllysine-Residue Acetyltransferase Immunoblotting Enzymology Molecular Sequence Data Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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