Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-7-29
pubmed:abstractText
The characteristic serological feature of primary biliary cirrhosis (PBC) is the presence of antimitochondrial antibodies (AMAs), and the major proteins recognized by AMAs are subunits of the 2-oxo acid dehydrogenase complexes (2-OADC), including the E2 components of the pyruvate dehydrogenase complex (PDC), the 2-oxo-glutarate dehydrogenase complex (OGDC), the branched-chain 2-oxoacid dehydrogenase complex (BCOADC), the E3 binding protein (E3BP or protein X) and the E1a component of mammalian PDC. Previous work has postulated that either E3BP, or a molecule cross-reactive with the PDC-E2 molecule, is uniquely expressed on the surface of biliary epithelial cells in PBC. To address this issue, we performed in situ hybridization for all of the major 2-OADC components at the mRNA level, including PDC-E2, BCOADC-E2, OGDC-E2, PDC-E1a, BCOADC-E1a, OGDC-E1, and E3BP using 13 PBC and 9 control livers using 7 mitochondrial antisense probes. In both PBC and controls, the expression of all 2-OADC component mRNA studied herein were found in hepatocytes and infiltrating mononuclear cells, without significant differences. Interestingly, however, despite published data on immunohistochemical staining, interlobular bile ducts including the injured bile ducts in PBC were generally negative or only faintly positive, with the exception of 1 bile duct in 1 of 13 cases of PBC and 1 of 9 control liver specimens. Moreover, confocal microscopic examination and image analysis revealed that the mRNA signal intensity of each of the 2-OADC components in the bile ducts of PBC was relatively lower in comparison with control liver diseases. These data suggest that continuous enhanced synthesis of the 2-OADC components is not likely to be occurring in the biliary epithelial cells in PBC, and that an increase of PDC-E2 or E3BP immunoreactivity in PBC is caused by exogenous imported or cross-reactive molecules.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0270-9139
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10385636-3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide), pubmed-meshheading:10385636-Aged, pubmed-meshheading:10385636-Bile Ducts, pubmed-meshheading:10385636-Blotting, Northern, pubmed-meshheading:10385636-Dihydrolipoyllysine-Residue Acetyltransferase, pubmed-meshheading:10385636-Female, pubmed-meshheading:10385636-Humans, pubmed-meshheading:10385636-In Situ Hybridization, pubmed-meshheading:10385636-Ketoglutarate Dehydrogenase Complex, pubmed-meshheading:10385636-Ketone Oxidoreductases, pubmed-meshheading:10385636-Liver, pubmed-meshheading:10385636-Liver Cirrhosis, Biliary, pubmed-meshheading:10385636-Liver Transplantation, pubmed-meshheading:10385636-Male, pubmed-meshheading:10385636-Middle Aged, pubmed-meshheading:10385636-Multienzyme Complexes, pubmed-meshheading:10385636-Peptides, pubmed-meshheading:10385636-Pyruvate Dehydrogenase Complex, pubmed-meshheading:10385636-RNA, Messenger, pubmed-meshheading:10385636-Transcription, Genetic
pubmed:year
1999
pubmed:articleTitle
In situ nucleic acid detection of PDC-E2, BCOADC-E2, OGDC-E2, PDC-E1alpha, BCOADC-E1alpha, OGDC-E1, and the E3 binding protein (protein X) in primary biliary cirrhosis.
pubmed:affiliation
Second Department of Pathology, Kanazawa University of School of Medicine, Kanazawa, Japan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't