873 A MIXTURE OF NATIVE AND RECOMBINANT MITOCHONDRIAL ANTIGENS IMPROVES THE DETECTION OF PRIMARY BILIARY CIRRHOSIS-SPECIFIC ANTIBODIES

2008 ◽  
Vol 48 ◽  
pp. S328
Author(s):  
C. Daehnrich ◽  
M. Mytilinaiou ◽  
A. Rosemann ◽  
C. Probst ◽  
W. Schlumberger ◽  
...  
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
Specific Antibodies ◽  
Mitochondrial Antigens

scholarly journals Mitochondrial antigens and antibodies in primary biliary cirrhosis.

1991 ◽  
Vol 67 (791) ◽  
pp. 790-797 ◽  
Author(s):  
P. Butler ◽  
F. Valle ◽  
A. K. Burroughs
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
Mitochondrial Antigens

scholarly journals Early Primary Biliary Cirrhosis: A New Association with Erythema Nodosum of Unknown Origin

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Nikolaos K. Gatselis ◽  
Kalliopi Zachou ◽  
George N. Dalekos
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Erythema Nodosum ◽  
Unknown Origin ◽  
Low Grade ◽  
Biliary Cirrhosis ◽  
Specific Antibodies ◽  
Immune Mediated ◽  
New Association ◽  
Early Primary ◽  
Work Up

Primary biliary cirrhosis (PBC) is associated with immune-mediated dermatologic disorders. The association of PBC with erythema nodosum (EN) seems rare. We report two females (42 and 44 years old) with low-grade fever, arthralgias, and elevated cholestatic enzymes in the first and fatigue in the second. Patients were also suffering from typical EN lesions characterized by multiple erythematous, painful nodules over the anterior portions of their lower extremities. Clinical and extensive laboratory work up excluded all known EN causes. PBC diagnosis was established according to the cholestatic biochemical profile, anti-mitochondrial antibodies (AMA) positivity and liver histology (first), and AMA and antinuclear (ANA) PBC-specific antibodies (second). Our report may suggest that PBC could be kept in mind in EN patients of unknown aetiology and particularly, when middle-aged female patients are affected. In such cases a thorough evaluation for AMA and/or ANA PBC-specific antibodies could be helpful to achieve a correct and timely diagnosis.

Mitochondrial Antigens as Targets of Cellular and Humoral Auto-Immunity in Primary Biliary Cirrhosis

2005 ◽  
Vol 28 (2) ◽  
pp. 083-092 ◽  
Author(s):  
Yasunori Ichiki ◽  
Carlo Selmi ◽  
Shinji Shimoda ◽  
Hiromi Ishibashi ◽  
Stuart C. Gordon ◽  
...  
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
Mitochondrial Antigens

scholarly journals The autoepitope of the 74-kD mitochondrial autoantigen of primary biliary cirrhosis corresponds to the functional site of dihydrolipoamide acetyltransferase.

1988 ◽  
Vol 167 (6) ◽  
pp. 1791-1799 ◽  
Author(s):  
J Van de Water ◽  
M E Gershwin ◽  
P Leung ◽  
A Ansari ◽  
R L Coppel
Keyword(s):  
Liver Disease ◽  
Primary Biliary Cirrhosis ◽  
Protein Product ◽  
Functional Site ◽  
Antigenic Determinants ◽  
Biliary Cirrhosis ◽  
Inner Mitochondrial Membrane ◽  
Mitochondrial Inner Membrane ◽  
Original Clone ◽  
Mitochondrial Antigens

Autoantibodies to mitochondrial antigens are characteristic of the autoimmune liver disease primary biliary cirrhosis (PBC), but the precise antigenic determinants recognized by these antibodies have not been defined. Recently, our laboratory identified a 1,370-bp rat liver cDNA clone that coded for a polypeptide recognized specifically by sera from patients with PBC but not by sera from patients with other forms of liver disease. This recombinant protein was identified as the 74-kD M2 mitochondrial inner membrane autoantigen, now known to be dihydrolipoamide acetyltransferase. In the present study, we have identified a 603-bp fragment that codes for a polypeptide containing all of the autoreactivity of the original clone. In addition, based on hydrophobicity/hydrophilicity plots of the amino acid sequence of this polypeptide segment, several peptides were synthesized and tested for reactivity by an inhibition assay using sera from patients with PBC. One peptide, defined by the amino acids AEIETDKATIGFEVQEEGYL, absorbed serum reactivity to the protein product of the original clone. Of particular interest was the finding that this peptide contains the lipoic acid binding site KATIGF of the dihydrolipoamide acetyltransferase found in the inner mitochondrial membrane. Thus, it appears that for this autoantigen, the target of the autoantibodies corresponds to a functional site of the dihydrolipoamide acetyltransferase.

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