Autoantibodies from patients with primary biliary cirrhosis recognize a region within the nucleoplasmic domain of inner nuclear membrane protein LBR
✍ Scribed by F Lin; C M Noyer; Q Ye; J Courvalin; H J Worman
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 232 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0270-9139
No coin nor oath required. For personal study only.
✦ Synopsis
Autoantibodies from rare patients with primary bili-gens. [1][2][3][4] Antibodies against the E2 subunits of the mitoary cirrhosis (PBC) recognize LBR, or lamin B receptor, chondrial oxo acid dehydrogenase complexes are found an integral membrane protein of the inner nuclear memin approximately 90% of patients with PBC and are brane. Human LBR has a nucleoplasmic, amino-terminal specific for this disease. [4][5][6][7] Approximately 30% of padomain of 208 amino acids followed by a carboxyl-termitients with PBC have autoantibodies against proteins nal domain with eight putative transmembrane segof the nuclear envelope. 8 The nuclear envelope protein ments. Autoantibodies against LBR from four patients most frequently recognized by autoantibodies from pawith PBC recognized the nucleoplasmic, amino-terminal tients with PBC is an integral membrane glycoprotein domain but not the carboxyl-terminal domain. Immuof the nuclear pore called gp210. [9][10][11] This protein is recnoblotting of smaller fusion proteins demonstrated that ognized by autoantibodies in 10% to 25% of pathese autoantibodies recognized a conformational epitope(s) contained within the stretch of amino acids from tients. 10,11 Less frequently, patients with PBC have an-1 to 60. These results, combined with those of previous tibodies against lamin B receptor (LBR), an integral studies, show that autoepitopes of nuclear membrane protein of the nuclear envelope inner membrane, 11,12 or proteins are located within their nucleocytoplasmic dothe intermediate filament nuclear lamins. 10 Autoantimains and that autoantibodies from patients with PBC bodies against LBR and gp210 are specific for PBC and predominantly react with one domain of a protein antirarely, if ever, found in patients with other liver or gen. This work also provides further characterization of autoimmune diseases. [10][11][12]
anti-LBR antibodies that have found utility as reagents
In some autoimmune diseases, self-antigens have in cell biology research. (HEPATOLOGY 1996;23:57-61.) been shown to trigger the disease, and specific autoantibodies are related to the pathological process. 13 In Primary biliary cirrhosis (PBC) is characterized by others, autoantibodies of different specificities and unintrahepatic bile duct destruction accompanied by imclear pathophysiological significance recognize a distrimune system abnormalities, most notably the presence bution of epitopes on different proteins. 13 In PBC, the of autoantibodies against intracellular protein antiautoantibodies characterized so far primarily recognize restricted regions of their respective protein antigens. Antibodies against the E2 subunit of the mitochondrial Abbreviations: PBC, primary biliary cirrhosis; LBR, lamin B receptor; GST, pyruvate dehydrogenase complex, for example, recogglutathione-S-transferase.
From the Departments of 1 Medicine and 2 Anatomy and Cell Biology, College nize a predominant epitope that is part of the inner of Physicians and Surgeons, Columbia University, New York, NY; the 3 Departlipoyl domain. [14][15][16] These antibodies may be involved