Characterization of the antigenicity of the formiminotransferase-cyclodeaminase in type 2 autoimmune hepatitis. 2004

Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
Service de Gastroentérologie et Nutrition, Hôpital Sainte-Justine, Montreal, Quebec, Canada H3T 1C5.

Human formiminotransferase-cyclodeaminase (hFTCD) is the autoantigen recognized by anti-liver cytosol type 1 (LC1) autoantibodies in type 2 autoimmune hepatitis (AIH) patients. In rats, this octameric protein is localized on the Golgi apparatus and binds brain microtubules (MTs) and vimentin. Subcellular localization of human formiminotransferase-cyclodeaminase and its implication in the pathogenesis of autoimmune hepatitis are unknown. Localization of the human formiminotransferase-cyclodeaminase in human hepatocytes was done using indirect immunofluorescence and subcellular fractionations followed by in vitro binding techniques. The formiminotransferase-cyclodeaminase antigen at two distinct locations in hepatocytes, free in the cytosol and associated with the Golgi membranes are recognized by anti-liver cytosol type 1 autoantibodies. The human formiminotransferase-cyclodeaminase binds reversibly to the Golgi membranes and this complex formation is increased by anti-liver cytosol type 1 autoantibodies. Finally, human formiminotransferase-cyclodeaminase does not interact with liver-specific cytoskeleton proteins. Anti-liver cytosol type 1 autoantibodies are directed against the mature high molecular form of human formiminotransferase-cyclodeaminase. Therefore, the subcellular location of the protein may influence the production of autoantibodies and their role in the pathogenesis of type 2 autoimmune hepatitis. This antigen-driven response does not appear to be facilitated or enhanced by a possible interaction between human formiminotransferase-cyclodeaminase and hepatocyte cytoskeleton proteins.

UI MeSH Term Description Entries
D007425 Intracellular Membranes Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES. Membranes, Intracellular,Intracellular Membrane,Membrane, Intracellular
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D002451 Cell Compartmentation A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc. Cell Compartmentations,Compartmentation, Cell,Compartmentations, Cell
D003598 Cytoskeletal Proteins Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible. Proteins, Cytoskeletal
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D005455 Fluorescent Antibody Technique Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy. Antinuclear Antibody Test, Fluorescent,Coon's Technique,Fluorescent Antinuclear Antibody Test,Fluorescent Protein Tracing,Immunofluorescence Technique,Coon's Technic,Fluorescent Antibody Technic,Immunofluorescence,Immunofluorescence Technic,Antibody Technic, Fluorescent,Antibody Technics, Fluorescent,Antibody Technique, Fluorescent,Antibody Techniques, Fluorescent,Coon Technic,Coon Technique,Coons Technic,Coons Technique,Fluorescent Antibody Technics,Fluorescent Antibody Techniques,Fluorescent Protein Tracings,Immunofluorescence Technics,Immunofluorescence Techniques,Protein Tracing, Fluorescent,Protein Tracings, Fluorescent,Technic, Coon's,Technic, Fluorescent Antibody,Technic, Immunofluorescence,Technics, Fluorescent Antibody,Technics, Immunofluorescence,Technique, Coon's,Technique, Fluorescent Antibody,Technique, Immunofluorescence,Techniques, Fluorescent Antibody,Techniques, Immunofluorescence,Tracing, Fluorescent Protein,Tracings, Fluorescent Protein
D006056 Golgi Apparatus A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990) Golgi Complex,Apparatus, Golgi,Complex, Golgi
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
September 2001, Hepatology (Baltimore, Md.),
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
March 1999, Gastroenterology,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
January 1980, Methods in enzymology,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
June 1999, Acta crystallographica. Section D, Biological crystallography,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
August 2006, Histochemistry and cell biology,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
August 2004, The EMBO journal,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
October 1980, The Journal of biological chemistry,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
January 2000, Structure (London, England : 1993),
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
August 1995, Biochemistry,
Reginald Renous, and Pascal Lapierre, and Idriss Djilali-Saiah, and Susana Vitozzi, and Fernando Alvarez
December 1998, The Journal of biological chemistry,
Copied contents to your clipboard!