Intracellular localization of histidyl-tRNA synthetase/Jo-1 antigen in T24 cells and some other cells

Journal of Autoimmunity

Volumn 22, Issue 3, 2004, Pages 201-210

  Kamei, Hiroya ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

Author keywords

ANA; Anti nuclear antibodies; cDNA; CLSFM; Complementary DNA; Confocal laser scanning fluorescence microscopy; ELISA; Enzyme linked immunosorbent assay; FBS; Fetal bovine serum; GFP; Histidyl tRNA synthetase; Jo 1 antigen; Myositis; PML nuclear body

Indexed keywords

GREEN FLUORESCENT PROTEIN; HISTIDINE TRANSFER RNA LIGASE;

ARTICLE; CELLULAR DISTRIBUTION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CYTOPLASM; GENE EXPRESSION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; PRIORITY JOURNAL;

GREEN FLUORESCENT PROTEINS; HELA CELLS; HISTIDINE-TRNA LIGASE; HUMANS; IMMUNOBLOTTING; LUMINESCENT PROTEINS; MICROSCOPY, FLUORESCENCE; SERUM; STAINING AND LABELING;

EID: 1642367398     PISSN: 08968411     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jaut.2004.01.004     Document Type: Article

References (34)

1. Nishikai M., Reichlin M. Heterogeneity of precipitating antibodies in polymyositis and dermatomyositis. Characterization of the Jo-1 antibody system. Arthritis Rheum. 23:1980;881-888.
2. His-containing antigen is recognized by the polymyositis-specific antibody anti-Jo-1. Nucleic Acid Res. 11:1983;853-870.
3. Mathews M.B., Bernstein R.M. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature. 304:1983;177-179.
4. Yang D.C.H., Dang C.V., Arnett F.C. Rat liver histidyl-tRNA synthetase. Purification and inhibition by the myositis-specific anti-Jo-1 autoantibody. Biochem Biophys Res Commun. 120:1984;15-21.
5. Fahoum S.K., Yang D.C. Purification of mammalian histidyl-tRNA synthetase and its interaction with myositis-specific anti-Jo-1 antibodies. Biochem. 26:1987;5871-5877.
6. Nishikai M., Ohya K., Kosaka M., Akiya K., Tojo T. Anti-Jo-1 antibodies in polymyositis or dermatomyositis: evaluation by ELISA using recombinant fusion protein Jo-1 as antigen. Br J Rheumatol. 37:1998;357-361.
7. Ramsden D.A., Chen J., Miller F.W., Misener V., Bernstein R.M., Siminovitch K.A., et al. Epitope mapping of the cloned human autoantigen, histidyl-tRNA synthetase. Analysis of the myositis-associated anti-Jo-1 autoimmune response. J Immunol. 143:1989;2267-2272.
8. Martin A., Shulman M.J., Tsui F.W.L. Epitope studies indicate that histidyl-tRNA synthetase is a stimulating antigen in idiopathic myositis. FASEB J. 9:1995;1226-1233.
9. Miller F.W., Waite K.A., Biswas T., Plotz P.H. The role of an autoantigen, histidyl-tRNA synthetase, in the induction and maintenance of autoimmunity. Proc Natl Acad Sci U S A. 87:1990;9933-9937.
10. Reichlin M., Arnett Jr F.C. Multiplicity of antibodies in myositis sera. Arthritis Rheum. 27:1984;1150-1156.
11. Dang C.V., LaDuca F.M., Bell W.R. Histidyl-tRNA synthetase, the myositis Jo-1 antigen, is cytoplasmic and unassociated with the cytoskeletal framework. Exp Cell Res. 164:1986;261-266.
12. Shi M.H., Tsui F.W.L., Rubin L.A. Cellular localization of the target structures recognized by the anti-Jo-1 antibody: immunofluorescence studies on cultured human myoblasts. J Rheumatol. 18:1991;252-258.
13. Vázquez-Abad D., Carson J.H., Rothfield N. Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line (HEp-2 cells). Cell Tissue Res. 286:1996;487-491.
14. Hampel A., Enger M.D. Subcellular distribution of aminoacyl-transfer RNA synthetases in Chinese hamster ovary cell culture. J Mol Biol. 79:1973;285-293.
15. Kamei H. A nuclear dot-like structure that has a relationship with perinuclear intermediate filaments. Exp Cell Res. 218:1995;155-165.
16. Kamei H. Reversible large-body formation from nuclear bodies upon amino acid(s) starvation in T24 cells. Exp Cell Res. 224:1996;302-311.
17. Kamei H. Cystine starvation induces reversible large-body formation from nuclear bodies in T24 cells. Exp Cell Res. 237:1997;207-216.
18. Sternsdorf T., Grotzinger T., Jensen K., Will H. Nuclear dots: actors on many stages. Immunobiol. 198:1997;307-331.
19. Maul G.G. Nuclear domain 10, the site of DNA virus transcription and replication. BioEssays. 20:1998;660-667.
20. Maul G.G., Negorev D., Bell P., Ishov A.M. Properties and assembly mechanisms of ND10, PML bodies, or PODs. J Struct Biol. 129:2000;278-287.
21. Borden K.L.B. Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies. Mol Cell Biol. 22:2002;5259-5269.
22. Ormo M., Cubitt A.B., Kallio K., Gross L.A., Tsien R.Y., Remington S.J. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 273:1996;1392-1395.
23. Bubenik J., Baresova M., Viklicky V., Jakoubkova J., Sainerova H., Donner J. Established cell line of urinary bladder carcinoma (T24) containing tumour-specific antigen. Int J Cancer. 11:1973;765-773.
24. Gey G.O., Coffman W.D., Kubicek M.T. Tissue culture studies of the proliferative capacity of cervical carcinoma and normal epithelium. Cancer Res. 12:1952;264-265.
25. Yaffe D. Retention of differentiation potentialities during prolonged cultivation of myogenic cells. Proc Natl Acad Sci U S A. 61:1968;477-483.
26. Fricker M., Hollinshead M., White N., Vaux D. Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope. J Cell Biol. 136:1997;531-544.
27. Szostecki C., Guldner H.H., Netter H.J., Will H. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J Immunol. 145:1990;4338-4347.
28. Sternsdorf T., Guldner H.H., Szostecki C., Grotzinger T., Will H. Two nuclear dot-associated proteins, PML and Sp100, are often co-autoimmunogenic in patients with primary biliary cirrhosis. Scand J Immunol. 42:1995;257-268.
29. Bloch D.B., de la Monte S.M., Guigaouri P., Filoppov A., Bloch K.D. Identification and characterization of a leukocyte-specific component of the nuclear body. J Biol Chem. 271:1996;29198-29204.
30. Brouwer R., Hengstman G.J., Vree Egberts W., Ehrfeld H., Bozic B., Ghirardello A., et al. Autoantibody profiles in the sera of European patients with myositis. Ann Rheum Dis. 60:2001;116-123.
31. Rutjes S.A., Vree Egberts W.T., Jongen P., van den Hoogen F., Pruijn G.J., van Venrooij W.J. Anti-Ro52 antibodies frequently co-occur with anti-Jo-1 antibodies in sera from patients with idiopathic inflammatory myopathy. Clin Exp Immunol. 109:1997;32-40.
32. Keech C.L., Gordon T.P., McCluskey J. Cytoplasmic accumulation of the 52 kDa Ro/SS-A nuclear autoantigen in transfected cell lines. J Autoimmun. 8:1995;699-712.
33. Ohlsson M., Jonsson R., Brokstad K.A. Subcellular redistribution and surface exposure of the Ro52, Ro60 and La48 autoantigens during apoptosis in human ductal epithelial cells: a possible mechanism in the pathogenesis of Sjogren's syndrome. Scand J Immunol. 56:2002;456-469.
34. Hisautoantibodies that recognize a conformational epitope in sera of patients with myositis. Arthritis Rheum. 41:1998;1428-1437.