Biopolym. Cell. 1992; 8(4):3-19.
http://dx.doi.org/10.7124/bc.000329
Reviews
Protein biosynthesis and autoimmunity
1Sidorik L. L.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

Literature data on the peculiarities of autoantibodies biosynthesis against some components of translation apparatus are presented in this review. The examples of detecting autoantibodies against aminoacyl-tRNA synthetases, ribosomes and ribosomal proteins under certain autoimmune pathologies are considered. Their properties given in comparison with structural and functional peculiarities of autoantibodies against the other types of the cellular cytoplasmic RNP as well as the nuclear ones are partially characterized. The main hypothesis for the origin of autoantibodies and their functional significance in normal and immunopathological states are presented.
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References

[1] Jäger. Klinische Immunologie und Allergologie: 2 Teile. Urban & Fischer, Mchn. 1998. 554 p.
[2] Grabar P. Hypothesis. Auto-antibodies and immunological theories: an analytical review. Clin Immunol Immunopathol. 1975;4(4):453-66.
[3] Rose NR. Autoimmunity: a personal memoir. Autoimmunity. 1988;1(1):15-21.
[4] Kronenberg M. Self-tolerance and autoimmunity. Cell. 1991;65(4):537-42.
[5] Bona CA, Victor-Kobrin C, Manheimer AJ, Bellon B, Rubinstein LJ. Regulatory arms of the immune network. Immunol Rev. 1984;79:25-44.
[6] Monroe JG, Carroll AM, Slaoui M. Cellular and molecular interactions in suppressor T cell-mediated immunoregulation: perspectives in autoimmunity. Concepts Immunopathol. 1985;1:72-84.
[7] Cruse JM, Lewis RE Jr. Contemporary concepts of autoimmunity. Concepts Immunopathol. 1985;1:1-31. Review.
[8] Vaughn M, Virella G, Lopes-Virella MF. Diabetes, autoimmunity, and arteriosclerosis. Clin Immunol Immunopathol. 1989;52(3):414-20.
[9] Wilkin T. Autoimmunity: attack, or defence? (The case for a primary lesion theory). Autoimmunity. 1989;3(1):57-73.
[10] Beutner EH, Chorzelski TP, Binder WL. Nature of autoimmunity; pathologic versus physiologic responses and a unifying concept. Immunopathology of the skin. New York : Wiley, 1979: 147.
[11] Benacerraf B. Role of MHC gene products in immune regulation. Science. 1981;212(4500):1229–38.
[12] Ishii N, Nagy ZA, Klein J. Absence of Ir gene control of T cells recognizing foreign antigen in the context of allogenic MHC molecules. Nature. 1982;295(5849):531-3.
[13] Carpenter AB, Rabin BS. Autoimmunity in immunopathology. Clin Lab Med. 1983;3(4):745-62.
[14] Theofilopoulos AN, Kofler R. Molecular aspects of autoimmunity. Immunol Today. 1989;10(6):180-3.
[15] Rose NR. The genetic basis of susceptibility to autoimmune disease. Farid, HLA in endocrine and metabolic disordes-New York : Acad, press, 1981; 1.
[16] Tobi M, Straus SE. Chronic Epstein-Barr virus disease: a workshop held by the National Institute of Allergy and Infectious Diseases. Ann Intern Med. 1985;103(6 (Pt 1)):951-3.
[17] Rose NR, Neumann DA, Herskowitz A. Autoimmune myocarditis: concepts and questions. Immunol Today. 1991;12(8):253-5.
[18] Allison AC. Autoimmune diseases: concepts of pathogenesis and control. Talal, autoimmunity: genetic, immunologic, virologic and clinical aspects. New York: Acad, press, 1977; 91.
[19] Zinkernagel RM. H-2 restriction of cell mediated virus specific immunity and immu nopathology: self-recognition, altered self and autoagression. New York: Acad, press, 1977; 363.
[20] Zinkernagel RM, Doherty PC. MHC-restricted cytotoxic T cells: studies on the biological role of polymorphic major transplantation antigens determining T-cell restriction-specificity, function, and responsiveness. Adv Immunol. 1979;27:51-177.
[21] Smith HR, Steinberg AD. Autoimmunity--a perspective. Annu Rev Immunol. 1983;1:175-210.
[22] Jerne NK. Towards a network theory of the immune system. Ann Immunol (Paris). 1974;125C(1-2):373-89.
[23] Korneva EA, Shkhinek EK. Hormones and the immune system. Leningrad: Nauka, 1988. 249 p.
[24] Landsteiner K. The specificity of serological reactions. Boston: Harvard univ. press, 1945: 115.
[25] Köhler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975;256(5517):495-7.
[26] Baumal R, Potter M, Scharff MD. Synthesis, assembly, and secretion of gamma globulin by mouse myeloma cells. 3. Assembly of the three subclasses of IgG. J Exp Med. 1971;134(5):1316-34.
[27] Tan LK, Morrison SL. Antibody structure and antibody engineering. Adv Drug Deliv Rev 1988;2(2):129–42.
[28] Oi VT, Morrison SL. Chimeric antibodies. Biotechniques. 1986; 4: 214.
[29] Sahagan BG, Dorai H, Saltzgaber-Muller J, Toneguzzo F, Guindon CA, Lilly SP, McDonald KW, Morrissey DV, Stone BA, Davis GL, et al. A genetically engineered murine/human chimeric antibody retains specificity for human tumor-associated antigen. J Immunol. 1986;137(3):1066-74.
[30] Petrov RB. Immunology. M. Meditsina, 1987. 415 p.
[31] Neuberger MS, Williams GT, Fox RO. Recombinant antibodies possessing novel effector functions. Nature. 1984 Dec 13-19;312(5995):604-8.
[32] Roux KH, Tankersley DL. A view of the human idiotypic repertoire. Electron microscopic and immunologic analyses of spontaneous idiotype-anti-idiotype dimers in pooled human IgG. J Immunol. 1990;144(4):1387-95.
[33] Zhou EM, Lohman KL, Kennedy RC. Administration of noninternal image monoclonal anti-idiotypic antibodies induces idiotype-restricted responses specific for human immunodeficiency virus envelope glycoprotein epitopes. Virology. 1990;174(1):9-17.
[34] Misplon JA, Reeves JP, Harvath L, Rubinstein LJ, Epstein SL. Induction of antigen-specific immunity with monoclonal anti-idiotypic antibodies in vivo: differences in potency and comparison of immunochemical properties. Eur J Immunol. 1989;19(12):2361-5.
[35] Schreiber JR, Patawaran M, Tosi M, Lennon J, Pier GB. Anti-idiotype-induced, lipopolysaccharide-specific antibody response to Pseudomonas aeruginosa. J Immunol. 1990;144(3):1023-9.
[36] Guéry JC, Tournade H, Pelletier L, Druet E, Druet P. Rat anti-glomerular basement membrane antibodies in toxin-induced autoimmunity and in chronic graft-vs.-host reaction share recurrent idiotypes. Eur J Immunol. 1990;20(1):101-5.
[37] Dighiero G, Lymberi P, Holmberg D, Lundquist I, Coutinho A, Avrameas S. High frequency of natural autoantibodies in normal newborn mice. J Immunol. 1985;134(2):765-71.
[38] Avrameas S, Guilbert B, Dighiero G. Natural antibodies against tubulin, actin myoglobin, thyroglobulin, fetuin, albumin and transferrin are present in normal human sera, and monoclonal immunoglobulins from multiple myeloma and Waldenström's macroglobulinemia may express similar antibody specificities. Ann Immunol (Paris). 1981;132C(2):231-6.
[39] Marion TN, Lawton AR 3rd, Kearney JF, Briles DE. Anti-DNA autoantibodies in (NZB X NZW)F1 mice are clonally heterogeneous, but the majority share a common idiotype. J Immunol. 1982;128(2):668-74.
[40] Jacob L, Viard JP, Allenet B, Anin MF, Slama FB, Vandekerckhove J, Primo J, Markovits J, Jacob F, Bach JF, et al. A monoclonal anti-double-stranded DNA autoantibody binds to a 94-kDa cell-surface protein on various cell types via nucleosomes or a DNA-histone complex. Proc Natl Acad Sci U S A. 1989;86(12):4669-73.
[41] Tan CK, Sullivan K, Li XY, Tan EM, Downey KM, So AG. Autoantibody to the proliferating cell nuclear antigen neutralizes the activity of the auxiliary protein for DNA polymerase delta. Nucleic Acids Res. 1987;15(22):9299-308.
[42] McCann MC, James K, Kumpel BM. Production and use of human monoclonal anti-D antibodies. J Immunol Methods. 1988;115(1):3-15.
[43] Siminovitch KA. Molecular characterization of human anti-DNA antibodies. In: The Molecular Aspects of Autoimmunity. Eds N. R. Farid, C. A. Bona.— San-Diego · Acad press, 1990;59–72.
[44] Lafer EM, Rauch J, Andrzejewski C Jr, Mudd D, Furie B, Furie B, Schwartz RS, Stollar BD. Polyspecific monoclonal lupus autoantibodies reactive with both polynucleotides and phospholipids. J Exp Med. 1981;153(4):897-909.
[45] Rossi F, Kazatchkine MD. Antiidiotypes against autoantibodies in pooled normal human polyspecific Ig. J Immunol. 1989;143(12):4104-9.
[46] de Boer M, Ossendorp FA, Al BJ, Hilgers J, de Vijlder JJ, Tager JM. Production of monoclonal antibodies to thyroglobulin by in vitro immunization with a free synthetic peptide. Mol Immunol. 1987;24(10):1081-6.
[47] Ericsson UB, Christensen SB, Thorell JI. A high prevalence of thyroglobulin autoantibodies in adults with and without thyroid disease as measured with a sensitive solid-phase immunosorbent radioassay. Clin Immunol Immunopathol. 1985;37(2):154-62.
[48] Piechaczyk M, Bouanani M, Salhi SL, Baldet L, Bastide M, Pau B, Bastide JM. Antigenic domains on the human thyroglobulin molecule recognized by autoantibodies in patients' sera and by natural autoantibodies isolated from the sera of healthy subjects. Clin Immunol Immunopathol. 1987;45(1):114-21.
[49] Bouanani M, Piechaczyk M, Pau B, Bastide M. Significance of the recognition of certain antigenic regions on the human thyroglobulin molecule by natural autoantibodies from healthy subjects. J Immunol. 1989;143(4):1129-32.
[50] Jaton J-C, Reininger L. Murine autoantibodies specific for bromelinized red blood cells use a restricted set of genetic elements and their heavy chains define a novel VH family. In: The molecular aspects of autoimmunity. Eds N. Farid, C. Bona. San Diego : Acad, press, 1990;91–105.
[51] Richman DP, Gomez CM, Berman PW, Burres SA, Fitch FW, Arnason BG. Monoclonal anti-acetylcholine receptor antibodies can cause experimental myasthenia. Nature. 1980;286(5774):738-9.
[52] Valente WA, Vitti P, Yavin Z, Yavin E, Rotella CM, Grollman EF, Toccafondi RS, Kohn LD. Monoclonal antibodies to the thyrotropin receptor: stimulating and blocking antibodies derived from the lymphocytes of patients with Graves disease. Proc Natl Acad Sci U S A. 1982;79(21):6680-4.
[53] A. M. Poverennyy, G. M. Rott, N. I. Sulayeva Interaction immunoglobulins with charged biopolymers : importance for humoral immunity regulation. Mol Biol. 1983; Iss. 1: 153.
[54] Morgan AC Jr, Rossen RD, Twomey JJ. Naturally occurring circulating immune complexes: normal human serum contains idiotype-anti-idiotype complexes dissociable by certain IgG antiglobulins. J Immunol. 1979;122(5):1672-80.
[55] Biswas T, Miller FW, Twitty SA, Plotz PH. An efficient method for enrichment of histidyl-tRNA synthetase (Jo-1 antigen) from HeLa cells. J Immunol Methods. 1987;98(2):235-41.
[56] Biswas T, Miller FW, Takagaki Y, Plotz PH. An enzyme-linked immunosorbent assay for the detection and quantitation of anti-Jo-1 antibody in human serum. J Immunol Methods. 1987;98(2):243-8.
[57] Walker EJ, Jeffrey PD. Purification of bovine liver histidyl-tRNA synthetase, the Jo-1 antigen of polymyositis: size of the whole enzyme and its characteristic proteolytic fragments. Biol Chem Hoppe Seyler. 1987;368(5):531-7.
[58] Ramsden DA, Chen J, Miller FW, Misener V, Bernstein RM, Siminovitch KA, Tsui FW. Epitope mapping of the cloned human autoantigen, histidyl-tRNA synthetase. Analysis of the myositis-associated anti-Jo-1 autoimmune response. J Immunol. 1989;143(7):2267-72.
[59] Mathews MB, Bernstein RM. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature. 1983 Jul 14-20;304(5922):177-9.
[60] Bernstein RM, Bunn CC, Hughes GR, Francoeur AM, Mathews MB. Cellular protein and RNA antigens in autoimmune disease. Mol Biol Med. 1984;2(2):105-20.
[61] Rosa MD, Hendrick JP Jr, Lerner MR, Steitz JA, Reichlin M. A mammalian tRNAHis-containing antigen is recognized by the polymyositis-specific antibody anti-Jo-1. Nucleic Acids Res. 1983;11(3):853-70.
[62] Hardin JA, Rahn DR, Shen C, Lerner MR, Wolin SL, Rosa MD, Steitz JA. Antibodies from patients with connective tissue diseases bind specific subsets of cellular RNA-protein particles. J Clin Invest. 1982;70(1):141-7.
[63] Targoff IN, Reichlin M. Measurement of antibody to Jo-1 by ELISA and comparison to enzyme inhibitory activity. J Immunol. 1987;138(9):2874-82.
[64] Nishikai M, Reichlin M. Heterogeneity of precipitating antibodies in polymyositis and dermatomyositis. Characterization of the Jo-1 antibody system. Arthritis Rheum. 1980;23(8):881-8.
[65] Yang DC, Dang CV, Arnett FC. Rat liver histidyl-tRNA synthetase. Purification and inhibition by the myositis-specific anti-Jo-1 autoantibody. Biochem Biophys Res Commun. 1984;120(1):15-21.
[66] Targoff IN. Autoantibodies to aminoacyl-transfer RNA synthetases for isoleucine and glycine. Two additional synthetases are antigenic in myositis. J Immunol. 1990;144(5):1737-43.
[67] Mathews MB, Reichlin M, Hughes GR, Bernstein RM. Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody. J Exp Med. 1984;160(2):420-34.
[68] Bunn CC, Bernstein RM, Mathews MB. Autoantibodies against alanyl-tRNA synthetase and tRNAAla coexist and are associated with myositis. J Exp Med. 1986;163(5):1281-91.
[69] Bunn CC, Mathews MB. Two human tRNA(Ala) families are recognized by autoantibodies in polymyositis sera. Mol Biol Med. 1987;4(1):21-36.
[70] Bunn CC, Mathews MB. Autoreactive epitope defined as the anticodon region of alanine transfer RNA. Science. 1987;238(4830):1116-9.
[71] Dang CV, Dang CV. Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states. Mol Cell Biochem. 1986;71(2):107-20.
[72] Mirande M, CirakoÄŸlu B, Waller JP. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. III. Assignment of aminoacyl-tRNA synthetase activities to the polypeptide components of the complexes. J Biol Chem. 1982;257(18):11056-63.
[73] Mirande M, Gache Y, Le Corre D, Waller JP. Seven mammalian aminoacyl-tRNA synthetases co-purified as high molecular weight entities are associated within the same complex. EMBO J. 1982;1(6):733-6.
[74] Kellermann O, Brevet A, Tonetti H, Waller JP. Macromolecular complexes of aminoacyl-tRNA synthetases from eukaryotes. 1. Extensive purification and characterization of the high-molecular-weight complex(es) of seven aminoacyl-tRNA synthetases from sheep liver. Eur J Biochem. 1979;99(3):541-50.
[75] Brevet A, Kellermann O, Tonetti H, Waller JP. Macromolecular complexes of aminoacyl-tRNA synthetases from eukaryotes. 2. Agarose gel-filtration behaviour of the extensively purified high-molecular-weight complex(es) of seven aminoacyl-tRNA synthetases from sheep liver. Eur J Biochem. 1979;99(3):551-8.
[76] Yang DC, Garcia JV, Johnson YD, Wahab S. Multienzyme complexes of mammalian aminoacyl-tRNA synthetases. Curr Top Cell Regul. 1985;26:325-35.
[77] Walker EJ, Treacy GB, Jeffrey PD. Molecular weights of mitochondrial and cytoplasmic aminoacyl-tRNA synthetases of beef liver and their complexes. Biochemistry. 1983;22(8):1934-41.
[78] Denney RM. Detection and partial purification of rapidly sedimenting forms of aminoacyl-transfer ribonucleic acid synthetases from human placenta. Arch Biochem Biophys. 1977;183(1):156-67.
[79] Cirakoglu B, Mirande M, Waller JP. A model for the structural organization of aminoacyl-tRNA synthetases in mammalian cells. FEBS Lett. 1985;183(2):185-90.
[80] Thömmes P, Fett R, Schray B, Kunze N, Knippers R. The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. Nucleic Acids Res. 1988;16(12):5391-406.
[81] Goldstein R, Duvic M, Targoff IN et al. Serologic and restriction enzyme studies of HLA-D region genes in myositis. Arthritis Rheum. 1988;31:S33.
[82] Hardin JA. The lupus autoantigens and the pathogenesis of systemic lupus erythematosus. Arthritis Rheum. 1986;29(4):457-60.
[83] Bandyopadhyay AK, Deutscher MP. Complex of aminoacyl-transfer RNA synthetases. J Mol Biol. 1971;60(1):113-22.
[84] Smulson M, Lin CS, Chirikjian JG. Function and properties of aminoacyl transferases and aminoacyl-tRNA synthetases in rat liver and HeLa cells. Arch Biochem Biophys. 1975;167(2):458-68.
[85] Kiselev LL. Aminoacyl-tRNA synthetases (codases) and their noncanonical functions. Mol Biol (Mosk). 1990;24(6):1445-73. PubMed
[86] Spirin AS, Ajtkhozhin MA. Informosomes and polyribosome-associated proteins in eukaryotes. Trends Biochem Sci. 1985;10(4):162–5.
[87] Alzhanova AT, Fedorov AN, Ovchinnikov LP. Aminoacyl-tRNA synthetases of rabbit reticulocytes with and without the ability to bind high-Mr RNA. FEBS Lett. 1982;144(1):149-53.
[88] Tan EM. Autoantibodies to nuclear antigens (ANA): their immunobiology and medicine. Adv Immunol. 1982;33:167-240.
[89] Christian CL, Elkon KB. Autoantibodies to intracellular proteins. Clinical and biologic significance. Am J Med. 1986;80(1):53-61.
[90] Jones BR. Lacrimal and salivary precipitating antibodies in Sjögren's syndrome. Lancet. 1958;2(7050):773-6.
[91] Anderson JR, Gray KG, Beck JS, Kinnear WF. Precipitating autoantibodies in Sjogren's disease. Lancet. 1961;2(7200):456-60.
[92] Alspaugh MA, Talal N, Tan EM. Differentiation and characterization of autoantibodies and their antigens in Sjögren's syndrome. Arthritis Rheum. 1976;19(2):216-22.
[93] Akizuki M, Powers R, Holman HR. A soluble acidic protein of the cell nucleus which reacts with serum from patients with systemic lupus erythermatosus and Sjögren's syndrome. J Clin Invest. 1977;59(2):264-72.
[94] Lerner MR, Boyle JA, Hardin JA, Steitz JA. Two novel classes of small ribonucleoproteins detected by antibodies associated with lupus erythematosus. Science. 1981;211(4480):400-2.
[95] Hendrick JP, Wolin SL, Rinke J, Lerner MR, Steitz JA. Ro small cytoplasmic ribonucleoproteins are a subclass of La ribonucleoproteins: further characterization of the Ro and La small ribonucleoproteins from uninfected mammalian cells. Mol Cell Biol. 1981;1(12):1138-49.
[96] Elkon KB, Culhane L. Partial immunochemical characterization of the Ro and La proteins using antibodies from patients with the sicca syndrome and lupus erythematosus. J Immunol. 1984;132(5):2350-6.
[97] Rosa MD, Gottlieb E, Lerner MR, Steitz JA. Striking similarities are exhibited by two small Epstein-Barr virus-encoded ribonucleic acids and the adenovirus-associated ribonucleic acids VAI and VAII. Mol Cell Biol. 1981;1(9):785-96.
[98] Bonfa E, Marshak-Rothstein A, Weissbach H, Brot N, Elkon K. Frequency and epitope recognition of anti-ribosome P antibodies from humans with systemic lupus erythematosus and MRL/lpr mice are similar. J Immunol. 1988;140(10):3434-7.
[99] Eisenberg RA, Craven SY, Warren RW, Cohen PL. Stochastic control of anti-Sm autoantibodies in MRL/Mp-lpr/lpr mice. J Clin Invest. 1987;80(3):691-7.
[100] Bachmann M, Mayet WJ, Schröder HC, Pfeifer K, Meyer zum Büschenfelde KH, Müller WE. Association of La and Ro antigens with intracellular structures in HEp-2 carcinoma cells. Proc Natl Acad Sci U S A. 1986;83(20):7770-4.
[101] Elkon KB, Bonfa E, Llovet R, Eisenberg RA. Association between anti-Sm and anti-ribosomal P protein autoantibodies in human systemic lupus erythematosus and MRL/lpr mice. J Immunol. 1989;143(5):1549-54.
[102] Maniatis T, Reed R. The role of small nuclear ribonucleoprotein particles in pre-mRNA splicing. Nature. 1987 Feb 19-25;325(6106):673-8.
[103] Stacey DW, Skelly S, Watson T, Elkon K, Weissbach H, Brot N. The inhibition of protein synthesis by IgG containing anti-ribosome P autoantibodies from systemic lupus erythematosus patients. Arch Biochem Biophys. 1988;267(1):398-403.
[104] Boak AM, Kovacs SA, Agris PF, Chakraborty D, Sarkar S. Small nuclear ribonucleoprotein antigens are absent from 10S translation inhibitory ribonucleoprotein but present in cytoplasmic messenger ribonucleoprotein and polysomes. Arch Biochem Biophys. 1986;248(1):89-100.
[105] Elkon K, Bonfa E, Llovet R, Danho W, Weissbach H, Brot N. Properties of the ribosomal P2 protein autoantigen are similar to those of foreign protein antigens. Proc Natl Acad Sci U S A. 1988;85(14):5186-9.
[106] Absi M, La Vergne JP, Marzouki A, Giraud F, Rigal D, Reboud AM, Reboud JP, Monier JC. Heterogeneity of ribosomal autoantibodies from human, murine and canine connective tissue diseases. Immunol Lett. 1989;23(1):35-41.
[107] Kieber-Emmons T, Kohler H. Evolutionary origin of autoreactive determinants (autogens). Proc Natl Acad Sci U S A. 1986;83(8):2521-5.
[108] Rokeach LA, Jannatipour M, Hoch SO. Heterologous expression and epitope mapping of a human small nuclear ribonucleoprotein-associated Sm-B'/B autoantigen. J Immunol. 1990;144(3):1015-22.
[109] Meek K, Takei M, Dang H, Sanz I, Dauphinée MJ, Capra JD, Talal N. Anti-peptide antibodies detect a lupus-related interspecies idiotype that maps to H chain CDR2. J Immunol. 1990;144(4):1375-81.
[110] Thornton JM, Sibanda BL. Amino and carboxy-terminal regions in globular proteins. J Mol Biol. 1983;167(2):443-60.
[111] Shoenfeld Y, Isenberg DA, Rauch J, Madaio MP, Stollar BD, Schwartz RS. Idiotypic cross-reactions of monoclonal human lupus autoantibodies. J Exp Med. 1983;158(3):718-30.
[112] Klinman DM, Steinberg AD. Idiotypy and autoimmunity. Arthritis Rheum. 1986;29(6):697-705.
[113] Zouali M, Eyquem A. Idiotypic/antiidiotypic interactions in systemic lupus erythematosus: demonstration of oscillating levels of anti-DNA autoantibodies and reciprocal antiidiotypic activity in a single patient. Ann Immunol (Paris). 1983;134C(3):377-91.
[114] Bjercke RJ, Langone JJ. Anti-idiotypic antibody probes of neuronal nicotinic receptors. Biochem Biophys Res Commun. 1989;162(3):1085-92.
[115] Guéry JC, Druet E, Glotz D, Hirsch F, Mandet C, De Heer E, Druet P. Specificity and cross-reactive idiotypes of anti-glomerular basement membrane autoantibodies in HgCl2-induced autoimmune glomerulonephritis. Eur J Immunol. 1990;20(1):93-100.
[116] Marion TN, Bothwell AL, Briles DE, Janeway CA Jr. IgG anti-DNA autoantibodies within an individual autoimmune mouse are the products of clonal selection. J Immunol. 1989;142(12):4269-74.
[117] Shlomchik MJ, Marshak-Rothstein A, Wolfowicz CB, Rothstein TL, Weigert MG. The role of clonal selection and somatic mutation in autoimmunity. Nature. 1987 Aug 27-Sep 2;328(6133):805-11.
[118] Kohler H, Muller S, Bona C. Internal antigen and immune network. Proc Soc Exp Biol Med. 1985;178(2):189-95.
[119] Cazenave PA, Roland J, Papillon M, Continho A. Idiotypic interactions of antibodies and cellular receptors that provide and regulate immune activity. Immunoglobulins and idiotypes, JCN-UCLA: Symp Mol Cell. Biol. New York: Acad, press, 1981; Vol. 20: 759.
[120] Jacobs J, Schultz PG, Sugasawara R, Powell M. Catalytic antibodies. J Am Chem Soc. 1987;109(7):2174–6.
[121] Hilvert D, Hill KW, Nared KD, Auditor MTM. Antibody catalysis of the Diels-Alder reaction. J Am Chem Soc. 1989;111(26):9261–2.
[122] Iverson BL, Cameron KE, Jahangiri GK, Pasternak DS. Selective cleavage of trityl protecting groups catalyzed by an antibody. J Am Chem Soc. 1990;112(13):5320–3.
[123] Powell MJ, Hansen DE. Catalytic antibodies--a new direction in enzyme design. Protein Eng. 1989;3(2):69-75.
[124] Jencks WP. Catalysis in chemistry and enzymology. New York: McGrow-Hill, 1969. 288 p.
[125] Shuster AM, Gololobov GV, Kvashuk OA, Gabibov AG. Anti-idiotypic and natural catalytically active antibodies. Mol Biol (Mosk). 1991;25(3):593-602.
[126] Paul S, Volle DJ, Beach CM, Johnson DR, Powell MJ, Massey RJ. Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science. 1989;244(4909):1158-62.
[127] BronshteÄ­n IB, Shuster AM, Shevchenko LV, Gromova II, Kvashuk OA, Geva ON, Gabibov AG. Topoisomerase I from human placenta. Functional activity of products of expression of cloned cDNA fragments. Mol Biol (Mosk). 1989;23(6):1553-7.
[128] Shuster AM, Gololobov GV, Kvashuk OA, Gabibov AG. DNA-specific catalytic antibodies in human blood sera. Dokl Akad Nauk SSSR. 1991;318(5):1262-4.
[129] Roubaty C, Bedin C, Charreire J. Prevention of experimental autoimmune thyroiditis through the anti-idiotypic network. J Immunol. 1990;144(6):2167-72.
[130] Vartanian OA. Detection of autoantibodies against phenylalanyl-, tyrosyl-, and tryptophanyl-tRNA-synthetase and anti-idiotypic antibodies to it in serum from patients with autoimmune diseases. Mol Biol (Mosk). 1991;25(4):1033-9.
[131] Ada G. Strategies for exploiting the immune system in the design of vaccines. Mol Immunol. 1991;28(3):225-30.
[132] Chen JJ, Saeki Y, Shi LF, Köhler H. Tumor idiotype vaccines. VI. Synergistic anti-tumor effects with combined "internal image" anti-idiotypes and chemotherapy. J Immunol. 1989;143(3):1053-7.
[133] Raychaudhuri S, Saeki Y, Fuji H, Kohler H. Tumor-specific idiotype vaccines. I. Generation and characterization of internal image tumor antigen. J Immunol. 1986;137(5):1743-9.
[134] Bhattacharya-Chatterjee M, Pride MW, Seon BK, Kohler H. Idiotype vaccines against human T cell acute lymphoblastic leukemia. I. Generation and characterization of biologically active monoclonal anti-idiotopes. J Immunol. 1987;139(4):1354-60.
[135] Herlyn D, Wettendorff M, Schmoll E, Iliopoulos D, Schedel I, Dreikhausen U, Raab R, Ross AH, Jaksche H, Scriba M, et al. Anti-idiotype immunization of cancer patients: modulation of the immune response. Proc Natl Acad Sci U S A. 1987;84(22):8055-9.
[136] McNamara MK, Ward RE, Kohler H. Monoclonal idiotope vaccine against Streptococcus pneumoniae infection. Science. 1984;226(4680):1325-6.
[137] Kennedy RC, Dreesman GR, Kohler H. Vaccines utilizing internal image anti-idiotypic antibodies that mimic antigens of infectious organism. BioTechniques. 1985; 3:4040.
[138] Oosterlaken TA, Harmsen M, Tangerman C, Schielen P, Kraaijeveld CA, Snippe H. A neutralization-inhibition enzyme immunoassay for anti-idiotypic antibodies that block monoclonal antibodies neutralizing Semliki Forest virus. J Immunol Methods. 1988;115(2):255-61.
[139] Kim WB, Jo YW, Choi EC, Kim BK. Inhibition ELISA for hepatitis B surface antigen (HBsAg) using monoclonal idiotype-anti-idiotype interaction. J Immunol Methods. 1989;125(1-2):273-8.
[140] Oldstone MB, Nerenberg M, Southern P, Price J, Lewicki H. Virus infection triggers insulin-dependent diabetes mellitus in a transgenic model: role of anti-self (virus) immune response. Cell. 1991;65(2):319-31.
[141] Roitt IM, Cooke A. Idiotypes and autoimmunity. Progr Immunol. Eds B. Cinaderr R. G. Miller. Orlando : Acad, press, 1987; 6:12.
[142] Kisselev LL., Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.
[143] Jacobo-Molina A, Peterson R, Yang DC. cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J Biol Chem. 1989;264(28):16608-12.
[144] Kontis KJ, Arfin SM. Isolation of a cDNA clone for human threonyl-tRNA synthetase: amplification of the structural gene in borrelidin-resistant cell lines. Mol Cell Biol. 1989;9(5):1832-8.
[145] Tsui FW, Siminovitch L. Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. Nucleic Acids Res. 1987;15(8):3349-67.
[146] Majumder AL, Akins RA, Wilkinson JG, Kelley RL, Snook AJ, Lambowitz AM. Involvement of tyrosyl-tRNA synthetase in splicing of group I introns in Neurospora crassa mitochondria: biochemical and immunochemical analyses of splicing activity. Mol Cell Biol. 1989;9(5):2089-104.
[147] Pollard JW, Galpine AR, Clemens MJ. A novel role for aminoacyl-tRNA synthetases in the regulation of polypeptide chain initiation. Eur J Biochem. 1989;182(1):1-9.
[148] Wahab SZ, Yang DC. Synthesis of diadenosine 5',5''' -P1,P4-tetraphosphate by lysyl-tRNA synthetase and a multienzyme complex of aminoacyl-tRNA synthetases from rat liver. J Biol Chem. 1985;260(9):5286-9.
[149] Sidorik LL, Popenko VI, Cherny NE, Tukalo MA, Beresten SF, Matsuka GKh. Immunoelectron-microscopic study of seryl-tRNA-synthetase localization in cells of higher eucaryotes. Biopolym Cell. 1990;6(5):72-7.
[150] Agris PF, Setzer D, Gehrke CW. Characterization of a unique enzyme complex composed of S-adenosyl-L-methionine-tRNA-methyltransferase and aminoacyl-tRNA synthetase activities. Nucleic Acids Res. 1977;4(11):3803-19.
[151] Smulson M, Lin CS, Chirikjian JG. Function and properties of aminoacyl transferases and aminoacyl-tRNA synthetases in rat liver and HeLa cells. Arch Biochem Biophys. 1975;167(2):458-68.
[152] Janeway CA. Autoimmune disease: immunotherapy by peptides? Nature. 1989;341(6242):482-3.
[153] Avrameas S. Natural autoantibodies: from 'horror autotoxicus' to 'gnothi seauton'. Immunol Today. 1991;12(5):154-9.