The Structure of Thyroid Autoantigens

References

• Edelhoch H. The structure of thyroglobulin and its role in iodination. Rec Prog Horm Re.? 1965; 21: 1–24
   PubMedGoogle Scholar
• Van Herle A J, Vassart G, Dumont J E. Control of thyroglobulin synthesis and secretion. Nen Engl J Med 1979; 301: 239–249; 307–314
   PubMed Web of Science ®Google Scholar
• Van Herle A J, Uller R P, Matthews N L, Brown J. Radioimmunoassay for measurement of thyroglobulin in human serum. J Clin Invest 1973; 52: 1320–1327
   PubMed Web of Science ®Google Scholar
• Kondo Y, Inoue K, Kondo E, Ui N. Electron microscopy of monoclonal antibody-linked chains of thyroglobulin molecules. Mol Cell Endocrinol 1985; 41: 223–227
   PubMed Web of Science ®Google Scholar
• Roitt I M, Torrigiani G. Identification and estimation of undegraded thyroglobulin in human serum. Endocrinology 1967; 81: 421–429
   PubMed Web of Science ®Google Scholar
• DeGroot L J, Neipomniszcze H. Biosynthesis of thyroid hormone: basic and clinical aspects. Meiabolism 1977; 26: 665–718
   PubMed Web of Science ®Google Scholar
• Vassart G, Refetoff S, Brocas M, Dinsart C, Dumont J E. Translation of thyroglobulin 33S messenger RNA as a means of determining thyroglobulin quaternary structure. Proc Nat Acad Sci 1975; 72(10)3839–3843
   PubMed Web of Science ®Google Scholar
• Berge-Lefranc J L, Cartouzou G, Malthiery Y, Perrin F, Yarry B, Lissitzky S. Cloning of four DNA fragments complementary to human thyroglobulin messenger RNA. Eur J Biochem 1981; 120: 1–7
   PubMedGoogle Scholar
• Baas F, Van Ommen G JC, Bikker H, Arnberg A C, de Vijlder I JM. The human thyroglobulin gene is over 300 Kb long and contains introns of up to 64Kb. Nucleic Acids Res 1986; 14(13)5171–5185
   PubMed Web of Science ®Google Scholar
• Mercken L, Simons M J, Swillens S, Massaer M, Vassart G. Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431–base complementary DNA. Naiure 1985; 316: 647–651
   PubMed Web of Science ®Google Scholar
• Malthiery Y, Lissitzky S. Primary structure of human thyroglobulin deduced from the sequence of its 8448–base complementary DNA. Eur J Biochem 1987; 165: 491–498
   PubMedGoogle Scholar
• Kondo Y, Inoue K, Kotani T, Ohtaki S. Immuloelectron microscopy of the hormonogenic sites of the thyroglobulin molecule. Mol Cell Endocrinol 1988; 57: 261–267
   PubMed Web of Science ®Google Scholar
• Vassart G, Bacolla A, Brocas H, Christophe D, de Martynoff G, Leriche A, et al. Structure, expression and regulation of the thyroglobulin gene. Mol Cell Endocrinol 1985; 40: 89–97
   PubMed Web of Science ®Google Scholar
• Koch N, Laner W, Hobicht J, Dobberstein B. Primary structure of the gene for the murine la antigen-associated invariant chains (Ii) An alternatively spliced exon encodes a cysteine-rich domain highly homologous to a repetitive sequence of thyroglobulin. EMBO J 1987; 6: 1671–1683
   Web of Science ®Google Scholar
• Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor S, et al. Primary structure of Torpedo Californica acetylcholinesterase deduced from its cDNA sequence. Nature 1986; 319: 407–409
   PubMed Web of Science ®Google Scholar
• Heidelberger M. The molecular composition of immune precipitates from rabbit sera. J Am Chem Soc 1938; 60: 242–251
   Google Scholar
• Nye L, Pontes de Carvalho L C, Roitt I M. Restrictions in the response to autologous thyroglobulin in the human. Clin Exp Immunol 1980; 41: 252–263
   PubMed Web of Science ®Google Scholar
• Chan C TJ, Byfield P GH, Himsworth R L, Shepherd P. Human autoantibodies to thyroglobulin are directed towards a restricted number of human specific epitopes. Clin Exp Immunol 1987; 70: 516–523
   Google Scholar
• Male D K, Champion B R, Pryce G, Matthews H, Shepherd P. Antigenic determinants of human thyroglobulin differentiated using antigen fragments. Immunology 1985; 54: 419–427
   PubMed Web of Science ®Google Scholar
• Shimojo N, Saito K, Kohno Y, Sasaki N, Tarutani O, Nakajima Y. Antigenic determinants on thyroglobulin: comparison of the reactivities of different thyroglobulin preparations with serum antibodies and T cells of patients with chronic thyroiditis. J Clin Endocrinol Metab 1988; 66(4)689–695
   PubMed Web of Science ®Google Scholar
• Dong Q, Ludgate M, Vassart G. Towards an antigenic map of human thyroglobulin: identification of ten epitope-bearing sequences within the primary structure of thyroglobulin. J Endocrinol 1989; 122: 169–176
   PubMed Web of Science ®Google Scholar
• Baechi N, Brown T R, Urdanivia E, Sundick R S. Induction of autoimmune thyroiditis in chickens by dietary iodine. Science 1985; 2: 325–327
   Google Scholar
• Ikekubo K, Konishi J, Endo K, Nakajima K, Okuno T, Kasagi K, et al. Anti-thyroxine and anti-triiodthyronine antibodies in three cases of Hashimoto thyroiditis. Acia Endocrinologica 1978; 89: 557–566
   PubMedGoogle Scholar
• Pearce C J, Byfield P GH, Edmonds C J, Lalloz M RA, Himsworth R L. Autoantibodies to thyroglobulin crossreacting with iodothyronines. Clin Endocrinol 1981; 15: 1–10
   PubMed Web of Science ®Google Scholar
• Swillens S, Ludgate M, Mercken L, Dumont J E, Vassart G. Analysis of sequence and structure homologies between thyroglobulin and acetylcholinesterase: possible functional and clinical significance. Biochem Biophys Res Commun 1986; 137(i)142–148
   PubMedGoogle Scholar
• Kriss J P, Lev S, Tao T. Affinity purified human anti-thyroglobulin antibodies: reactivity to thyroglobulin and acetylcholinesterase. Endocrinology 1987; 120(suppl)T–48
   Google Scholar
• Weetman A P, Tse C K, Randall W R, Tsim W K, Barnard E A. Acetylcholinesterase antibodies and thyroid autoimmunity. Clin Exp Immunol 1988; 71: 96–99
   PubMed Web of Science ®Google Scholar
• Mori N, Itoh N, Salvaterra P M. Evolutionary origin of cholinergic macro-molecules and thyroglobulin. Proc Nail Acad Sci USA 1987; 84: 2813–2817
   PubMed Web of Science ®Google Scholar
• Ludgate M, Dong Q, Dinsart C, Taylor P. Epitopes common to thyroglobulin (Tg) and acetylcholinesterase (Ache) demonstrated at the molecular level. Annales d'endocrinol 1988; 49(3)232
   Web of Science ®Google Scholar
• Belyavin G, Trotter W R. Investigations of thyroid antigens reacting with Hashimoto sera. Evidence for an antigen other than thyroglobulin. Lancet 28th March, 1959; 648–652
   PubMed Web of Science ®Google Scholar
• Holborow E J, Brown P C, Roitt I M, Doniach D. Cytoplasmic localization of “complement-fixing” autoantigen in human thyroid epithelium. Brit J Exp Pathol 1959; XL(6)583–588
   Google Scholar
• Roitt I M, Ling N R, Doniach D, Couchman K G. The cytoplasmic autoantigen of the human thyroid. Immunological and biochemical characteristics. Immunology 1964; 7: 375–393
   PubMed Web of Science ®Google Scholar
• Mariotti S, Pinchera A. Solubilization of human thyroid microsomal antigen. J Clin Endocrinol Metab 1979; 48: 207–212
   PubMed Web of Science ®Google Scholar
• Alexander NM. Purification of bovine thyroid peroxidase. Endocrinology 1977; 100: 1610–1620
   PubMed Web of Science ®Google Scholar
• Virion A, Courtin F, Denze D, Michot J L, Kaniewski J, Pommier J. Spectral characteristics and catalytic properties of thyroid peroxidase-H2O2 compounds in the iodination and coupling reactions. Arch Biochem Bioph 1985; 242(1)41–47
   PubMed Web of Science ®Google Scholar
• Nakajima Y, Howells R D, Pegg C, Davies Jones E, Rees Smith B. Structure-activity analysis of microsomal antigen/thyroid peroxidase. Mol Cell Endocrinol 1987; 53: 15–23
   PubMed Web of Science ®Google Scholar
• Khoury E L, Bottazzo G F, Roitt I M. The thyroid “microsomal” antibody revisited. Its paradoxical binding in vivo to the apical surface of the follicular epithelium. J Exp Med 1984; 159: 577–591
   PubMed Web of Science ®Google Scholar
• Nilsson M, Molne J, Karlsson I A, Ericson L E. Immunoelectron microsopic studies on the cell surface location of the thyroid microsomal antigen. Mol Cell Endocrinol 1987; 53: 177–186
   PubMed Web of Science ®Google Scholar
• Czarnocka B, Ruf J, Ferrand M, Carayon P, Lissitzky S. Purification of the human thyroid peroxidase and its identification as the microsomal antigen involved in thyroid disease. FEBS Letts 1985; 190(1)147–153
   PubMed Web of Science ®Google Scholar
• Kotani T, Umeki K, Matsunga S, Kato E, Ohtaki S. Detection of autoantibodies to thyroid peroxidase in autoimmune thyroid diseases by micro-ELISA and immunoblotting. J Clin Endocrinol Metab 1986; 62: 928–933
   PubMed Web of Science ®Google Scholar
• Kohno Y, Hiyama Y, Shimojo N, Niimi H, Nakajima H, Hosoya T. Autoantibodies to thyroid peroxidase in patients with chronic thyroiditis: effect of antibody binding on enzyme activities. Clin Exp Immunol 1986; 65: 534–541
   PubMed Web of Science ®Google Scholar
• Portman L, Hamada N, Heinrich G, DeGroot L J. Anti-thyroid peroxidase antibody in patients with autoimmune thyroid disease: possible identity with anti-microsomal antibody. J Clin Endocrinol Metab 1985; 61(5)1001–1003
   PubMed Web of Science ®Google Scholar
• Czarnocka B, Ruf J, Ferrand M, Lissitzky S, Carayon P. Interaction of highly purified thyroid peroxidase with anti-microsomal antibodies in autoimmune thyroid diseases. J Endocrinol Invest 1986; 9: 135–138
   PubMed Web of Science ®Google Scholar
• Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, et al. Thyroid peroxidase, an autoantigen with a mosaic structure made of nuclear and mitochondrial gene modules. Emho J 1987; 6(13)4193–4196
   PubMedGoogle Scholar
• Banga J P, Pryce G, Hammond L, Roitt I M. Structure features of the autoantigens involved in thyroid autoimmune disease: the thyroid microsomal/microvillar antigen. Mol Immunol 1985; 22(6)629–642
   PubMed Web of Science ®Google Scholar
• Kajita Y, Morgan D, Parkes A B, Rees Smith B. Labelling and immunoprecipitation of thyroid microsomal antigen. FEBS Letts 1985; 187(2)334–338
   PubMed Web of Science ®Google Scholar
• Hamada N, Grimm C, Mori H, DeGroot L J. Identification of a thyroid microsomal antigen by western blot and immunoprecipitation. J Clin Endocrinol Metab 1985; 61: 120–128
   PubMed Web of Science ®Google Scholar
• Petersen V B, Nakajima Y, Beever K, Rees Smith B. Monoclonal antibodies against human thyroid microsomal antigen and porcine thyroid peroxidase which cross-react with lactoperoxidase and horseradish peroxidase. J Endocrinol 1988; 117(suppl)162
   Google Scholar
• Magnusson R P, Chazenbalk G D, Gestautas J, Seto P, Filetti S, DeGroot J L, et al. Molecular cloning of the complementary deoxyribonucleic acid for human thyroid peroxidase. Mol Endocrinol 1987; 1(11)856–861
   PubMedGoogle Scholar
• Rees Smith B, Nakajima Y, Davenport S M, Petersen V. The role of intrachain disulphide bridges in the antibody binding sites of thyroid microsomal antigenlthyroid peroxidase. J Endocrinol 1988; 117(suppl)153
   Google Scholar
• Hamada N, Jaeduck N, Portmann L, Ito K, DeGroot L J. Antibodies against denatured and reduced thyroid microsomal antigen in autoimmune thyroid disease. J Clin Endocrinol Metab 1987; 64: 230–238
   PubMed Web of Science ®Google Scholar
• Yokoyama N, Taurog A, Klee G G. Thyroid peroxidase and thyroid microsomal autoantibodies. J Clin Endocrinol Metab 1989; 68: 766–773
   PubMed Web of Science ®Google Scholar
• Ruf J, Toubert M E, Czarnocka B, Durand-Gorde J M, Ferrand M, Carayon P. Relationship between immunological structure and biochemical properties of human thyroid peroxidase. Endocrinology 1989; 125(3)1211–1218
   PubMed Web of Science ®Google Scholar
• Doble N D, Banga J P, Pope R, Lalor E, Kilduff P, McGregor A M. Autoantibodies to the thyroid microsomal/thyroid peroxidase antigen are polyclonal and directed to several distinct antigenic sites. Immunology 1988; 64: 23–29
   PubMed Web of Science ®Google Scholar
• Kimura S, Kotani T, McBride O W, Umeki K, Hirai K, Nakayama T, et al. Human thyroid peroxidase: complete cDNA and protein-sequence, chromosome mapping and identification of two alternately-spliced mRNAs. Proc Natl Acad Sci USA 1987; 84: 5555–5559
   PubMed Web of Science ®Google Scholar
• Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, et al. Complete nucleotide sequence of the human thyroid peroxidase-microsomal antigen cDNA. Nucl Acids Res 1987; 15(16)6735
   PubMed Web of Science ®Google Scholar
• Seto P, Hirayu H, Magnusson R P, Bestautas J, Portmann L, DeGroot L J, et al. Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with gene for thyroid peroxidase. J Clin Invest 1987; 80: 1205–1208
   PubMed Web of Science ®Google Scholar
• Ludgate M, Mariotti S, Libert F, Dinsart C, Piccolo P, Santini F, et al. Antibodies to human thyroid peroxidase in autoimmune thyroid disease: studies with a cloned recombinant complementary deoxyribonucleic acid epitope. J Clin Endocrinol and Metab 1989; 68(6)1091–1096
   PubMed Web of Science ®Google Scholar
• Yamada M, Hur S J, Hashnaka K, Tsuneoka K, Saeki T, Nishio C, et al. Isolation and characterization of a cDNA coding for human myeloperoxidase. Arch Biochem Biophys 1987; 255(1)147–155
   PubMed Web of Science ®Google Scholar
• Kimura S, Hong Y-S, Kotani T, Ohtaki S, Kikkawa F. Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry 1989; 4481–4489
   PubMed Web of Science ®Google Scholar
• Kaufman K D, Rapoport B, Seto P, Chazenbalk G D, Magnusson R P. Generation of recombinant, enzymatically active human thyroid peroxidase and its recognition by antibodies in the sera of patients with Hashimoto's thyroiditis. J Clin Invest 1989; 84: 394–403
   PubMed Web of Science ®Google Scholar
• Hata J, Yamashita S, Yagihashi S, Kato M, Kabeno S, Hirai K, et al. Stable high level expression of human thyroid peroxidase in cultured Chinese hamster ovary cells. Biochem Biophvs Res Comm 1989; 164(3)1268–1273
   PubMed Web of Science ®Google Scholar
• Dorrington K J, Munro D S. The long acting thyroid stimulator. Clin Pharmacol Ther 1966; 7: 788–806
   PubMed Web of Science ®Google Scholar
• McKenzie JM. Humoral factors in the pathogenesis of Graves' disease. Physiol Rev 1968; 43: 252–310
   Google Scholar
• Rees Smith B. Thyrotropin receptor antibodies. Receptors and recognition Series B. 1981; Vol. 13: 217–244
   Google Scholar
• Manley S W, Bourke J R, Hawker R W. The thyrotrophin receptor in guinea pig thyroid homogenate: interaction with the long-acting thyroid stimulator. J Endocrinol 1974; 61: 437–445
   PubMed Web of Science ®Google Scholar
• Smith B R, Hall R. Thyroid stimulating immunoglobulins in Graves' disease. Lancet 1974; 2: 427–431
   PubMed Web of Science ®Google Scholar
• Mehdi S Q, Nussey S S. A radio-ligand receptor assay for the long-acting thyroid stimulator. Biochem J 1975; 145: 105–111
   PubMed Web of Science ®Google Scholar
• Furmaniak J, Nakajima Y, Hashim F A, Creagh F M, Davies Jones E, Howells R D, et al. The TSH receptor: structure and interaction with autoantibodies in thyroid disease. Acta Endocrinol (suppl) 1987; 281: 157–165
   PubMedGoogle Scholar
• Rees Smith B, Rickards C R, Davies Jones E, Kajita Y, Buckland P R, Creagh F M, et al. The thyrotropin receptor and its role in Graves' disease. J Endocrinol Invest 1985; 8: 175–182
   PubMed Web of Science ®Google Scholar
• Ji TH. The application of chemical crosslinking on cell membranes and identification of surface receptors. Biochim Biophys Acta 1979; 559: 39–69
   PubMedGoogle Scholar
• Buckland P R, Rickards C R, Howells R D, Davies Jones ED, Rees Smith B. Photoaffinity labelling of the thyrotropin receptor. FEBS Lett 1982; 145: 245–249
   Google Scholar
• Buckland P R, Rees Smith B. A structural comparison of guinca pig thyroid and fat TSH receptors by photoaffinity labelling. FEBS Lett 1984; 166: 109–114
   PubMed Web of Science ®Google Scholar
• Buckland P R, Howells R D, Rickards C R, Rees Smith B. Affinity labelling of the thyrotropin receptor: characterization of the photoactive ligand. Biochem J 1985; 255: 753–760
   Google Scholar
• Buckland P R, Rickards C R, Howells R D, Rees Smith B. Thyrotropin cross-links to the thyrotropin receptor through both the alpha and beta subunits. Biochem J 1986; 235: 879–882
   PubMed Web of Science ®Google Scholar
• Buckland P R, Strickland T W, Pierce J G, Rees Smith B. TSH crosslinks to the TSH receptor through the beta subunit. Endocrinology 1985; 116: 2122–2124
   PubMed Web of Science ®Google Scholar
• Kajita Y, Rickards C R, Buckland P R, Howells R D, Rees Smith B. A structure for the porcine TSH receptor. FEBS Lett 1985; 181: 218–222
   Web of Science ®Google Scholar
• Kajita Y, Rickards C R, Buckland P R, Howells R D, Rees Smith B. Analysis of thyrotropin receptors by photoaffinity labelling: orientation of receptor subunits in the cell membrane. Biochem J 1985; 227: 413–420
   PubMed Web of Science ®Google Scholar
• Davies Jones E, Hashim F A, Kajita Y, Creagh F M, Buckland P R, Petersen V B, et al. Interaction of autoantibodies to thyrotropin receptor with a hydrophilic subunit of the thyrotropin receptor. Biochem J 1985; 228: 111–117
   PubMed Web of Science ®Google Scholar
• Furmaniak J, Hashim F A, Buckland P R, Petersen V B, Beever K, Howells R D, et al. Photoaffinity labelling of the TSH receptor on FRTL, cells. FEBS Lett 1987; 215: 316–322
   PubMed Web of Science ®Google Scholar
• McQuade R, Thomas C G, Nayfeh S N. Further studies on the covalent crosslinking of thyrotropin to its receptor: evidence that both the alpha and beta subunits of thyrotropin are crosslinked to the receptor. Arch Bichem Biohphys 1987; 252: 409–417
   PubMed Web of Science ®Google Scholar
• Carrey EA. B, Hall R. A salt-induced reversible co-operative transition in the pig thyrotropin receptor. Biochem Soc Truns 1978; 6: 1352–1353
   PubMed Web of Science ®Google Scholar
• Pekonen R, Weintraub B D. Thyrotropin receptors on bovine thyroid membranes: two types with different affinities and specificities. Endocrinologr 1979; 105: 352–359
   PubMed Web of Science ®Google Scholar
• Furmaniak J. E, Buckland P R, Howells R D, Rees Smith B. Assessment of the shape and molecular size of TSH-TSH receptor complexes. Mol Cell Endocrinol 1986; 48: 31–38
   PubMed Web of Science ®Google Scholar
• McFarland K C, Sprengel K, Phillips H S, Kohler M, Rosemblit N, Nikolics K, et al. Lutropin-choriongonadotropin receptor: An unusual member of the G protein-coupled receptor family. Science 1989; 245: 494–499
   PubMed Web of Science ®Google Scholar
• Loosfelt H, Misrahi M, Atger M, Salesse R, Tu Vu Mai-Luu Thi M, Jolivet A, et al. Cloning and sequencing of porcine LH-hCG receptor cDNA: variants lacking transmembrane domain. Science 1989; 245: 525–528
   PubMed Web of Science ®Google Scholar
• Lefkowitz R J, Caron M G. Adrenergic receptors Models for the study of receptors coupled to guanine nucleotide regulatory proteins. J Biol Chem 1988; 263(11)4993–4996
   PubMed Web of Science ®Google Scholar
• Ealey P A, Kohn L D, Ekins R P, Marshall N J. Characterisation of monoclonal antibodies derived from lymphocytes from Graves' disease patients in a cytochemical bioassay for thyroid stimulators. J Clioin Encocrinol Metab 1984; 58(5)909–914
   PubMed Web of Science ®Google Scholar
• Libert F, Parmentier M, Lefort A, Dinsart Ch, Van Sande J, Maenhaut C, et al. Selective amplification and cloning of four new members of the G protein-coupled receptor family. Science 1989; 244: 569–572
   PubMed Web of Science ®Google Scholar
• Parmentier M, Libert F, Maenhault C, Lefort An, Gerard C, Perret J, et al. Molecular cloning of the thyrotropin receptor. Science 1989; 246: 1620–1622
   PubMed Web of Science ®Google Scholar
• Parmentier M, Libert F, Maenhaut C, Lefort A, Gerard C, Perret J, et al. Nucleotide sequence of the dog thyrotropin receptor cDNA. Nucleic Acids Research 1989; 17(24)10493
   PubMed Web of Science ®Google Scholar
• Libert F, Lefort A, Gerard C, Parmentier M, Merret J, Ludgate M, et al. sequencing and expression of the human thyrotropin (TSH) receptor: evidence for binding of autoantiodies. Biochem Eiophys Res Commun 1989; 165(3)1250–1255
   PubMed Web of Science ®Google Scholar
• Nagayama Y, Kaufman K D, Seto P, Rapoport B. Molecular cloning, sequence and functional expression of the cDNA for the human thyrotopin receptor. Biochem Biophys Res Commun 1989; 165(3)1184–1190
   PubMed Web of Science ®Google Scholar
• Kusuda S, Dufau M L. Characterisation of ovarian gonadotropin receptor. J Biol Chem 1988; 263(6)3046–3049
   PubMed Web of Science ®Google Scholar
• Smith BR. Characterisation of long-acting thyroid stimulator G binding protein. Eiochim Biophys Acta 1971; 229: 649–662
   PubMed Web of Science ®Google Scholar
• Adlkofer F, Schleusener H, Uher L, Ananos A. Heterogeneity of long acting thyroid stimulating (LATS) activity thyroglobulin antibodies and thyroid microsomal antibodies. Acta Endocrinol (Copenh) 1973; 73: 483–488
   PubMedGoogle Scholar
• Lonergan C, Babiarz D, Burke G. Isoelectric focusing of long acting thyroid stimulator immunoglobulin G. J Clin Endocrinol Metub 1973; 36: 439–444
   PubMed Web of Science ®Google Scholar
• Zakarija M, McKenzie J M. Isoelectric focusing of thyroid-stimulating antibody of Graves' disease. Endocrinology 1978; 103: 1469–1475
   PubMed Web of Science ®Google Scholar
• Creagh F M, Howells R D, Williams S, Didcote S, Hashim F A, Petersen V B, et al. IgG thyrotropin receptor antibody activity in Graves' disease: a study of TSH agonist and antagonist activities by isoelectric focusing. Clin Endocrinol (Oxf) 1986; 24: 79–88
   PubMed Web of Science ®Google Scholar
• Hashim F A, Davies Jones E, Howells R D, Rees Smith B. Isoelectric focusing of the human TSH receptor A subunit. Biosci Rep 1986; 6: 685–689
   PubMed Web of Science ®Google Scholar
• Ambesi-Lmpiombato FS. AM, Coon G H. Culture of hormone-dependent functional epithelial cells from rat thyroids. Proc Natl Acad Sci USA 1980; 77: 3455–3459
   PubMed Web of Science ®Google Scholar
• Petersen V B, Dawes P JD, Rees Smith B, Hall R. The interaction of thyroid-stimulating antibodies with solubilised human thyrotropin receptors. FEBS Lett 1977; 83: 63–67
   PubMed Web of Science ®Google Scholar
• Rickards C R, Buckland P R, Rees Smith B, Hall R. The interaction of Graves' IgG with the thyrotropin receptor. FEBS Lett 1981; 127: 17–21
   PubMed Web of Science ®Google Scholar
• Parkes A B, Kajita Y, Buckland P R, Howells R D, Rickards C R, Creagh F M, et al. Immunoprecipi-tation of TSH-TSH receptor complexes. Clin Endocrinol (Oxf) 1985; 22: 511–520
   PubMed Web of Science ®Google Scholar
• de Bruin T WA, Van Der Heide D. Antithyrotropin receptor antibodies in Graves' disease as demonstrated directly by immunoprecipitation assay. Acta Endocrinof (Copenh) 1983; 102: 49–56
   PubMedGoogle Scholar
• Heyma P, Harrison L C. Precipitation of the thyrotropin receptor and indentification of thyroid autoantigens using Graves' disease immunoglobulins. J Clin Invest 1984; 74: 1090–1097
   PubMed Web of Science ®Google Scholar
• Davies Jones E, Hashim F A, Creagh F M, Williams S E, Rees Smith B. The interaction between the TSH receptor and Graves' sera with TSH agonist or antagonist properties. Mol Cell Endocrinol 1985; 41: 257–261
   PubMed Web of Science ®Google Scholar
• Creagh F M, Parkes A B, Tunn E, Ginsberg J, Hashim F, Rees Smith B. Thyroid stimulation by (Fab), and Fab fragments of TSH receptor antibody. Clin Endocrinol (Oxf) 1985; 23: 175–183
   PubMed Web of Science ®Google Scholar
• Hashim F A, Creagh F M, El Hawrani A, Parkes A B, Buckland P R, Rees Smith B. Characterization of TSH anatagonist activity in the serum of patients with thyroid disease. Clin Endocrinol (Oxf) 1986; 25: 275–281
   PubMed Web of Science ®Google Scholar
• Harrison L C, Flier J S, Roth J, Karlsson F A, Kahn C R. Immunoprecipitation of the insulin receptor: a sensitive assay for receptor antibodies and a specific technique for receptor identification. J Clin Endocrinol Metab 1979; 48: 59–65
   PubMed Web of Science ®Google Scholar