Literature DB >> 2453350

Monoclonal antibodies to the thyrotropin receptor raised by an autoantiidiotypic protocol and their relationship to monoclonal autoantibodies from Graves' patients.

B L Hill1, B F Erlanger.   

Abstract

Monoclonal antibodies that bind to the TSH receptor were obtained by an autoantiidiotypic approach in which immunization of BALB/c mice was performed with mixtures of bovine (b) and human (h) TSH. Two of 28 positive wells were selected for cloning and characterization: D2 and 4G11. Their antiidiotypic character was evidenced by TSH-inhibitable binding to affinity-purified polyclonal anti-TSH. The specificity of D2 and 4G11 for the hormone-binding region of the TSH receptor was demonstrated by several findings: 1) they inhibited the binding of [125I]iodo-bTSH to receptor in a dose-dependent manner; 2) their binding to partially purified thyroid plasma membranes could be completely inhibited by bTSH and hTSH; and 3) they inhibited the TSH-dependent growth and adenylate cyclase stimulation in FRTL-5 cells in a dose-dependent manner. By Western blot analysis of bovine thyroid membranes, D2 bound to a polypeptide of 188,000-195,000 mol wt under nonreducing conditions and 54,000-59,000 mol wt after treatment of membranes with beta-mercaptoethanol; the 4G11 epitope was undetectable. Scatchard analysis of the binding of 125I-labeled antibodies to receptor showed that 4G11 bound to a single site with a Kd of 5.7 X 10(-9) M, whereas D2 showed complex binding characterized by high affinity (Kd = 1.74 X 10(-11) M) and low affinity (Kd = 1.3 X 10(-8) M) sites. Binding studies in which D2 and 4G11 competed with each other for the TSH receptor showed mutual but unequal inhibition. The data suggest that portions of the D2 and 4G11 epitopes overlap, but that there is a high affinity binding site(s) for D2 for which 4G11 competes less effectively. The binding of D2 and 4G11 to TSH receptor was inhibited by monoclonal antibodies secreted by Graves' heterohybridomas, showing that D2 and 4G11 share characteristics with autoantibodies of Graves' disease and lending support to the hypothesis that idiotypic network interactions may play a role in the pathogenesis of Graves' disease.

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Year:  1988        PMID: 2453350     DOI: 10.1210/endo-122-6-2840

Source DB:  PubMed          Journal:  Endocrinology        ISSN: 0013-7227            Impact factor:   4.736


  5 in total

1.  Two-subunit structure of the human thyrotropin receptor.

Authors:  H Loosfelt; C Pichon; A Jolivet; M Misrahi; B Caillou; M Jamous; B Vannier; E Milgrom
Journal:  Proc Natl Acad Sci U S A       Date:  1992-05-01       Impact factor: 11.205

2.  ANCA patients have T cells responsive to complementary PR-3 antigen.

Authors:  Jiajin Yang; David J Bautz; Sofia Lionaki; Susan L Hogan; Hyunsook Chin; Roland M Tisch; John L Schmitz; Barrak M Pressler; J Charles Jennette; Ronald J Falk; Gloria A Preston
Journal:  Kidney Int       Date:  2008-07-02       Impact factor: 10.612

Review 3.  Autoantigen complementarity: a new theory implicating complementary proteins as initiators of autoimmune disease.

Authors:  William F Pendergraft; Barrak M Pressler; J Charles Jennette; Ronald J Falk; Gloria A Preston
Journal:  J Mol Med (Berl)       Date:  2004-12-11       Impact factor: 4.599

4.  A monoclonal antibody recognizing an epitope shared by receptors for growth hormone, prolactin, interleukin 2 and interleukin 6.

Authors:  S A Longhi; M E Miranda; M G Gobet; L A Retegui
Journal:  Mol Cell Biochem       Date:  1999-05       Impact factor: 3.396

5.  Longitudinal studies of patients with ANCA vasculitis demonstrate concurrent reactivity to complementary PR3 protein segments cPR3m and cPR3C and with no reactivity to cPR3N.

Authors:  Peter Hewins; Frances Belmonte; J Charles Jennette; Ronald J Falk; Gloria A Preston
Journal:  Autoimmunity       Date:  2010-08-16       Impact factor: 2.815

  5 in total

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