Induction of Hyperthyroxinemia in Balb/C but not in Several Other Strains of Mice

We recently expressed the extracellular domain of the human TSHR (ETSHR) protein using a baculovirus expression system and purified it to homogeneity. The ETSHR specifically binds both TSH and antibodies to TSHR. In the present study, C57BL/6J, SJL/J, BALB/cJ and BlOBR.SgSnJ mice were immunized with...

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Veröffentlicht in:Autoimmunity (Chur, Switzerland) Switzerland), 1994, Vol.18 (2), p.103-112
Hauptverfasser: Wagle, Neelam M., Dallas, John S., Seetharamaiah, Gattadahalli S., Fan, Ji-Lao, Desai, Rajesh K., Memar, Omeed, Rajaraman, Srinivasan, Prabhakar, Bellur S.
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container_end_page 112
container_issue 2
container_start_page 103
container_title Autoimmunity (Chur, Switzerland)
container_volume 18
creator Wagle, Neelam M.
Dallas, John S.
Seetharamaiah, Gattadahalli S.
Fan, Ji-Lao
Desai, Rajesh K.
Memar, Omeed
Rajaraman, Srinivasan
Prabhakar, Bellur S.
description We recently expressed the extracellular domain of the human TSHR (ETSHR) protein using a baculovirus expression system and purified it to homogeneity. The ETSHR specifically binds both TSH and antibodies to TSHR. In the present study, C57BL/6J, SJL/J, BALB/cJ and BlOBR.SgSnJ mice were immunized with the recombinant ETSHR or an equivalent amount of control antigen. All strains of mice produced high titers of antibody against the TSHR protein which were capable of blocking the binding of TSH to native TSHR. However, only BALB/cJ mice showed significantly elevated levels of thyroxine in their sera compared to the control mice. Similarly, BALB/cJ mice primed with ETSHR and then challenged with thyroid membranes showed significantly elevated levels of thyroxine. In addition, histopathological examination of thyroid glands from affected mice showed morphological changes characterized by hydropic and subnuclear vacuolar changes and focal scalloping, with no apparent inflammation or glandular destruction. Moreover, mice with elevated thyroxine levels showed increased in vivo thyroidal uptake of l31 Iodine. Together, these data suggest that BALB/cJ mice are susceptible to the induction of hyperthyroxinemia.
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The ETSHR specifically binds both TSH and antibodies to TSHR. In the present study, C57BL/6J, SJL/J, BALB/cJ and BlOBR.SgSnJ mice were immunized with the recombinant ETSHR or an equivalent amount of control antigen. All strains of mice produced high titers of antibody against the TSHR protein which were capable of blocking the binding of TSH to native TSHR. However, only BALB/cJ mice showed significantly elevated levels of thyroxine in their sera compared to the control mice. Similarly, BALB/cJ mice primed with ETSHR and then challenged with thyroid membranes showed significantly elevated levels of thyroxine. In addition, histopathological examination of thyroid glands from affected mice showed morphological changes characterized by hydropic and subnuclear vacuolar changes and focal scalloping, with no apparent inflammation or glandular destruction. Moreover, mice with elevated thyroxine levels showed increased in vivo thyroidal uptake of l31 Iodine. 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identifier ISSN: 0891-6934
ispartof Autoimmunity (Chur, Switzerland), 1994, Vol.18 (2), p.103-112
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source MEDLINE; Taylor & Francis:Master (3349 titles)
subjects Animals
Antibodies - analysis
Antibody Formation
Binding, Competitive
Cell Membrane - immunology
Enzyme-Linked Immunosorbent Assay
Female
Graves' disease
Hyperthyroxinemia
Hyperthyroxinemia - immunology
Immunization
Immunoglobulins, Thyroid-Stimulating - blood
Immunoglobulins, Thyroid-Stimulating - immunology
Mice
Mice, Inbred BALB C - immunology
Mice, Inbred C57BL
Mice, Inbred Strains
Receptors, Thyrotropin - immunology
Recombinant Proteins - immunology
Thyroid Gland - immunology
Thyroid Gland - pathology
Thyrotropin receptor
Thyroxine - blood
title Induction of Hyperthyroxinemia in Balb/C but not in Several Other Strains of Mice
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