In Vivo Effects of TSH Receptor Antibodies in Xenotransplanted Human Thyroid Tissue

2009 ◽  
Vol 100 (04/05) ◽  
pp. 41-44
Author(s):  
P.-M. Schumm-Draeger ◽  
H. J. C. Wenisch ◽  
K. H. Usadel
Keyword(s):  
Thyroid Tissue ◽  
Tsh Receptor ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
In Vivo Effects ◽  
Receptor Antibodies ◽  
Tsh Receptor Antibodies

Anti-TSH receptor antibodies in Graves' disease modulate the kinetic behaviour of autologous thyroid TSH receptors. Evidence of the IgG-induced cross-linkage of autologous TSH receptors

1984 ◽  
Vol 105 (3) ◽  
pp. 330-340 ◽  
Author(s):  
Tjerk W. A. de Bruin ◽  
Daan van der Heide ◽  
Maria C. Krol
Keyword(s):  
Binding Sites ◽  
Plasma Membranes ◽  
Tsh Receptor ◽  
Human Thyroid ◽  
Graves Disease ◽  
Kinetic Behaviour ◽  
High Affinity ◽  
Cross Linkage ◽  
Receptor Antibodies ◽  
Tsh Receptor Antibodies

Abstract. The effect of the anti-TSH receptor antibodies present in the sera of 8 patients with Graves' disease on the affinity constant (Ka) and the number (R) of TSH receptors in autologous human thyroid plasma membranes was investigated. Kinetic analysis of [125I]bTSH binding to human thyroid plasma membranes in the presence of autologous Graves' and normal gammaglobulins was carried out by means of a computer fitting programme. Analysis of the TSH-TSH receptor interaction in the presence of TSH alone yielded curvilinear Scatchard plots, indicating the existence of two independent classes of binding sites (high affinity Ka: 8.5 ± 4.8 × 108 m−1; low affinity Ka: 5.3 ± 2.7 × 106 m−1). Similarly the Scatchard plot for this interaction in the presence of normal gammaglobulins is also curvilinear. Linear Scatchard plots, indicating the existence of only one class of high affinity TSH binding sites (Ka: 3.5 ± 1.8 × 108 m−1), were obtained for both autologous gammaglobulins and pure IgG from 8 patients with Graves' disease. The number of high affinity TSH binding sites in the presence of Graves' gammaglobulins had increased on the average by a factor 3.76 ± 0.74 (sd) with respect to the number found in the presence of normal gammaglobulins. This marked change in the kinetic behaviour of the TSH binding sites provided evidence that there is a direct interaction between anti-TSH receptor antibodies and autologous TSH receptors. Divalency of Graves' IgG or linkage of Fab fragments by anti-Fab antiserum proved to be necessary to produce this specific change in the kinetic behaviour of TSH binding sites. Graves' IgG monovalent Fab and Fc fragments had no effect. We suggest that the mechanism by which anti-TSH receptor antibodies in Graves' disease mimick the biological action of TSH is the IgG-induced cross-linkage of TSH receptors.

Immunoprecipitation Isolates Multiple TSH Receptor Forms from Human Thyroid Tissue

Thyroid ◽  
1995 ◽  
Vol 5 (2) ◽  
pp. 101-105 ◽  
Author(s):  
R.F. GROSSMAN ◽  
T. BAN ◽  
Q.Y. DUH ◽  
S. TEZELMAN ◽  
G. JOSSART ◽  
...  
Keyword(s):  
Thyroid Tissue ◽  
Tsh Receptor ◽  
Human Thyroid ◽  
Human Thyroid Tissue

STUDIES OF THE TSH RADIORECEPTOR ASSAY

1979 ◽  
Vol 90 (2) ◽  
pp. 217-226 ◽  
Author(s):  
Gildon N. Beall ◽  
Inder J. Chopra ◽  
David H. Solomon ◽  
W. James Irvine ◽  
Sally R. Kruger
Keyword(s):  
Protease Inhibitor ◽  
Specific Binding ◽  
Thyroid Tissue ◽  
Radioreceptor Assay ◽  
Tsh Receptor ◽  
Human Thyroid ◽  
Post Mortem ◽  
Human Thyroid Tissue ◽  
Several Variables ◽  
Bovine Tsh

ABSTRACT We have examined several variables in the reagents and procedures used in the TSH radioreceptor assay, the binding of iodinated TSH to its thyroidal receptor. We found that iodinated bovine TSH (S.A. 30 U/mg) was more effectively bound to receptor than iodinated human TSH (S.A. 7.3 U/mg). Iodination of TSH with the Bolton-Hunter acylation method apparently prevented binding to TSH receptor. Surgically removed human thyroid tissue specifically bound 10.3 ±1.0 (mean ± sem) of added [125I]TSH, but post-mortem human thyroid bound only 3.9 ± 0.4% of [125I]TSH (P< 0.001). Maximal binding of [125I]TSH was found at pH 5.8. Many tissue preparations contained activity, possibly due to proteases, which inactivated TSH, and inclusion of a protease inhibitor, aprotinin, significantly increased specific binding.

The TSH receptor: Structure and interaction with autoantibodies in thyroid disease

1987 ◽  
Vol 116 (1_Suppl) ◽  
pp. S157-S165 ◽  
Author(s):  
J. Furmaniak ◽  
Y. Nakajima ◽  
F. A. Hashim ◽  
F. M. Creagh ◽  
E. Davies Jones ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Thyroid Tissue ◽  
Tsh Receptor ◽  
Sds Page ◽  
Affinity Labelling ◽  
Stokes Radius ◽  
A Subunit ◽  
Receptor Antibodies ◽  
Derivatives Of ◽  
Tsh Receptor Antibodies

Abstract. Studies of the TSH receptor using affinity labelling with photoactive derivatives of TSH and analysis by SDS-PAGE have shown that the receptor contains 2 subunits (A and B), linked by a disulphide bridge. Similar results are obtained with TSH receptors from human, porcine and guinea pig thyroid tissue and from guinea pig fat. Analysis of affinity labelled receptors under non-denaturing conditions suggest that subunits additional to the A and B subunits are not present. Hydrodynamic measurements indicate that the receptor A subunit has an approximately spherical structure (Stokes' radius 70Å) and when this interacts with TSH (an elongated structure with Stokes' radius 56Å) a very elongated complex (Stokes' radius 104Å) is formed. Isoelectric focusing studies of the TSH receptor A subunit, TSH and TSH receptor antibodies indicate that charge-charge interactions are of considerable importance in the binding of hormone and antibody to the receptor.

Evidence of in vivo iodine-induced hyperthyroidism in hyperfunctional autoimmune and autonomous human thyroid tissue xenotransplanted to nude mice

1987 ◽  
Vol 65 (4) ◽  
pp. 197-201 ◽  
Author(s):  
P. -M. Schumm-Draeger ◽  
R. Senekowitsch ◽  
F. -D. Maul ◽  
H. J. C. Wenisch ◽  
C. R. Pickardt ◽  
...  
Keyword(s):  
Nude Mice ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Human Thyroid Tissue

IODOTHYRONINE CONTENT OF HUMAN THYROID ALBUMIN

1976 ◽  
Vol 81 (2) ◽  
pp. 288-297
Author(s):  
Colette Thomas-Morvan
Keyword(s):  
Thyroid Hormones ◽  
Gel Electrophoresis ◽  
Thyroid Tissue ◽  
Iodine Concentration ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Normal Human ◽  
The Difference ◽  
Radioactive Measurement

ABSTRACT Stable thyroid hormones (T4 and T3)1) have been demonstrated in pure albumin isolated from normal human thyroid tissue iodinated in vivo. Five samples of albumin were separated from other thyroid proteins by acrylamide gel electrophoresis. After pronase hydrolysis, the content of Thyroid hormones was measured chemically (T4 + T3) as well as by competitive radioactive measurement (T4) and radioimmunoassay (T3). The purity of the albumin and validity of these measurements were confirmed by different techniques. The synthesis of thyroid hormones is not therefore a property unique to Tg and may occur in albumin. However the amount of iodothyronines in the albumin (average 0.004 residue per molecule) is much less than that found in Tg (0.5 residue per molecule). In the albumin as in Tg the number of hormone residues per molecule is proportional to the number of atoms of iodine. At an equivalent iodine concentration, the albumin seems capable of forming the thyroid hormones as well as Tg. The difference between these two proteins, in their capacity to synthesize thyroid hormones, seems to depend on their capacity for iodination. This difference of iodination does not seem to be linked with the number of tyrosyl residues, but might be related to the position of these residues.

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