In vivo Effect of Thyroid-Stimulating Hormone on Human Thyroid Tissue in Nude Mice1

2015 ◽  
pp. 109-122 ◽  
Author(s):  
Henning Dralle
Keyword(s):  
Thyroid Tissue ◽  
Thyroid Stimulating Hormone ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Stimulating Hormone

Estrogen and thyroid-stimulating hormone (TSH) receptors in neoplastic and nonneoplastic human thyroid tissue

1985 ◽  
Vol 38 (2) ◽  
pp. 89-96 ◽  
Author(s):  
Orlo H. Clark ◽  
Patricia L. Gerend ◽  
Mary Davis ◽  
Peter E. Goretzki ◽  
Philip G. Hoffman
Keyword(s):  
Thyroid Tissue ◽  
Thyroid Stimulating Hormone ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Stimulating Hormone

COMPARATIVE STUDIES ON THE REDUCTION OF THE RESPONSE TO THE LONG-ACTING THYROID STIMULATOR BY SOLUBLE FRACTIONS FROM HUMAN, OVINE, BOVINE AND PORCINE THYROIDS

1973 ◽  
Vol 59 (3) ◽  
pp. 579-592 ◽  
Author(s):  
SUSAN DIRMIKIS ◽  
D. S. MUNRO
Keyword(s):  
Thyroid Tissue ◽  
Thyroid Stimulating Hormone ◽  
Binding Activity ◽  
Human Thyroid ◽  
Detectable Effect ◽  
Freezing And Thawing ◽  
Human Thyroid Tissue ◽  
Long Acting ◽  
S Peak ◽  
Soluble Fractions

SUMMARY The response to the long-acting thyroid stimulator (LATS) but not to bovine thyroid-stimulating hormone (TSH) was reduced by soluble fractions from human, ovine, bovine and porcine thyroids. A significant increase in the capacities of human, ovine and bovine thyroidal soluble fractions to reduce the response to LATS occurred upon freezing and thawing of thyroidal homogenates. In human thyroids this change took place predominantly in the 4 S peak, which was the most active of the soluble fractions from frozen human thyroid tissue. However, in ovine and bovine thyroids, the change could be accounted for mainly by components of the 19 S peak, this being also the most active of the soluble fractions of frozen animal thyroids in reducing the response to LATS. Whereas human LATS-binding activity (LAA) was destroyed by heating at 56 °C for 1 h the capacities of ovine, bovine and porcine thyroidal soluble fractions (or their 19 S components) to reduce the response to LATS were not affected by this treatment. The interaction between human LAA and LATS can be reversed by 2 m-NaSCN, which also destroys LAA. However, NaSCN had no detectable effect on the capacities of soluble fractions (or their 19 S components) from ovine, bovine and porcine thyroids to reduce the response to LATS. The reduction of the response to LATS by very high concentrations of 4 S components, from frozen ovine thyroidal homogenate, was partially reversed by 2 m-NaSCN. Thus ovine thyroids may be a source of a substance with the properties of human LAA, but with a yield of approximately 10% of that obtained from human thyroid tissue. It was concluded that ovine, bovine and porcine thyroidal soluble fractions reduced the response to LATS mainly by mechanisms other than binding to LAA.

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.

Iodine-Induced Expression of Immunoglobulin Supergene Family in Normal Human Thyroid Tissue in vivo

1996 ◽  
pp. 32-35
Author(s):  
Petra-Maria Schumm-Draeger ◽  
Hans-Peter Fortmeyer ◽  
Hubertus Johannes Christoph Wenisch ◽  
Claudia Müller ◽  
Klaus Henning Usadel
Keyword(s):  
Thyroid Tissue ◽  
Human Thyroid ◽  
Induced Expression ◽  
Human Thyroid Tissue ◽  
Normal Human ◽  
Immunoglobulin Supergene Family ◽  
Supergene Family

EFFECT OF ENDOGENOUS THYROID STIMULATING HORMONE LEVELS ON THE SECRETION OF THYROID HORMONES IN MAN

1979 ◽  
Vol 92 (1) ◽  
pp. 73-84 ◽  
Author(s):  
A. Carpi ◽  
R. Bianchi ◽  
G. C. Zucchelli ◽  
L. Del Corso ◽  
C. Levanti ◽  
...  
Keyword(s):  
Thyroid Tissue ◽  
Serum Levels ◽  
Progressive Increase ◽  
Thyroid Stimulating Hormone ◽  
Human Thyroid ◽  
Surgical Removal ◽  
Thyroid Secretion ◽  
Serum Tsh ◽  
Stimulation Of ◽  
Stimulating Hormone

ABSTRACT The effect of endogenous thyroid stimulating hormone (TSH) on the thyroid secretion of triiodothyronine (T3) and thyroxine (T4) was evaluated by serial determinations of serum T3, T4 and TSH concentrations in the following groups of patients: a) three patients submitted to surgical removal of a solitary, autonomous thyroid nodule which had completely inhibited the extranodular tissue; b) five subjects, with the same disease, in whom functional recovery of the extranodular tissue was induced by increased circulating TSH levels, produced by treatment with methimazole; c) one patient submitted to hemithyroidectomy for multinodular goitre; d) two hyperthyroid patients who had been treated with methimazole. In all these patients serum T3 and T4 levels progressively decreased, with a consequent progressive increase in serum TSH concentrations, leading to stimulation of the thyroid gland. During this TSH-induced stimulation of thyroid tissue, a significant positive correlation was found between the serum TSH concentrations and the corresponding ratio betwen the serum levels of T3 and T4 (T3/T4), both within each patient group (P < 0.001) and among all patients (P < 0.001). The same correlation also governs the relationship between the TSH and the T3/T4 values of 34 euthyroid control subjects and one patient with incipient hypothyroidism. These data strongly suggest that endogenous TSH can induce a preferential secretion of T3 over T4 by the human thyroid.

Sign in / Sign up

Export Citation Format

Share Document