scholarly journals Large scale purification of the nuclear thyroid hormone receptor from rat liver and sequence-specific binding of the receptor to DNA.

1988 ◽  
Vol 263 (19) ◽  
pp. 9409-9417
Author(s):  
J W Apriletti ◽  
J D Baxter ◽  
T N Lavin
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Hormone Receptor ◽  
Large Scale ◽  
Thyroid Hormone Receptor ◽  
Specific Binding

Association of the thyroid hormone receptor with rat liver chromatin

Biochemistry ◽  
1981 ◽  
Vol 20 (24) ◽  
pp. 6781-6789 ◽  
Author(s):  
Donald B. Jump ◽  
Steven Seelig ◽  
Harold L. Schwartz ◽  
Jack H. Oppenheimer
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Liver Chromatin

Stabilization, accurate determination, and purification of rat liver nuclear thyroid hormone receptor

1989 ◽  
Vol 120 (2) ◽  
pp. 237-243 ◽  
Author(s):  
K. Ichikawa ◽  
J. Brtko ◽  
L. J. DeGroot ◽  
K. Hashizume ◽  
T. Yamada
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Hormone Receptor ◽  
Half Life ◽  
Thyroid Hormone Receptor ◽  
Binding Capacity ◽  
Accurate Determination ◽  
Nuclear Extract ◽  
Heat Inactivation ◽  
Accurate Estimation

ABSTRACT Rat liver nuclear thyroid hormone receptor lost 3,5,3′-tri-iodo-l-thyronine (T3)-binding activity with a half-life of 14 days, 4 h, 139 min, 62 min, 16 min or 6 min at 0, 36, 38, 40, 43 or 45 °C respectively, when present in crude nuclear extracts. Glycerol increased the half-life of the receptor during heat inactivation. Protection was reversible by removing the glycerol. The receptor was unstable at a pH below 6·0 or above 10·0. We also found a loss of the receptor activity during the separation of bound and free hormone using the resin test. Of several conditions tested for the separation of bound and free hormone, the addition of heated nuclear extract gave the most accurate estimation of bound hormone when using the resin test. Using these characteristics of the receptor, we purified the receptor to 1220 pmol T3-binding capacity/mg protein with a final yield of 14·6 μg/4 kg rat liver. Journal of Endocrinology (1989) 120, 237–243

scholarly journals A Large-Scale Population-Based Analysis of Common Genetic Variation in the Thyroid Hormone Receptor Alpha Locus and Bone

Thyroid ◽  
2012 ◽  
Vol 22 (2) ◽  
pp. 223-224 ◽  
Author(s):  
Marco Medici ◽  
Fernando Rivadeneira ◽  
Wendy M. van der Deure ◽  
Albert Hofman ◽  
Joyce B.J. van Meurs ◽  
...  
Keyword(s):  
Genetic Variation ◽  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Large Scale ◽  
Thyroid Hormone Receptor ◽  
Population Based ◽  
Common Genetic Variation ◽  
Receptor Alpha ◽  
Scale Population

Thyroid hormone receptor β1 gene expression is increased by Dexamethasone at transcriptional level in rat liver

Life Sciences ◽  
2006 ◽  
Vol 78 (22) ◽  
pp. 2584-2594 ◽  
Author(s):  
M.M. Montesinos ◽  
C.G. Pellizas ◽  
M.L. Vélez ◽  
S. Susperreguy ◽  
A.M. Masini-Repiso ◽  
...  
Keyword(s):  
Gene Expression ◽  
Thyroid Hormone ◽  
Rat Liver ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Transcriptional Level

scholarly journals Thyroid hormone regulation of prohormone convertase 1 (PC1): regional expression in rat brain and in vitro characterization of negative thyroid hormone response elements

2004 ◽  
Vol 33 (1) ◽  
pp. 21-33 ◽  
Author(s):  
X Shen ◽  
QL Li ◽  
GA Brent ◽  
TC Friedman
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Specific Binding ◽  
Gh3 Cells ◽  
Mrna Levels ◽  
Hormone Response ◽  
Mobility Shift ◽  
Response Elements ◽  
Hormone Response Elements

Most pro-neuropeptides are processed by the prohormone convertases, PC1 and PC2. We previously reported that changes in thyroid status altered anterior pituitary PC1 mRNA and this regulation was due to triiodothyronine (T(3))-dependent interaction of thyroid hormone receptor (TR) with negative thyroid hormone response elements (nTREs) contained in a large region of the human PC1 promoter. In this study, we demonstrated that hypothyroidism stimulated, while hyperthyroidism suppressed, PC1 mRNA levels in rat hypothalamus and cerebral cortex, but not in hippocampus. In situ hybridization was used to confirm real-time PCR changes and localize the regulation within the hypothalamus and cortex. Using a human PC1 (hPC1) promoter construct (with and without deletions in two regions that each contain a negative TRE) transiently transfected into GH3 cells, we found that T(3) negatively regulated hPC1 promoter activity, and this regulation required both of these two regions. Electrophoretic mobility shift assays (EMSAs) using purified thyroid hormone receptor alpha1 (TRalpha1) and retinoid X receptor beta (RXRbeta) proteins demonstrated that RXR and TRalpha both bound the PC1 promoter. Addition of TRalpha1/RXRbeta to the wild-type PC1 probe demonstrated binding as both homodimers and a heterodimer. EMSAs with oligonucleotides containing deletion mutations of the putative nTREs demonstrated that the proximal nTRE binds more strongly to TR and RXR than the distal nTRE, but that both regions exhibit specific binding. We conclude that there are multiple novel TRE-like sequences in the hPC1 promoter and that these regions act in a unique manner to facilitate the negative effect of thyroid hormone on PC1.

scholarly journals The Thyroid Hormone Receptor-β Agonist GC-1 Induces Cell Proliferation in Rat Liver and Pancreas

Endocrinology ◽  
2006 ◽  
Vol 147 (7) ◽  
pp. 3211-3218 ◽  
Author(s):  
Amedeo Columbano ◽  
Monica Pibiri ◽  
Manuela Deidda ◽  
Costanza Cossu ◽  
Thomas S. Scanlan ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Thyroid Hormone ◽  
Rat Liver ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Liver And Pancreas ◽  
Thyroid Hormone Receptor Β
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