scholarly journals Polychlorinated Biphenyls 105 and 118 Form Thyroid Hormone Receptor Agonists after Cytochrome P4501A1 Activation in Rat Pituitary GH3 Cells

2007 ◽  
Vol 115 (11) ◽  
pp. 1623-1630 ◽  
Author(s):  
Kelly J. Gauger ◽  
Stefanie Giera ◽  
David S. Sharlin ◽  
Ruby Bansal ◽  
Eric Iannacone ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Polychlorinated Biphenyls ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Gh3 Cells ◽  
Cytochrome P4501a1 ◽  
Receptor Agonists ◽  
Rat Pituitary

scholarly journals Polychlorinated Biphenyls Suppress Thyroid Hormone Receptor-mediated Transcription through a Novel Mechanism

2004 ◽  
Vol 279 (18) ◽  
pp. 18195-18202 ◽  
Author(s):  
Wataru Miyazaki ◽  
Toshiharu Iwasaki ◽  
Akira Takeshita ◽  
Yoichiro Kuroda ◽  
Noriyuki Koibuchi
Keyword(s):  
Thyroid Hormone ◽  
Polychlorinated Biphenyls ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor

scholarly journals The Amelioration of Hepatic Steatosis by Thyroid Hormone Receptor Agonists Is Insufficient to Restore Insulin Sensitivity in Ob/Ob Mice

PLoS ONE ◽  
2015 ◽  
Vol 10 (4) ◽  
pp. e0122987 ◽  
Author(s):  
Alexandro J. Martagón ◽  
Jean Z. Lin ◽  
Stephanie L. Cimini ◽  
Paul Webb ◽  
Kevin J. Phillips
Keyword(s):  
Insulin Sensitivity ◽  
Thyroid Hormone ◽  
Hepatic Steatosis ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Receptor Agonists

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 Transcriptomic and phenotypic profiling in developing zebrafish exposed to thyroid hormone receptor agonists

2018 ◽  
Vol 77 ◽  
pp. 80-93 ◽  
Author(s):  
Derik E. Haggard ◽  
Pamela D. Noyes ◽  
Katrina M. Waters ◽  
Robert L. Tanguay
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Receptor Agonists
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