Responsiveness to Thyroid Hormone is Enhanced in Rat Hepatocytes Cultured as Spheroids Compared with that in Monolayers: Altered Responsiveness to Thyroid Hormone Possibly Involves Complex Formed on Thyroid Hormone Response Elements

Thyroid ◽  
1999 ◽  
Vol 9 (9) ◽  
pp. 959-967 ◽  
Author(s):  
MASAFUMI MENJO ◽  
SHUNSUKE YAMAGUCHI ◽  
YOSHIHARU MURATA ◽  
YOSHITAKA HAYASHI ◽  
TAKASHI NAGAYA ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Rat Hepatocytes ◽  
Hormone Response ◽  
Response Elements ◽  
Hormone Response Elements

scholarly journals Different Configurations of Specific Thyroid Hormone Response Elements Mediate Opposite Effects of Thyroid Hormone and GC-1 on Gene Expression

Endocrinology ◽  
2005 ◽  
Vol 146 (11) ◽  
pp. 4926-4933 ◽  
Author(s):  
Bernd Gloss ◽  
Gisele Giannocco ◽  
Eric A. Swanson ◽  
Anselmo S. Moriscot ◽  
Grazia Chiellini ◽  
...  
Keyword(s):  
Gene Expression ◽  
Thyroid Hormone ◽  
Hormone Response ◽  
Response Elements ◽  
Hormone Response Elements

Regulation of regional expression in rat brain PC2 by thyroid hormone/characterization of novel negative thyroid hormone response elements in the PC2 promoter

2005 ◽  
Vol 288 (1) ◽  
pp. E236-E245 ◽  
Author(s):  
Xiaoxiong Shen ◽  
Qiao-Ling Li ◽  
Gregory A. Brent ◽  
Theodore C. Friedman
Keyword(s):  
Retinoic Acid ◽  
Thyroid Hormone ◽  
Thyroid Hormone Receptor ◽  
Specific Binding ◽  
Gh3 Cells ◽  
Mrna Levels ◽  
Hormone Response ◽  
Thyroid Status ◽  
Response Elements ◽  
Hormone Response Elements

The prohormone convertases (PCs) PC1 and PC2 are involved in the tissue-specific endoproteolytic processing of neuropeptide precursors within the secretory pathway. We previously showed that changes in thyroid status altered pituitary PC2 mRNA and that this regulation was due to triiodothyronine-dependent interaction of the thyroid hormone receptor (TR) with negative thyroid hormone response elements (nTREs) contained in a large proximal region of the human PC2 promoter. In the current study, we examined the in vivo regulation of brain PC2 mRNA by thyroid status and found that 6- n-propyl-2-thiouracil-induced hypothyroidism stimulated, whereas thyroxine-induced hyperthyroidism suppressed, PC2 mRNA levels in the rat hypothalamus and cerebral cortex. To address the mechanism of T3 regulation of the PC2 gene, we used human PC2 (hPC2) promoter constructs transiently transfected into GH3 cells and found that triiodothyronine negatively and 9- cis-retinoic acid positively regulated hPC2 promoter activity. EMSAs, using purified TRα1 and retinoid X receptor-β (RXRβ) proteins demonstrated that TRα bound the distal putative nTRE-containing oligonucleotide in the PC2 promoter, and RXR bound to both nTRE-containing oligonucleotides. EMSAs with oligonucleotides containing deletion mutations of the nTREs demonstrated that the binding to TR and RXR separately is reduced, but specific binding to TR and RXR together persists even with deletion of each putative nTRE. We conclude that there are two novel TRE-like sequences in the hPC2 promoter and that these regions act in concert in a unique manner to facilitate the effects of thyroid hormone and 9- cis-retinoic acid on PC2.

The function of retinoid X receptors on negative thyroid hormone response elements

1997 ◽  
Vol 128 (1-2) ◽  
pp. 85-96 ◽  
Author(s):  
Teiji Takeda ◽  
Takeshi Nagasawa ◽  
Takahide Miyamoto ◽  
Kiyoshi Hashizume ◽  
Leslie J DeGroot
Keyword(s):  
Thyroid Hormone ◽  
Hormone Response ◽  
Retinoid X Receptors ◽  
Response Elements ◽  
Hormone Response Elements ◽  
X Receptors
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