Ontogeny of thyroid hormone receptors and c-erbA expression during brown adipose tissue development: evidence of fetal acquisition of the mature thyroid status

Tuca, A

doi:10.1210/en.132.5.1913

Cited by 11 publications

(14 citation statements)

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“…Regulation of fat mass is controlled by multiple neuroendocrine signals. Thyroid hormones are predominantly considered as hormones involved in adipose tissue development and metabolism (Levacher et al, 1984;Tuca et al, 1993). Their most obvious and well-known action is an increase in basal energy expenditure obtained acting on adipose tissue metabolism.…”

Section: Discussionmentioning

confidence: 99%

Mapping, expression and regulation of the TRα gene in porcine adipose tissue

Cai¹,

Sheng²,

Zhang³

et al. 2011

Genet. Mol. Res.

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Section: Discussionmentioning

confidence: 99%

Mapping, expression and regulation of the TRα gene in porcine adipose tissue

Cai¹,

Sheng²,

Zhang³

et al. 2011

Genet. Mol. Res.

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“…PPAR activity may be released from suppression by TR due to decreased number of TR during fasting, resulting in the increased transcriptional levels of enzymes regulating fatty acid ␤-oxidation such as aox gene. Furthermore, TR expression is regulated by hormones (54) and strictly controlled during ontogeny and development (55)(56)(57)(58). TRs exert their effects on lipid metabolism through convergence of PPAR signaling pathways.…”

Section: Table I Protein Expression Of Tra1 and Its Dbd Mutant In Cosmentioning

confidence: 99%

Inhibition of Peroxisome Proliferator Signaling Pathways by Thyroid Hormone Receptor

Miyamoto¹,

Kaneko²,

Kakizawa

et al. 1997

Journal of Biological Chemistry

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Peroxisome proliferators (e.g. clofibric acid) and thyroid hormone play an important role in the metabolism of lipids. These effectors display their action through their own nuclear receptors, peroxisome proliferatoractivated receptor (PPAR) and thyroid hormone receptor (TR). PPAR and TR are ligand-dependent, DNA binding, trans-acting transcriptional factors belonging to the erbA-related nuclear receptor superfamily. The present study focused on the convergence of the effectors on the peroxisome proliferator response element (PPRE). Transcriptional activation induced by PPAR through a PPRE was significantly suppressed by cotransfection of TR in transient transfection assays. The inhibition, however, was not affected by adding 3,5,3-triiodo-L-thyronine (T3). Furthermore, the inhibition was not observed in cells cotransfected with retinoic acid receptor or vitamin D3 receptor. The inhibitory action by TR was lost by introducing a mutation in the DNA binding domain of TR, indicating that competition for DNA binding is involved in the molecular basis of this functional interaction. Gel shift assays revealed that TRs, expressed in insect cells, specifically bound to the 32 P-labeled PPRE as heterodimers with the retinoid X receptor (RXR). Both PPAR and TR bind to PPRE, although only PPAR mediates transcriptional activation via PPRE. TR⅐RXR heterodimers are potential competitors with PPAR•RXR for binding to PPREs. It is concluded that PPAR-mediated gene expression is negatively controlled by TR at the level of PPAR binding to PPRE. We report here the novel action of thyroid hormone receptor in controlling gene expression through PPREs.Peroxisomes are cytoplasmic organelles that are important in mammalian lipid homeostasis (1). The structurally diverse xenobiotic peroxisome proliferators (PPs), 1 such as clofibrate, nafenopin, and WY-14,643 stimulate the proliferation of peroxisomes (2-5) and cause tumorigenic transformation of hepatic cells in rodents (6, 7). Some of these compounds have been used in man as hypolipidemic agents. PPs have been shown to induce peroxisomal and microsomal enzymes involved in lipid metabolism through activation of the peroxisome proliferatoractivated receptor (PPAR) (8, 9). The PPAR is a member of the nuclear receptor superfamily of ligand-dependent transcriptional factors and is structurally related to the subfamily of receptors that includes the thyroid hormone receptor (TR), retinoic acid receptor (RAR), and vitamin D3 receptor (VDR) (10). To date, three subtypes of PPARs have been identified in amphibians, rodents, and humans, PPAR␣,9,[11][12][13][14]. Further investigation revealed that natural fatty acids are also potent activators of PPAR␣ (14, 15), although no direct interaction of PPAR␣ with either PPs or fatty acids has been described so far. Recently, ligands for PPAR␥ have been identified that are potent inducers of adipogenesis in vivo. These include thiazolidine diones, a class of anti-diabetic drugs, and the arachidonic acid derivative 15-deoxy-D12, 14-prostaglandin J2 (16 ...

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“…In rat, northern blot analysis showed that TRa mRNA concentration increased in brain, liver, and brown adipose tissue from 18 days of development onwards to reach its highest level perinatally (Strait et al 1990, Tuca et al 1993. TRb mRNA also increased perinatally in brain, but was reported to reach its peak only in the second postnatal week (Strait et al 1990).…”

Section: Introductionmentioning

confidence: 99%

“…TRb mRNA also increased perinatally in brain, but was reported to reach its peak only in the second postnatal week (Strait et al 1990). In contrast, TRb mRNA decreased perinatally in liver and brown adipose tissue (Strait et al 1990, Tuca et al 1993. In the developing nervous system of the rat, the highest cellular concentration of TRa mRNAs was found in the areas of neuronal differentiation such as the fetal neocortical plate, whereas TRb mRNAs were largely restricted to the zones with neuroblast proliferation, such as the germinal trigone and the cortical ventricular layer (Bradley et al 1992).…”

Section: Introductionmentioning

confidence: 99%

“…Since our in situ probes did not differentiate between the respective splice variants, quantitative PCR techniques were used to determine the tissue levels of TRa 1 , TRa 2 , TRb 1 , and TRb 2 mRNA. Since tissue TR mRNA level and nuclear thyroid hormone-binding capacity (i.e., functional TR protein) do not always correlate (Strait et al 1990, Tuca et al 1993, we also investigated tissue TR protein level by western blot analysis and immunohistochemistry, using our recently described antisera (Zandieh Doulabi et al 2002, 2003. We report a highly specific, but heterogeneous spatial and temporal expression pattern of the TRa and TRb mRNAs, and report evidence for extensive posttranscriptional regulation in the perinatal period.…”

Section: Introductionmentioning

confidence: 99%

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Expression of thyroid hormone receptors A and B in developing rat tissues; evidence for extensive posttranscriptional regulation

Keijzer

Blommaart²,

Labruyère³

et al. 2007

Journal of Molecular Endocrinology

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The perinatal changes in the pattern of expression of the thyroid hormone receptor (TR) isoforms TRa 1 TRa 2 , TRb 1 , and TRb 2 were investigated using in situ hybridization and immunohistochemistry, and RT-PCR and western blotting as visualization and quantification techniques respectively. In liver, lung, and kidney, TRa mRNA was expressed in the stromal and TRb mRNA in the parenchymal component of the tissues. When compared with liver, TRa mRNA concentrations were tenfold higher in lung, kidney, and intestine, and 100-fold higher in brain, with TRa 2 mRNA concentrations exceeding those of TRa 1 5-to 10-fold. Tissue TRb 1 mRNA concentrations were similar in liver, lung, and brain, and 3-to 5-fold higher in kidney and intestine. None of the TRb 2 mRNA could be detected outside the pituitary. Tissue TRa 2 and TRb 1 protein levels reached adult levels at 5 days before birth, whereas TRa 1 protein peaked after birth. Because of the distinct time-course of thyroid hormonebinding receptors TRa 1 and TRb 1 , we speculate that an initiating, TRb 1 -mediated signaling from the parenchyma is followed by a TRa 1 -mediated response in the stroma. When compared with organs with a complementary parenchymal-stromal expression pattern, organs with extensive cellular co-expression of TRa and TRb (brain and intestinal epithelium) were characterized by a very low TRa protein: mRNA ratio, implying a low translational efficiency of TR mRNA or a high turnover of TR protein. The data indicate that the TR-dependent regulatory cascades are controlled differently in organs with a complementary tissue expression pattern and in those with cellular co-expression of the TRa and TRb genes.

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Ontogeny of thyroid hormone receptors and c-erbA expression during brown adipose tissue development: evidence of fetal acquisition of the mature thyroid status

Cited by 11 publications

References 0 publications

Mapping, expression and regulation of the TRα gene in porcine adipose tissue

Mapping, expression and regulation of the TRα gene in porcine adipose tissue

Inhibition of Peroxisome Proliferator Signaling Pathways by Thyroid Hormone Receptor

Expression of thyroid hormone receptors A and B in developing rat tissues; evidence for extensive posttranscriptional regulation

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