Trans-activation by thyroid hormone receptors: functional parallels with steroid hormone receptors.

Thompson, Catherine C.; Evans, Ronald M.

doi:10.1073/pnas.86.10.3494

Cited by 143 publications

(40 citation statements)

References 39 publications

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“…1, the three TRs are least similar at their amino termini. Although this region does not appear to be required for transcriptional activation of a TREpal-containing reporter gene by TR#31 (77), this situation may be analogous to the A and B forms of the progesterone receptor, which differ only in their amino termini yet differentially activate target genes (78). The amino terminal "T-l" domain of the glucocorticoid receptor (79) also modulates transcriptional activation.…”

Section: Discussionmentioning

confidence: 99%

Nuclear thyroid hormone receptors.

Lazar¹,

Chin²

1990

J. Clin. Invest.

173

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Thyroid hormones (L-T3 and L-T4) are important for nearly all human tissues. They have profound effects on metabolic rate and oxygen consumption, but also have unique functions in a variety of organs, including the heart, liver, and pituitary gland, which reflect the specialized nature of these systems.Many of the effects of thyroid hormone occur at the level of gene expression, and are mediated by nuclear thyroid hormone receptors (TR)' (1). Evidence for the existence and importance of nuclear TRs with high affinity and specificity for T3 has been recently reviewed by Oppenheimer et al. (2) and, in this journal, by Samuels et al. (3). The purpose of this Perspective is to provide an up-to-date summary of new knowledge that has directly resulted from the cloning of multiple TRs and related molecules.

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Section: Discussionmentioning

confidence: 99%

Nuclear thyroid hormone receptors.

Lazar¹,

Chin²

1990

J. Clin. Invest.

173

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“…Dilutions were made in RPMI 1640 medium. Thompson et al showed that the transcriptional activities of thyroid hormone receptors α and β are dose dependent from 1 to 100 nM T3 [20], while the threshold T3 concentration for non-genomic effects ranges from 0.1 to 30 nM [21]. Therefore, 0.1 to 100 nM T3 was used for pre-incubation in most experiments in the study.…”

Section: Cell Culturementioning

confidence: 99%

A high concentration of triiodothyronine attenuates the stimulatory effect on hemin-induced erythroid differentiation of human erythroleukemia K562 cells

et al. 2015

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Thyroid hormone stimulates erythropoiesis and clinical hypothyroidism is often complicated by reductions in red cell mass and total blood volume, and by normocytic normochromic anemia [1][2][3][4]. Clinically, bone marrow has been observed to show erythroid hyperplasia in patients with hyperthyroidism [5]. However, anemia is sometimes observed in patients with hyperthyroidism such as Graves' disease (GD). Some reports indicate that anemia associated with hyperthyroidism occurs in 10-22% of cases of non-treated hyperthyroidism, and that these cases recover well with treatment of A high concentration of triiodothyronine attenuates the stimulatory effect on hemin-induced erythroid differentiation of human erythroleukemia K562 cells Abstract. Although thyroid hormone is a known stimulator of erythropoietic differentiation, severe anemia is sometimes observed in patients with hyperthyroidism and this mechanism is not fully understood. The aim of this study was to investigate the effect of triiodothyronine (T3) on hemin-induced erythropoiesis. Human erythroleukemia K562 cells were used as an erythroid differentiation model. Cell differentiation was induced by hemin and the effect of pre-incubation with T3 (0.1 to 100 nM) was analyzed by measuring the benzidine-positive rate, hemoglobin content, CD71 expression (transferrin receptor), and mRNA expression for transcription factors related to erythropoiesis and thyroid hormone receptors (TRs). Hemin, a promoter of erythroid differentiation, increased the levels of mRNAs for TRα, TRβ, and retinoid X receptor α (RXRα), as well as those for nuclear factor-erythroid 2 (NFE2), GATA-binding protein 1 (GATA1) and GATA-binding protein 2 (GATA2). Lower concentrations of T3 had a stimulatory effect on hemin-induced hemoglobin production (1 and 10 nM), CD71 expression (0.1 nM), and α-globin mRNA expression (1 nM), while a higher concentration of T3 (100 nM) abrogated the stimulatory effect on these parameters. T3 at 100 nM did not affect cell viability and proliferation, suggesting that the abrogation of erythropoiesis enhancement was not due to toxicity. T3 at 100 nM also significantly inhibited expression of GATA2 and RXRα mRNA, compared to 1 nM T3. We conclude that a high concentration of T3 attenuates the classical stimulatory effect on erythropoiesis exerted by a low concentration of T3 in hemin-induced K562 cells.

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“…Lastly, hT3R␤1, which does not contain a cluster of basic amino acids in the A/B region corresponding to amino acids 21 to 30 of cT3R␣, binds TFIIB less efficiently than cT3R␣ (35). This may explain the finding that hT3R␤1 activates transcription less efficiently than hT3R␣1 (71), which has the same basic sequence in the A/B region as cT3R␣.…”

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confidence: 98%

“…Thus, three T3Rs which primarily differ in the A/B domain are expressed, suggesting that this region may play a role in mediating different effects of these receptors. For example, hT3R␣1 has been suggested to be more active in transfection experiments than hT3R␤1 (71).…”

mentioning

confidence: 99%

A 10-Amino-Acid Sequence in the N-Terminal A/B Domain of Thyroid Hormone Receptor α Is Essential for Transcriptional Activation and Interaction with the General Transcription Factor TFIIB

Hadzic

Desai-Yajnik

Helmer

et al. 1995

Molecular and Cellular Biology

109

111

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Transcription of eukaryotic protein-encoding genes by RNA polymerase II is modulated by two distinct classes of transcription factors. The first class comprises general transcription factors which are necessary for accurate initiation of transcription. These factors include TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIG/J, and TFIIH (11, 82). TFIID is a multiprotein complex consisting of TATA-binding protein (TBP) complexed with a number of TBP-associated factors (73). The binding of TFIID is thought to be the first step in transcriptional initiation (11, 82). The subsequent binding of TFIIB is thought to be involved in bringing RNA polymerase II to the complex through the association of TFIIF (34, 37). This leads to the recruitment of TFIIE and TFIIH and possibly other factors, which ultimately results in the initiation of transcription (11,75,82).The magnitude of transcriptional activity is greatly affected by the second class of transcription factors that generally bind to distal control DNA elements (52). These sequence-specific factors act to either promote or inhibit the formation of an active transcriptional initiation complex. Recent in vitro transcription studies suggest that the entry of TFIIB may be rate limiting for transcriptional initiation and that several transcriptional activators act to recruit or stabilize the interaction of TFIIB with the initiation complex (14, 62). TFIIB contains a potential N-terminal zinc finger structure (amino acids 14 to 36) that may be important for interaction with RNA polymerase II and TFIIF (34), a more C-terminal amphipathic ␣ helix (amino acids 184 to 201), and two imperfect repeats (amino acids 124 to 201 and 218 to 294) (34,37,62) (Fig. 1A). The amphipathic ␣ helix appears to be important for interaction with TBP (34, 37) and several transcriptional activators such as the herpes simplex virus VP16 protein (62).Members of the steroid/thyroid hormone receptor gene family are sequence-specific DNA-binding proteins that play important roles in gene regulation. The steroid hormone receptor subfamily includes the receptors which mediate the effects of glucocorticoids, progestins, mineralocorticoids, androgens, and estrogens (12, 16). The thyroid/retinoid receptor subfamily (16, 21) includes receptors that mediate the effects of thyroid hormone (3,5,3Ј-triiodo-L-thyronine [T3]), all-trans retinoic acid, 9-cis retinoic acid, and 1,25-dihydroxyvitamin D 3 as well as several orphan receptors (e.g., COUP-TF and c-ErbA␣2) whose ligands, if any, are unknown (26,27,44). Steroid/thyroid receptors bind to specific DNA sequences known as hormone response elements (HREs) and mediate ligand-dependent ac-

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Trans-activation by thyroid hormone receptors: functional parallels with steroid hormone receptors.

Abstract: The effects of thyroid hormones are mediated through nuclear receptor proteins that modulate the transcription of specific genes in target cells. We previously isolated cDNAs encoding two different mammalian thyroid hormone receptors, one from human placenta (hTRI3) and the other

Cited by 143 publications

References 39 publications

Nuclear thyroid hormone receptors.

Nuclear thyroid hormone receptors.

A high concentration of triiodothyronine attenuates the stimulatory effect on hemin-induced erythroid differentiation of human erythroleukemia K562 cells

A 10-Amino-Acid Sequence in the N-Terminal A/B Domain of Thyroid Hormone Receptor α Is Essential for Transcriptional Activation and Interaction with the General Transcription Factor TFIIB

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