The Ca2+- and reduced nicotinamide adenine dinucleotide phosphate-dependent hydrogen peroxide generating system is induced by thyrotropin in porcine thyroid cells.

Carvalho, Denise P.; Dupuy, Corinne; Gorin, Yves; Legué, Odette; Pommier, Jacques; Haye, Bernard; Virion, Alain

doi:10.1210/endo.137.3.8603567

Cited by 42 publications

(19 citation statements)

References 33 publications

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“…We also demonstrated that human DuOx2 promoter activity is induced by TSH and forskolin in PCCL3. In fact, TSH, through the cAMP cascade, regulates H 2 O 2 production, which is essential for thyroid hormone biosynthesis [5], in accordance with our data. A previous study using forskolin 10 -5 M suggested that human DuOx promoter is not positively controlled by cAMP in thyroid cells [3].…”

Section: Discussionsupporting

confidence: 89%

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DuOx2 Promoter Regulation by Hormones, Transcriptional Factors and the Coactivator TAZ

Cardoso-Weide

Cardoso-Penha²,

Costa

et al. 2015

Eur Thyroid J

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The production of H₂O₂, which is essential to thyroid hormone synthesis, involves two NADPH oxidases: dual oxidases 1 and 2 (DuOx1 and DuOx2). A functional study with human DuOx genes and their 5′-flanking regions showed that DuOx1 and -2 promoters are different from thyroid-specific gene promoters. Furthermore, their transcriptional activities are not restricted to thyroid cells. While regulation of Tg (thyroglobulin) and TPO (thyroperoxidase) expression have been extensively studied, DuOx2 promoter regulation by hormones and transcriptional factors need to be more explored. Herein we investigated the role of TSH, insulin and insulin-like growth factor 1 (IGF-1), as well as the cAMP effect on DuOx2 promoter (ptx41) activity in transfected rat thyroid cell lines (PCCL3). We also assessed DuOx2 promoter activity in the presence of transcriptional factors crucial to thyroid development such as TTF-1 (thyroid transcription factor 1), PAX8, CREB, DREAM, Nkx2.5 and the coactivator TAZ in HeLa and HEK 293T-transfected cells. Our results show that TSH and forskolin, which increase cAMP in thyroid cells, stimulated DuOx2 promoter activity. IGF-1 led to pronounced stimulation, while insulin induction was not statistically different from DuOx2 promoter basal activity. All transcriptional factors selected for this work and coactivator TAZ, except DREAM, stimulated DuOx2 promoter activity. Moreover, Nkx2.5 and TAZ synergistically increased DuOx2 promoter activity. In conclusion, we show that DuOx2 expression is regulated by hormones and transcription factors involved in thyroid organogenesis and carcinogenesis, reinforcing the importance of the control of H₂O₂ generation in the thyroid.

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Section: Discussionsupporting

confidence: 89%

“…In human thyroid, DuOx2 mRNA is 1.5-5 times more abundant than DuOx1 [3]. Biochemical studies have revealed that DuOx activity is stimulated by calcium [4] and TSH through the cAMP cascade [5]. On the other hand, thyroid H 2 O 2 generation is inhibited by iodide in vivo, the Wolff-Chaikoff effect [6,7] and in cell culture [8].…”

Section: Introductionmentioning

confidence: 99%

DuOx2 Promoter Regulation by Hormones, Transcriptional Factors and the Coactivator TAZ

Cardoso-Weide

Cardoso-Penha²,

Costa

et al. 2015

Eur Thyroid J

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“…6). The migration of methyl and benzyl groups from selenium to nitrogen atom was readily occurred when the samples were heated to 40-50 • C. The isomerization was followed by 1 H, 13 C and 77 Se NMR spectroscopy and the thermodynamically stable final products were characterized by single crystal X-ray studies. Compounds 12 and 13 were also synthesized by independent methods and compared with the isomerized products.…”

Section: Inhibition Of Lpo-catalyzed Oxidation Of Abts By Anti-thyroimentioning

confidence: 99%

Selenium Analogues of Anti-Thyroid Drugs

Roy

Mugesh

2008

Phosphorus, Sulfur, and Silicon and the Related Elements

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The inhibition of lactoperoxidase (LPO)-catalyzed oxidation of ABTS by antithyroid drugs and related derivatives is described. The commonly used anti-thyroid agent methimazole (MMI) inhibits the LPO with an IC 50 value of 7.0 ± 1.1 µM which is much lower than that of the other two anti-thyroid drugs, PTU and MTU. The selenium analogue of methimazole (MSeI) also inhibits LPO with an IC 50 value of 16.4 ± 1.5 µM, which is about 4-5 times lower than that of PTU and MTU. In contrast to thiones and selones, the S-and Se-protected compounds do not show any noticeable inhibition under identical experimental conditions. While the inhibition of LPO by MMI cannot be reversed by increasing the hydrogen peroxide concentration, the inhibition by MSeI can be completely reversed by increasing the peroxide concentration. Experimental and theoretical studies were performed on a number of selones, which suggest that these compounds exist as selenolates or zwitterions in which the selenium atom carries a large negative charge. The structures of selones were studied in solution by NMR spectroscopy and the 77 Se NMR chemical shifts for the selones show large upfield shifts in the signals, confirming the zwitterionic structure of the selones in solution. The thermal isomerization of some S-and Se-substituted methyl and benzyl imidazole derivatives to produce the thermodynamically more stable N-substituted derivatives is described.

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“…TSH (6)(7)(8). However, evidence against a TSH regulation for the latter enzyme has been reported recently (9). Prev.ous reports suggested a role of MAO and NADPH-cy-MATERIALS AND METHODS tochrome c reductase in H2O2 generation (1), although this hypothesis was not further supported (8)(9)(10)(11).…”

mentioning

confidence: 96%

“…However, evidence against a TSH regulation for the latter enzyme has been reported recently (9). Prev.ous reports suggested a role of MAO and NADPH-cy-MATERIALS AND METHODS tochrome c reductase in H2O2 generation (1), although this hypothesis was not further supported (8)(9)(10)(11). T-The ontogenesis of thyroid function has been studied in several species, and sequential developmental steps in the Fetal and adult bovine thyroid glands were obtained at biochemical maturation have been described (12)(13)(14)(15)(16).…”

mentioning

confidence: 99%

Biochemical and Functional Changes During the Bovine Fetal Thyroid Development

Masini-Repiso

Orgnero-Gaisán²,

Bonaterra³

et al. 1998

Thyroid

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To establish biochemical and functional relations during thyroid development, the activity of thyroid peroxidase (TPO), nicotinamide adenine dinucleotide phosphate (NADPH)-cytochrome c reductase and monoamine oxidase (MAO) in a particulate fraction and the iodide transport and organification in slices of bovine fetal thyroid were examined throughout gestation. The cytochemical localization of TPO, H2O2 generating sites and MAO was also studied. Fetal glands were grouped in stages I to V according to increasing developmental features; adult tissues were also analyzed. TPO activity in each of the fetal stages was higher than in the adult; a marked increase was observed in stages IV and V. Iodide transport (T/M) was similar in stages I to V and the adult. Iodide organification in fetal thyroids showed a similar pattern to that of TPO activity. When compared with the adult, at midgestation (stages II to III), a lower iodination coexisted with a higher TPO activity. The activity of NADPH-cytochrome c reductase and MAO, two enzymes previously proposed to participate in thyroid H2O2 generation, did not parallel the level of iodide organification. Cells from stages II to V exhibited a positive cytochemical reaction for TPO in the rough endoplasmic reticulum (RER) and the perinuclear cisternae (PC). In stages IV, V, and adult, TPO was occasionally found in apical vesicles and microvilli, whereas H2O2 was detected within the RER and the PC. MAO reaction was positive in adult, but not in fetal thyroid. These results indicate that a high TPO activity accompanied the onset of the organification process during fetal thyroid development. The level of iodination was associated with the presence of TPO at a proper site rather than to the level of TPO activity. Evidence against a role of NADPH-cytochrome c reductase and MAO in the iodide organification was obtained.

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The Ca2+- and reduced nicotinamide adenine dinucleotide phosphate-dependent hydrogen peroxide generating system is induced by thyrotropin in porcine thyroid cells.

Cited by 42 publications

References 33 publications

DuOx2 Promoter Regulation by Hormones, Transcriptional Factors and the Coactivator TAZ

DuOx2 Promoter Regulation by Hormones, Transcriptional Factors and the Coactivator TAZ

Selenium Analogues of Anti-Thyroid Drugs

Biochemical and Functional Changes During the Bovine Fetal Thyroid Development

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