DNA Binding Activity of the Aryl Hydrocarbon Receptor Is Sensitive to Redox Changes in Intact Cells

Xu, Chuanli; Siu, Chu-Sin; Pasco, David S.

doi:10.1006/abbi.1998.0851

Cited by 15 publications

(7 citation statements)

References 50 publications

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“…Elevation of Se up to 1.70 mg Se/kg in the present study also markedly up-regulated hepatic expression of gr. Transcription factors can be affected by the redox status of the cell; thus, oxidative stress may alter their activity, and such is the case of gr (Di Giulio & Meyer, 2008;Esposito et al, 1998;Olsvik et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…In vitro studies have demonstrated a reduction of gr DNA binding in conditions of high oxidative stress (Esposito et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Expression of catalase (cat) can be used to evaluate oxidative status, and high doses of Se have been observed to increase its activity in several fish species (Ashouri et al, 2015;Elia, Prearo, Pacini, Dörr, & Abete, 2011;Mansour et al, 2017;Misra, Hamilton, & Niyogi, 2012;Penglase, Hamre, Rasinger, & Ellingsen, 2014). Oxidative stress may also alter transcription factors, such as glucocorticoid receptors (gr; Di Giulio & Meyer, 2008;Esposito, Cuccovillo, Morra, Russo, & Cimino, 1998;Olsvik, Torstensen, Hemre, Sanden, & Waagbø, 2011), which are zinc-finger-containing proteins, and as such are susceptible to inhibition by reducible Se compounds (with oxidation state of −I or higher) in which sodium selenite is included (oxidation state +IV; Blessing, Kraus, Heindl, Bal, & Hartwig, 2004). Furthermore, selenite catalyses the oxidation of SH groups, such as those present in the glucocorticoid receptor hormone binding sites (Tashima et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Optimum selenium levels in diets high in plant‐based feedstuffs for gilthead sea bream (Sparus aurata) fingerlings

et al. 2019

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Substitution of marine ingredients (FM‐FO) by plant protein and oil sources can modify selenium (Se) levels in feeds. Se plays an important role in the antioxidative defence by forming part of selenoproteins. Se requirements of gilthead sea bream are not accurately determined; therefore, this study was conducted to define Se supplementation levels in low FM‐FO practical diets for sea bream fingerlings. A plant‐based diet containing 0.45 mg Se/kg diet was used as the basal diet. Four other diets were supplemented to contain 0.68, 0.86, 1.00 or 1.70 mg Se/kg diet, supplied as sodium selenite. Sea bream, weighing 12.6 ± 1.4 g, were distributed in triplicate groups per diet and fed for 42 days. Se supplementation up to 1.00 mg Se/kg significantly improved the growth of sea bream, whereas further increase up to 1.70 mg Se/kg diet reduced growth. The results of this study suggest that the optimum dietary levels of sodium selenite in diets with low FM‐FO with basal levels of 0.45 mg Se/kg are around 0.94 mg Se/kg to promote growth of gilthead sea bream juveniles. On the contrary, dietary levels of 1.70 mg Se/kg were found to be excessive and caused growth reduction, increased catalase expression and hydropic degeneration in the liver.

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Section: Discussionmentioning

confidence: 99%

“…In vitro studies have demonstrated a reduction of gr DNA binding in conditions of high oxidative stress (Esposito et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Optimum selenium levels in diets high in plant‐based feedstuffs for gilthead sea bream (Sparus aurata) fingerlings

et al. 2019

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“…P1A1-LUC is similar to P1A1-4X1-LUC except it lacks the four copies of XRE1. Both expression vectors have been described previously (Xu et al, 1998; a gift from Dr. D. Pasco, University of Mississippi, Oxford, MS). PCMV␤gal was purchased from Pharmacia Biotech (Piscataway, NJ).…”

Section: Expression Vectorsmentioning

confidence: 99%

Recruitment of Dioxin Receptor to Active Transcription Sites

Elbi

Misteli

Hager

2002

MBoC

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The aryl hydrocarbon receptor (AhR or dioxin receptor) is a ligand-activated transcription factor that heterodimerizes with the AhR nuclear translocator (ARNT/HIF-1beta) to form an AhR/ARNT transcription factor complex. This complex binds to specific DNA sites in the regulatory domains of numerous target genes and mediates the biological effects of exogenous ligands. Herein, we have investigated the subcellular distribution of the AhR/ARNT complex in response to ligand stimulation, by using live-cell confocal and high-resolution deconvolution microscopy. We found that unliganded AhR shows a predominantly cytoplasmic diffuse distribution in mouse hepatoma cells. On addition of ligand, AhR rapidly translocates to the nucleus and accumulates in multiple bright foci. Inhibition of transcription prevented the formation of AhR foci. Dual- and triple-immunolabeling experiments, combined with labeling of nascent RNA, showed that the foci are transcription sites, indicating that upon ligand stimulation, AhR is recruited to active transcription sites. The interaction of AhR with ARNT was both necessary and sufficient for the recruitment of AhR to transcription sites. These results indicate that AhR/ARNT complexes are recruited to specific subnuclear compartments in a ligand-dependent manner and that these foci represent the sites of AhR target genes.

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“…The precise step in the AHR signaling pathway that is acted on by oxidative stress is not clear. Sulfhydryl-modifying agents have been shown to block binding of TCDD to the AHR [6±8] and AHR DNA binding [9,10], suggesting that AHR activation may be directly redox regulated. In addition, H 2 O 2 has been shown to inhibit Cyp1a1 inducibility [11] and disrupt reporter gene expression driven by AHR-responsive promoter sequences [12].…”

Section: Introductionmentioning

confidence: 99%

Disruption of dioxin-inducible phase I and phase II gene expression patterns by cadmium, chromium, and arsenic

2000

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Recent work suggesting that cellular oxidative stress exerts an inhibitory effect on aromatic hydrocarbon receptor (AHR)–dependent gene expression led us to test the hypothesis that pro‐oxidant environmental pollutants might alter the induction of detoxification genes by 2,3,7,8‐tetrachlorodibenzo‐p‐dioxin (TCDD), an AHR ligand. We found that, in mouse hepatoma Hepa‐1 cells, TCDD‐inducible cytochrome P450, Cyp1a1, and nicotinamide adenine dinucleotide phosphate–quinone oxidoreductase (Nqo1) mRNA accumulation were differentially affected by cadmium (Cd2+), chromium (Cr6+), and arsenic (As3+). Cadmium or arsenic did not change Cyp1a1 mRNA levels but did enhance TCDD‐inducible levels of Nqo1 mRNA, an effect that paralleled the ability of these metals to activate a β‐galactosidase gene reporter system regulated by an electrophile response promoter element. Chromium inhibited mRNA accumulation for both Cyp1a1 and Nqo1. Manipulation of cellular thiol status did not modify the response to combined chromium‐TCDD exposure, suggesting that the response was not caused by oxidative stress. Chromium did not block DNA‐binding competence of the AHR and did not have an effect on mRNA stability, but it inhibited Cyp1a1 gene transcription and the expression of an AHR‐dependent luciferase reporter. These data indicate that coexposure to pro‐oxidant metals and AHR ligands, which is common in the environment, can disrupt the regulation of phase I and phase II detoxification genes, leading to imbalances in gene expression that may have important consequences for the toxicity of complex mixtures. Mol. Carcinog. 28:225–235, 2000. © 2000 Wiley‐Liss, Inc.

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DNA Binding Activity of the Aryl Hydrocarbon Receptor Is Sensitive to Redox Changes in Intact Cells

Cited by 15 publications

References 50 publications

Optimum selenium levels in diets high in plant‐based feedstuffs for gilthead sea bream (Sparus aurata) fingerlings

Optimum selenium levels in diets high in plant‐based feedstuffs for gilthead sea bream (Sparus aurata) fingerlings

Recruitment of Dioxin Receptor to Active Transcription Sites

Disruption of dioxin-inducible phase I and phase II gene expression patterns by cadmium, chromium, and arsenic

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