Epigallocatechin-3-gallate enhances key enzymatic activities of hepatic thioredoxin and glutathione systems in selenium-optimal mice but activates hepatic Nrf2 responses in selenium-deficient mice
| العنوان: | Epigallocatechin-3-gallate enhances key enzymatic activities of hepatic thioredoxin and glutathione systems in selenium-optimal mice but activates hepatic Nrf2 responses in selenium-deficient mice |
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| المؤلفون: | Ruixia Dong, Pingping Chen, Chung S. Yang, Xiaoxiao Wang, Ke Zhang, Jinsong Zhang, Dongxu Wang |
| المصدر: | Redox Biology, Vol 10, Iss C, Pp 221-232 (2016) Redox Biology |
| بيانات النشر: | Elsevier, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Antioxidant, medicine.medical_treatment, Thioredoxin reductase, NQO1, NAD(P)H:quinone oxidoreductase 1, Clinical Biochemistry, Glutathione reductase, GAPDH, glyceraldehyde 3-phosphate dehydrogenase, RIPA, tissue fluid of fast pyrolysis, AST, aspartate aminotransferase, Nrf2 response, Biochemistry, Nrf2, nuclear factor erythroid 2-related factor 2, Antioxidants, Catechin, GST, glutathione S-transferase, RT-PCR, reverse transcriptase polymerase chain reaction, chemistry.chemical_compound, Mice, EDTA, ethylene diamine tetraacetic acid, Thioredoxins, Glutaredoxin, GSH, glutathione, GR, glutathione reductase, Trx, thioredoxin, heterocyclic compounds, IL-6, interleukin-6, lcsh:QH301-705.5, HO1, heme oxygenase 1, EGCG, epigallocatechin-3-gallate, lcsh:R5-920, GPx, glutathione peroxidase, Epigallocatechin-3-gallate, GSSG, oxidized glutathione, food and beverages, BSO, buthionine sulfoximine, IL-10, interleukin-10, FoxO, Forkhead box class O, Thioredoxin system, Glutathione, CDNB, 1-chloro-2, 4-dinitrobenzene, Glutathione Reductase, Grx, glutaredoxin, H2O2, hydrogen peroxide, PBS, phosphate buffer solution, qPCR, quantitative polymerase chain reaction, RT, room temperature, Thioredoxin, ECL, enhanced chemiluminescense, lcsh:Medicine (General), Signal Transduction, Research Paper, inorganic chemicals, TrxR, thioredoxin reductase, Glutathione system, Thioredoxin-Disulfide Reductase, PVDF, polyvinylidene fluoride, SDS, sodium dodecyl sulfate, NF-E2-Related Factor 2, Rps6, ribosomal protein S6, UPLC, ultra-high performance liquid chromatography, Biology, complex mixtures, RNS, reactive nitrogen species, Se, selenium, 03 medical and health sciences, Selenium, ROS, reactive oxygen species, Sp1/Sp3, specificity protein 1/3, Thioredoxin Reductase 1, IL-2, interleukin-2, ALT, alanine aminotransferase, 4-HNE, 4-hydroxynonenal, SOD, superoxide dismutase, medicine, Animals, Glutaredoxins, Organic Chemistry, γ-H2AX, phosphorylated histone 2AX, NADHP, nicotinamide-adenine dinucleotide phosphate, SelP, selenoprotein P, 030104 developmental biology, chemistry, Gene Expression Regulation, lcsh:Biology (General), Sec, selenocysteine, Keap1, kelch-like ECH-associated protein 1, Prx, peroxiredoxin, NAD+ kinase, QQQ-MS/MS, triple quadrupole mass spectrometer, sense organs, Reactive Oxygen Species, TBS-T, tris-buffered saline with 0.05% Tween 20 |
| الوصف: | Selenium participates in the antioxidant defense mainly through a class of selenoproteins, including thioredoxin reductase. Epigallocatechin-3-gallate (EGCG) is the most abundant and biologically active catechin in green tea. Depending upon the dose and biological systems, EGCG may function either as an antioxidant or as an inducer of antioxidant defense via its pro-oxidant action or other unidentified mechanisms. By manipulating the selenium status, the present study investigated the interactions of EGCG with antioxidant defense systems including the thioredoxin system comprising of thioredoxin and thioredoxin reductase, the glutathione system comprising of glutathione and glutathione reductase coupled with glutaredoxin, and the Nrf2 system. In selenium-optimal mice, EGCG increased hepatic activities of thioredoxin reductase, glutathione reductase and glutaredoxin. These effects of EGCG appeared to be not due to overt pro-oxidant action because melatonin, a powerful antioxidant, did not influence the increase. However, in selenium-deficient mice, with low basal levels of thioredoxin reductase 1, the same dose of EGCG did not elevate the above-mentioned enzymes; intriguingly EGCG in turn activated hepatic Nrf2 response, leading to increased heme oxygenase 1 and NAD(P)H:quinone oxidoreductase 1 protein levels and thioredoxin activity. Overall, the present work reveals that EGCG is a robust inducer of the Nrf2 system only in selenium-deficient conditions. Under normal physiological conditions, in selenium-optimal mice, thioredoxin and glutathione systems serve as the first line defense systems against the stress induced by high doses of EGCG, sparing the activation of the Nrf2 system. Highlights • EGCG increases hepatic activities of TrxR, GR and Grx in selenium-optimal mice. • EGCG fails to manipulate the above-mentioned enzymes in selenium-deficient mice. • EGCG in turn activates hepatic Nrf2 response in selenium-deficient mice. • Selenium deficiency does not increase EGCG toxicity due to potent Nrf2 response. Graphical abstract fx1 |
| اللغة: | English |
| تدمد: | 2213-2317 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb7266d574e203ea4c2eff947b654886 http://www.sciencedirect.com/science/article/pii/S2213231716302129 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bb7266d574e203ea4c2eff947b654886 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 22132317 |
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