Search results for "Thioredoxin Reductase 1"

showing 4 items of 4 documents

Yeast thioredoxin reductase Trr1p controls TORC1-regulated processes

2018

The thioredoxin system plays a predominant role in the control of cellular redox status. Thioredoxin reductase fuels the system with reducing power in the form of NADPH. The TORC1 complex promotes growth and protein synthesis when nutrients, particularly amino acids, are abundant. It also represses catabolic processes, like autophagy, which are activated during starvation. We analyzed the impact of yeast cytosolic thioredoxin reductase TRR1 deletion under different environmental conditions. It shortens chronological life span and reduces growth in grape juice fermentation. TRR1 deletion has a global impact on metabolism during fermentation. As expected, it reduces oxidative stress tolerance…

0301 basic medicineThioredoxin Reductase 1Estrès oxidatiuThioredoxin reductaseScienceMicrobiologiaMechanistic Target of Rapamycin Complex 1Grape Juice FermentationArticleAntioxidants03 medical and health scienceschemistry.chemical_compoundTORC1 PathwayYeastsAmino AcidsMultidisciplinary030102 biochemistry & molecular biologyKinaseAutophagyChronological Life SpanQFungal geneticsRGlutathioneMetabolismTORC1 ComplexThioredoxin SystemYeastCell biology030104 developmental biologychemistryMedicineThioredoxinGene DeletionSignal TransductionScientific Reports
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Characterization of Hydrophilic Gold(I) N-Heterocyclic Carbene (NHC) Complexes as Potent TrxR Inhibitors Using Biochemical and Mass Spectrometric App…

2017

We report here on the synthesis of a series of mono-and dinuclear gold(I) complexes exhibiting sulfonated bis(NHC) ligands and novel hydroxylated mono(NHC) Au(I) compounds, which were also examined for their 'biological activities. Initial cell viability assays show strong antiproliferative activities of the hydroxylated mono(NHC) gold compounds (8 > 9 > 10) against 2008 human ovarian cancer cells even after 1 h incubation. In order to gain insight into the mechanism of biological action of the gold compounds, their effect on the pivotal cellular target seleno-enzyme thioredoxin reductase (TrxR), involved in the maintenance of intracellular redox balance, was investigated in depth. Th…

Thioredoxin Reductase 1AuranofinSilverStereochemistryThioredoxin reductaseThioredoxin Reductase 2WATER-SOLUBLE RUTHENIUM(II)Antineoplastic Agents010402 general chemistryG-quadruplexLigandsIN-VITRO CYTOTOXICITYLIGANDS SYNTHESIS01 natural sciencesInorganic Chemistrychemistry.chemical_compoundDrug StabilityThioredoxin Reductase 1Coordination ComplexesTHIOREDOXIN REDUCTASE INHIBITIONCell Line TumormedicineOrganogold CompoundsAnimalsHumansCRYSTAL-STRUCTURESPhysical and Theoretical ChemistryCANCER CELLSBIOLOGICAL-PROPERTIES010405 organic chemistryChemistryMOLECULAR-MECHANISMSDNA0104 chemical sciencesRatsG-QuadruplexesGlutathione ReductaseSolubilityBiological targetCancer cellPLATINUM ANTICANCER DRUGSMETAL-COMPLEXESGoldReactive Oxygen SpeciesCarbeneHydrophobic and Hydrophilic InteractionsOrganogold Compoundsmedicine.drugInorganic Chemistry
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Thioredoxin-related protein of 14 kDa may directly reduce protein cysteinylation motifs

2018

Disulfide stress has been associated with inflammation and characterized by an increase in cystine levels and protein cysteinylation. Furthermore, it was recently discovered that thioredoxin-related protein of 14 kDa (TRP14, encoded by TXNDC17) exhibits efficient cystine reductase activity. The aim of our research was to elucidate if TRP14 is also able to reduce cysteinylated proteins in mammalian cells. Thus, protein cysteinylation was assessed in control and TRP14 knockdown cells in vitro through their pre-treatment with 25 µg/ml cycloheximide for 30 min and incubation with 250 µM biotinylated cysteine for 1 h. Moreover, such TRP14 knockdown cell lysates were tested as cysteinylated subst…

chemistry.chemical_classificationChemistryCystineCystine reductase activityCycloheximideBiochemistrychemistry.chemical_compoundEnzymeBiochemistryThioredoxin Reductase 1Physiology (medical)BiotinylationThioredoxinCysteineFree Radical Biology and Medicine
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Prolonging in utero-like oxygenation after birth diminishes oxidative stress in the lung and brain of mice pups☆

2013

Background Fetal-to-neonatal transition is associated with oxidative stress. In preterm infants, immaturity of the antioxidant system favours supplemental oxygen-derived morbidity and mortality. Objectives To assess if prolonging in utero-like oxygenation during the fetal-to-neonatal transition limits oxidative stress in the lung and brain, improving postnatal adaptation of mice pups. Material and methods Inspiratory oxygen fraction (FiO2) in pregnant mice was reduced from 21% (room air) to 14% (hypoxia) 8–12 h prior to delivery and reset to 21% 6–8 h after birth. The control group was kept at 21% during the procedure. Reduced (GSH) and oxidized (GSSG) glutathione and its precursors [γ-glut…

gsr (glutathione reductase gene)pgd phosphogluconate dehydrogenase geneGPX1FiO2 inspiratory oxygen fractionγ-GC (gamma-glutamyl cysteine)PhysiologyBiochemistryMice0302 clinical medicinePregnancyquinone oxidoreductase 1) [noq1 (NAD(P)H]NAD(P)H Dehydrogenase (Quinone)gapdh glyceraldehyde-3-phosphate dehydrogenase geneP7 1 week after birthGSH (reduced glutathione)Oxidoreductases Acting on Sulfur Group Donorsme1 (malic enzyme 1 gene)glutathioneLungSpO2 oxygen saturationlcsh:QH301-705.5γ-GC–NEM gamma-glutamyl cysteine covalently bonded to N-ethylmaleimidechemistry.chemical_classification0303 health sciencesGSSG oxidized glutathioneGlutathione peroxidaseO14 (hypoxia group FiO2=14%)Brainm/z mass-to-charge ratioG18 18th day of gestationCell Hypoxia3. Good healthpgd (phosphogluconate dehydrogenase gene)In uterogclm glutamylcysteine ligase modifier subunit genesrnx1 sulfiredoxin 1 genelcsh:Medicine (General)me1 malic enzyme 1 genesrnx1 (sulfiredoxin 1 gene)gclm (glutamylcysteine ligase modifier subunit gene)γ-GC–NEM (gamma-glutamyl cysteine covalently bonded to N-ethylmaleimide)trxnd1 (thioredoxin reductase 1 gene)redox regulation03 medical and health sciencesnoq1 NAD(P)H:quinone oxidoreductase 1γ-GC gamma-glutamyl cysteineCySH L-cysteinePregnancyg6pdx (glucose 6 phosphate dehydrogenase gene)GlutathioneOxygenationgapdh (glyceraldehyde-3-phosphate dehydrogenase gene)medicine.diseaseMice Inbred C57BLOxygenP1 24 h after birthGCL glutamylcysteine ligasechemistryOxidative stressRedox regulationNEM (N-ethylmaleimide)O14 hypoxia group (FiO2=14%)GSH reduced glutathioneClinical Biochemistrymedicine.disease_causechemistry.chemical_compoundGlutathione Peroxidase GPX1GS–NEM reduced glutathione covalently bonded to N-ethylmaleimideSpO2 (oxygen saturation)oxidative stressg6pdx glucose 6 phosphate dehydrogenase genelcsh:R5-920GSSG (oxidized glutathione)G18 (18th day of gestation)gsr glutathione reductase geneGlutathionegpx1 glutathione peroxidase 1 genemedicine.anatomical_structurem/z (mass-to-charge ratio)LC–MS/MS (liquid chromatography coupled to tandem mass spectrometry)FemaleLC–MS/MS liquid chromatography coupled to tandem mass spectrometryO21 (normoxia group FiO2=21%)paO2 (partial pressure of oxygen)gpx1 (glutathione peroxidase 1 gene)Research Papernoq1 (NAD(P)H:quinone oxidoreductase 1)CySH (l-cysteine)FiO2 (inspiratory oxygen fraction)CyS–NEM (cysteine covalently bonded to N-ethylmaleimide)030225 pediatricsmedicineP7 (1 week after birth)AnimalsGCL (glutamylcysteine ligase)P1 (24 h after birth)O21 normoxia group (FiO2=21%)CyS–NEM cysteine covalently bonded to N-ethylmaleimide030304 developmental biologyGlutathione PeroxidaseLungOrganic ChemistryGS–NEM (reduced glutathione covalently bonded to N-ethylmaleimide)trxnd1 thioredoxin reductase 1 geneMolecular biologypaO2 partial pressure of oxygenAnimals NewbornGene Expression Regulationlcsh:Biology (General)NEM N-ethylmaleimidefetal-to-neonatal transitionoxygenOxidative stressFetal-to-neonatal transition
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