Search results for "glutathione transferase"

showing 10 items of 84 documents

Blood Glutathione as an Index of Radiation-Induced Oxidative Stress in Mice and Humans

1997

Abstract The effect of x-rays on GSH and GSSG levels in blood was studied in mice and humans. An HPLC method that we recently developed was applied to accurately determine GSSG levels in blood. The glutathione redox status (GSH/GSSG) decreases after irradiation. This effect is mainly due to an increase in GSSG levels. Mice received single fraction radiotherapy, at total doses of 1.0 to 7.0 Gy. Changes in GSSG in mouse blood can be detected 10 min after irradiation and last for 6 h within a range of 2.0–7.0 Gy. The highest levels of GSSG (20.1 ± 2.9 μ M), a 4.7-fold increase as compared with controls) in mouse blood are found 2 h after radiation exposure (5 Gy). Breast and lung cancer patien…

Maleinorganic chemicalsmedicine.medical_specialtyLung NeoplasmsRadicalBreast NeoplasmsRadiation inducedOxidative phosphorylationGlucosephosphate Dehydrogenasemedicine.disease_causeBiochemistryMicechemistry.chemical_compoundfluids and secretionsPhysiology (medical)Internal medicinemedicineAnimalsHumansIrradiationRadiation InjuriesChromatography High Pressure LiquidGlutathione TransferaseGlutathione PeroxidaseGlutathione DisulfideChemistryDose-Response Relationship RadiationGlutathioneGlutathioneRedox statusSingle fractionOxidative StressGlutathione ReductaseEndocrinologyBiochemistryFemaleOxidation-ReductionOxidative stressFree Radical Biology and Medicine
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The Effect of Indobufen on the Activities of Selected Rat Liver Phase I and Phase II Drug Metabolizing Enzymes, Peroxisomal β-oxidation and Hepatic G…

1994

Abstract Oral administration of indobufen to male rats for three days at daily doses of 5, 10 and 20 mg kg−1 resulted in no changes in liver total glutathione, cytosolic glutathione S-transferases or microsomal epoxide hydrolase. Reduced glutathione appeared slightly diminished to about 84% of control at the highest dose level. Microsomal cytochrome P450-dependent ethoxyresorufin O-de-ethylase and pentoxyresorufin de-alkylase activities were decreased to 64% (not significantly) and 67% of control at the lowest dose level. 6α- and 7α-Hydroxytestosterone activities were decreased to 67 and 68% of control at the highest dose level. Cyanide-insensitive peroxisomal fatty acid β-oxidation was inc…

Malemedicine.medical_specialtyPharmaceutical ScienceIsoindolesBiologyMicrobodieschemistry.chemical_compoundCytochrome P-450 Enzyme SystemOral administrationInternal medicinemedicineAnimalsGlutathione TransferaseEpoxide HydrolasesPharmacologychemistry.chemical_classificationIndobufenDose-Response Relationship DrugFatty AcidsFatty acidCytochrome P450Rats Inbred StrainsGlutathionePeroxisomeGlutathionePhenylbutyratesRatsEndocrinologyLiverchemistryMicrosomal epoxide hydrolaseMicrosomebiology.proteinOxidation-Reductionmedicine.drugJournal of Pharmacy and Pharmacology
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Some glutathione-related enzymic activities in skeletal muscle and myocardium of the rat : adaptations to endurance training

1991

Malemedicine.medical_specialtyPhysical ExertionBiologyBiochemistrychemistry.chemical_compoundCytosolEndurance trainingInternal medicinemedicineAnimalsGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseSuperoxide DismutaseMusclesMyocardiumSkeletal muscleRats Inbred StrainsGlutathioneGlutathioneRatsIsoenzymesEndocrinologyEnzymemedicine.anatomical_structureGlutathione ReductasechemistryPhysical EnduranceBiochemical Society Transactions
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Characterization of cryopreserved rat liver parenchymal cells by metabolism of diagnostic substrates and activities of related enzymes

1992

The metabolism of testosterone and benzo(a)pyrene (BaP) which is mediated by diverse enzymes was determined in cryopreserved rat liver parenchymal cells and compared with that found in freshly isolated cells. In addition, the activities of single xenobiotic-metabolizing enzymes were measured by using specific substrates. The cytochrome P450 (P450)-mediated total metabolic conversion of testosterone was reduced to 55% in cryopreserved cells. The metabolite profile, i.e. the formation of single metabolites compared with total metabolic conversion, was however unchanged when compared with freshly isolated cells. A concomitant reduction in the activities of the involved P450 isoenzymes can ther…

MetaboliteCell CountBiologyHydroxylationBiochemistryIsozymeCryopreservationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemBenzo(a)pyreneAnimalsTestosteroneGlutathione TransferaseCryopreservationPharmacologyProteinsCytochrome P450Trypan BlueMetabolismArylsulfotransferaseRatsLiverchemistryBiochemistryCell culturebiology.proteinPercollDrug metabolismBiochemical Pharmacology
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Glutathione Conjugation of Bay- and Fjord-Region Diol Epoxides of Polycyclic Aromatic Hydrocarbons by Glutathione Transferases M1-1 and P1-1

1997

Metabolism of polycyclic aromatic hydrocarbons in mammalian cells results in the formation of vicinal diol epoxides considered as ultimate carcinogens if the oxirane ring is located in a bay- or fjord-region of the parent compound. In the present study, individual stereoisomers of the bay-region diol epoxides of chrysene, dibenz[a,h]anthracene, and benzo[a]pyrene as well as of the fjord-region diol epoxides of benzo[c]phenanthrene, benzo[c]chrysene, and benzo[g]-chrysene have been incubated with GSH in the presence of human glutathione transferases GSTM1-1 (a mu-class enzyme) and GSTP1-1 (a pi-class enzyme). As previously shown with GSTA1-1 (an alpha-class enzyme) both M1-1 and P1-1 demonst…

Models MolecularChryseneStereochemistryConjugated systemToxicologySubstrate Specificitychemistry.chemical_compoundpolycyclic compoundsHumansPolycyclic Aromatic HydrocarbonsCarcinogenGlutathione TransferaseBay-Region Polycyclic Aromatic Hydrocarbonchemistry.chemical_classificationAnthraceneintegumentary systemStereoisomerismGeneral MedicineGlutathionePhenanthreneGlutathioneIsoenzymesKineticsEnzymechemistryCarcinogensEpoxy CompoundsPyreneCrystallizationChemical Research in Toxicology
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Diversity of Omega Glutathione Transferases in mushroom-forming fungi revealed by phylogenetic, transcriptomic, biochemical and structural approaches

2021

International audience; The Omega class of glutathione transferases (GSTs) forms a distinct class within the cytosolic GST superfamily because most of them possess a catalytic cysteine residue. The human GST Omega 1 isoform was first characterized twenty years ago, but it took years of work to clarify the roles of the human isoforms. Concerning the kingdom of fungi, little is known about the cellular functions of Omega glutathione transferases (GSTOs), although they are widely represented in some of these organisms. In this study, we re-assess the phylogeny and the classification of GSTOs based on 240 genomes of mushroom-forming fungi (Agaricomycetes). We observe that the number of GSTOs is…

Models MolecularGene isoformProtein ConformationCrystallography X-RayMicrobiologyAgaricomycetesstructure-functionFungal ProteinsSerine03 medical and health scienceschemistry.chemical_compoundPhylogeneticsGeneticsPolyporalesflavonoid[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyglutathionePhylogeny[SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/MycologyGlutathione Transferase030304 developmental biologychemistry.chemical_classification0303 health sciencesBinding Sitesbiology030306 microbiologyGene Expression ProfilingGenetic VariationGlutathionebiology.organism_classificationenzymeEnzymeBiochemistrychemistryfungi[SDE.BE]Environmental Sciences/Biodiversity and EcologyAgaricalesCysteine[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/Symbiosis
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Genome-wide association study identifies five loci associated with lung function

2009

Pulmonary function measures are heritable traits that predict morbidity and mortality and define chronic obstructive pulmonary disease (COPD). We tested genome-wide association with forced expiratory volume in 1 s (FEV(1)) and the ratio of FEV(1) to forced vital capacity (FVC) in the SpiroMeta consortium (n = 20,288 individuals of European ancestry). We conducted a meta-analysis of top signals with data from direct genotyping (n < or = 32,184 additional individuals) and in silico summary association data from the CHARGE Consortium (n = 21,209) and the Health 2000 survey (n < or = 883). We confirmed the reported locus at 4q31 and identified associations with FEV(1) or FEV(1)/FVC and co…

OncologySpirometryMalemedicine.medical_specialtyVital capacityPopulationReceptor for Advanced Glycation End ProductsVital CapacityGenome-wide association studyBiologyPolymorphism Single NucleotideArticlePulmonary function testing03 medical and health sciencesFEV1/FVC ratioPulmonary Disease Chronic Obstructive0302 clinical medicineMeta-Analysis as TopicInternal medicineTensinsForced Expiratory VolumeGeneticsmedicineHumansRNA MessengerReceptors ImmunologiceducationLung030304 developmental biologyGlutathione Transferase0303 health scienceseducation.field_of_studyCOPDmedicine.diagnostic_testGenome HumanGene Expression ProfilingMicrofilament Proteinsrespiratory systemmedicine.disease3. Good healthRespiratory Function Tests030228 respiratory systemSpirometryImmunologyFemaleReceptors Serotonin 5-HT4Hedgehog interacting proteinThrombospondinsGenome-Wide Association Study
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Significance of Various Enzymes in the Control of Mutagenic and Carcinogenic Metabolites Derived from Aromatic Structures

1984

One important early contribution to the control of chemical carcinogenesis is provided by the enzyme pattern responsible for the generation and disposition of reactive metabolites. Especially well studied is the important group of enzymes responsible for the control of reactive epoxides. Many natural as well as man-made foreign compounds, including Pharmaceuticals, possess olefinic or aromatic double bonds. Such compounds can be transformed to epoxides by microsomal monooxygenases present in very many mammalian organs. By virtue of their electrophilic reactivity such epoxides may spontaneously react with nucleophilic centers in the cell and thus covalently bind to DNA, RNA, and protein. Su…

Oxidoreductases Acting on CH-CH Group Donors040301 veterinary sciencesEpoxideToxicology030226 pharmacology & pharmacyMixed Function OxygenasesPathology and Forensic Medicine0403 veterinary scienceToxicology03 medical and health scienceschemistry.chemical_compoundCytosol0302 clinical medicineBiosynthesisAnimalsPolycyclic CompoundsMolecular BiologyCarcinogenGlutathione TransferaseEpoxide Hydrolaseschemistry.chemical_classification04 agricultural and veterinary sciencesCell BiologyMetabolismMonooxygenaseEnzymesAlcohol OxidoreductasesKineticsEnzymechemistryBiochemistryEpoxide HydrolasesCarcinogensMicrosomes LiverOxidoreductasesDNAMutagensToxicologic Pathology
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The activity of glutathione S-transferase in hepatopancreas of Procambarus clarkii: Seasonal variations and the influence of environmental pollutants

1991

Abstract 1. 1The glutathione S -transferase activity in hepatopancreas of the American red crayfish Procambarus clarkii after 15 days' acclimatization in tap water aquaria was measured in specimens collected monthly for a whole year, and shows seasonal variation. 2. 2. Previous data on the environmental pollution of Lake Albufera suggest a possible correlation with the activity tested in the different seasons of the year considering the results of non-acclimatized animals.

PharmacologyPollutantProcambarus clarkiiImmunologyZoologyEnvironmental pollutionAstacoideaGlutathioneBiologySeasonalitybiology.organism_classificationmedicine.diseaseCrayfishAcclimatizationToxicologychemistry.chemical_compoundchemistrymedicineAnimalsHepatopancreasSeasonsDigestive SystemWater Pollutants ChemicalGlutathione TransferaseComparative Biochemistry and Physiology Part C: Comparative Pharmacology
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PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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