Search results for "Glutathion"

showing 10 items of 744 documents

Different impacts of cardiovascular risk factors on oxidative stress.

2011

The objective of the study was to evaluate oxidative stress (OS) status in subjects with different cardiovascular risk factors. With this in mind, we have studied three models of high cardiovascular risk: hypertension (HT) with and without metabolic syndrome, familial hypercholesterolemia (FH) and familial combined hyperlipidemia (FCH) with and without insulin resistance. Oxidative stress markers (oxidized/reduced glutathione ratio, 8-oxo-deoxyguanosine and malondialdehide) together with the activity of antioxidant enzyme triad (superoxide dismutase, catalase, glutathione peroxidase) and activation of both pro-oxidant enzyme (NAPDH oxidase components) and AGTR1 genes, as well as antioxidant…

MaleGPX1Antioxidantmedicine.medical_treatmentGlutathione reductaseHyperlipidemia Familial Combinedmedicine.disease_causelcsh:Chemistrychemistry.chemical_compoundRisk FactorsMalondialdehydeoxidative stressglutathione peroxidaselcsh:QH301-705.5Spectroscopychemistry.chemical_classificationbiologyfamilial hypercholesterolemiaChemistryGlutathione peroxidaseGeneral MedicineMiddle AgedCatalaseGlutathioneComputer Science ApplicationsGlutathione Reductase8-Hydroxy-2'-DeoxyguanosineCardiovascular DiseasesFemaleThioredoxinAdultmedicine.medical_specialtyhypertensionmRNACatalysisGlutathione SynthaseArticleInorganic ChemistrySuperoxide dismutaseHyperlipoproteinemia Type IIInternal medicinemedicineHumansPhysical and Theoretical ChemistryMolecular BiologySuperoxide DismutaseGene Expression ProfilingOrganic ChemistryDeoxyguanosineNADPH OxidasesGlutathionesuperoxide dismutasesPhosphoproteinscombined familial dyslipidemiaEndocrinologylcsh:Biology (General)lcsh:QD1-999biology.proteinOxidative stressBiomarkersInternational journal of molecular sciences
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Regulation of glutathione metabolism in Ehrlich ascites tumour cells.

1992

Glutathione metabolism was studied in cancer cells during the growth of an Ehrlich ascites tumour. GSH, but not GSSG, content decreases when cell proliferation and the rate of protein synthesis in the tumour decrease. This change correlates with a decrease in the rate of GSH synthesis and an increase in glutathione peroxidase and glutathione S-transferase activities. Glutathione efflux from tumour cells seems to co-ordinate with the rate of GSH synthesis. Cysteine, and not methionine, promotes GSH synthesis in tumour cells. However, changes in the rate of GSH synthesis are not due to limitations in the supply of blood cysteine or to changes in the intracellular amino acid pool of the cancer…

MaleGPX1Glutathione reductaseProtein metabolismMice Inbred StrainsBiologyGlucosephosphate DehydrogenaseBiochemistrychemistry.chemical_compoundMiceMethionineReference ValuesAnimalsAmino AcidsCarcinoma Ehrlich TumorMolecular BiologyCells CulturedGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseGlutathione DisulfideGlutathione peroxidaseCell BiologyGlutathioneGlutathioneAcetylcysteineRatsKineticsGlutathione ReductasechemistryBiochemistryLiverCancer cellGlutathione disulfidesense organsCell DivisionCysteineSubcellular FractionsResearch ArticleThe Biochemical journal
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Silibinin improves hepatic and myocardial injury in mice with nonalcoholic steatohepatitis

2012

Abstract Background Nonalcoholic fatty liver disease is a chronic metabolic disorder with significant impact on cardiovascular and liver mortality. Aims In this study, we examined the effects of silibinin on liver and myocardium injury in an experimental model of nonalcoholic fatty liver disease. Methods A four-week daily dose of silibinin (20 mg/kg i.p.) was administrated to db/db mice fed a methionine–choline deficient diet. Hepatic and myocardial histology, oxidative stress and inflammatory cytokines were evaluated. Results Silibinin administration decreased HOMA-IR, serum ALT and markedly improved hepatic and myocardial damage. Silibinin reduced isoprostanes, 8-deoxyguanosine and nitrit…

MaleGene ExpressionIsoprostanesmedicine.disease_causeGastroenterologyAntioxidantsMicechemistry.chemical_compoundMethionineNon-alcoholic Fatty Liver DiseaseNonalcoholic fatty liver diseasePhosphorylationGastroenterologyAlanine TransaminaseGlutathioneCholine DeficiencyMitochondrial respiratory chainLiverHeart Inflammation NAFLD Oxidative stress SilibininCytokinesmedicine.symptomSilymarinmedicine.medical_specialtySilibininInflammationStatistics NonparametricProinflammatory cytokineInsulin resistanceInternal medicinemedicineAnimalsNitritesAnalysis of VarianceNitratesHepatologySettore BIO/16 - Anatomia Umanabusiness.industryMyocardiumJNK Mitogen-Activated Protein KinasesGlutathionemedicine.diseaseDietFatty LiverOxidative StressEndocrinologychemistrySilybinInsulin ResistancebusinessOxidative stressDigestive and Liver Disease
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Increased Oxidative Damage Associated with Unfavorable Cytogenetic Subgroups in Chronic Lymphocytic Leukemia

2014

Oxidative stress contributes to genomic instability in chronic lymphocytic leukemia (CLL), but its relationship with the acquisition of specific chromosomal abnormalities is unknown. We recruited 55 untreated CLL patients and assessed 8-oxo-2′-deoxyguanosine (8-oxo-dG), glutathione, and malondialdehyde (MDA) levels, and we compared them among the cytogenetic subgroups established using fluorescence in situ hybridization (FISH). Significant increases in 8-oxo-dG and/or MDA were observed in patients with unfavorable cytogenetic aberrations (17p and 11q deletions) compared to the 13q deletion group.TP53deletion patients exhibited a diminished DNA repair efficiency. Finally, cases with normal F…

MaleGenome instabilityArticle SubjectDNA RepairDNA damageDNA repairChronic lymphocytic leukemialcsh:MedicineBiologymedicine.disease_causeGeneral Biochemistry Genetics and Molecular BiologyCohort Studieschemistry.chemical_compoundMalondialdehydemedicineHumansLymphocytesIn Situ Hybridization FluorescenceAgedAged 80 and overChromosome AberrationsGeneral Immunology and Microbiologymedicine.diagnostic_testlcsh:RDeoxyguanosineGeneral MedicineGlutathioneMiddle AgedMalondialdehydemedicine.diseaseGlutathioneLeukemia Lymphocytic Chronic B-CellOxidative Stresschemistry8-Hydroxy-2'-DeoxyguanosineImmunologyFemaleLipid PeroxidationReactive Oxygen SpeciesGene DeletionOxidative stressDNA DamageResearch ArticleFluorescence in situ hybridizationBioMed Research International
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Effects of polymorphisms in vitamin E-, vitamin C-, and glutathione peroxidase-related genes on serum biomarkers and associations with glaucoma.

2012

Purpose To study the association of selected polymorphism in genes related to vitamin E, vitamin C, and glutathione peroxidase with these biomarkers and primary open-angle glaucoma (POAG) risk. Methods A case-control study matched for age, sex, and bodyweight was undertaken. Two hundred fifty POAG cases and 250 controls were recruited from a Mediterranean population. Plasma concentrations of vitamin C, vitamin E, and glutathione peroxidase (GPx) activity were measured. We analyzed the polymorphisms rs1279683 in the Na+-dependent L-ascorbic acid transporter 2 (SLC23A2) gene, rs6994076 in the tocopherol alpha transfer protein (TTPA) gene, rs737723 in the tocopherol-associated protein (SEC14L2…

MaleGlutathione PeroxidasePolymorphism Geneticgenetic structuresLipoproteinsEpistasis GeneticAscorbic AcidMiddle AgedPhospholipid Hydroperoxide Glutathione PeroxidasePolymorphism Single Nucleotideeye diseasesRisk FactorsCase-Control StudiesTrans-ActivatorsHumansVitamin EFemaleCarrier ProteinsSodium-Coupled Vitamin C TransportersBiomarkersGenetic Association StudiesGlaucoma Open-AngleAgedResearch ArticleMolecular vision
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Modification of hepatic drug-metabolizing enzymes in rat fed naturally occurring allyl sulphides

1994

1. The effects of feeding allyl sulphides to rat (2000 ppm of the diet for 15 days) were investigated on various microsomal hepatic drug-metabolizing enzymes by their immunochemical detection and catalytic activity. 2. Allyl sulphides provoked a temporary dietary restriction, which enhanced the microsomal level of P450 and the activities of NADH-cytochrome c reductase and p-hydroxybiphenyl UDP-glucuronyltransferase (UDPGT 2), and lowered the activities of p-nitrophenol hydroxylase (PNPH), N-nitrosodimethylamine demethylase (NDMAD), laurate omega-hydroxylase (LAH) and glutathione S-transferase (GST). Therefore, pair-fed animals were used as a more relevant control for the dietary effects of …

MaleHealth Toxicology and MutagenesisImmunoblottingAllyl compoundAntineoplastic Agents[SDV.BID]Life Sciences [q-bio]/BiodiversitySulfidesReductaseToxicologyBiochemistryEating03 medical and health scienceschemistry.chemical_compound0302 clinical medicineIMMUNOCHIMIECytochrome P-450 Enzyme SystemAnimalsDisulfidesGlucuronosyltransferaseRats WistarEpoxide hydrolaseAnticarcinogenGlutathione Transferase030304 developmental biologyEpoxide HydrolasesPharmacologychemistry.chemical_classification0303 health sciencesDose-Response Relationship DrugbiologyChemistryBody WeightCytochrome P450Organ SizeGeneral MedicineGlutathioneDietRatsAllyl CompoundsEnzymeLiverBiochemistryTOXICOLOGIE030220 oncology & carcinogenesisMicrosomes Liverbiology.proteinMicrosomeRAT[SDV.BID] Life Sciences [q-bio]/Biodiversity
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A Simple Microassay for the Determination of Hydrazine in Biological Samples. Effect of Hydrazine and Isoniazid on Liver and Brain Glutathione

1987

A simple microassay for the determination of hydrazine in laboratory samples is presented. The colored product of the reaction of p-dimethylaminobenzaldehyde with hydrazine was tested at 470 nm using double-beam mode in different samples. Internal standards and data on blood serum, liver, and brain of rats treated with hydrazine or isoniazid are presented. The tissue glutathione content of these rats was determined, and the possible implication of glutathione in the brain toxicity of hydrazine is discussed.

MaleHealth Toxicology and MutagenesisMetaboliteToxicologyAnalytical Chemistrychemistry.chemical_compoundBlood serumSpectrophotometryIsoniazidmedicineAnimalsEnvironmental ChemistryHydrazine (antidepressant)Brain ChemistryChemical Health and SafetyChromatographymedicine.diagnostic_testIsoniazidMetabolismGlutathioneGlutathioneRatsHydrazinesLiverchemistryBiochemistryToxicitymedicine.drugJournal of Analytical Toxicology
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Irreversible protein binding of acrylonitrile.

1981

1. After i.p. injection of [2,3-14C]acrylonitrile to rats, a significant portion of radioactivity becomes irreversibly attached to proteins of liver, lung, spleen and other tissues. 2. When rat liver microsomes were incubated with [2,3-14C]acrylonitrile, a time-dependent irreversible binding of radioactivity occurred to microsomal proteins. This binding was not dependent on NADPH. A high extent of binding to heat-inactivated microsomes indicated that no enzymic metabolic step was involved. 3. The irreversible binding of [2,3-14C]acrylonitrile to rat liver microsomal protein in vitro was inhibited by thiols (cysteine, glutathione, mercaptoethanol). The greatest inhibitory potency was display…

MaleHot TemperatureHealth Toxicology and MutagenesisSpleenPlasma protein bindingToxicologyBiochemistryDithiocarbchemistry.chemical_compoundNitrilesmedicineAnimalsSulfhydryl CompoundsPharmacologyAcrylonitrileChemistryGeneral MedicineGlutathioneIn vitroRatsmedicine.anatomical_structureBiochemistryLiverMicrosomeMicrosomes LiverAcrylonitrileDitiocarbSpleenCysteineProtein BindingXenobiotica; the fate of foreign compounds in biological systems
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Hepatic metabolism of diallyl disulfide in rat and man

2003

International audience; 1. The metabolism of diallyl disulphide was investigated in vitro with rat and human liver cell subfractions and ex vivo with an isolated perfused rat liver. 2. Diallyl disulphide was oxidized to diallylthiosulphinate by rat liver microsomes with an apparent K-m = 0.86 +/- 0.1 mM and an apparent V-max = 0.47 +/- 0.12 nmol min(-1) mg(-1) protein (mean +/- SE). Both cytochrome P450 (CYP) and flavin-containing monooxygenases were involved, with CYP2B1/2 and CYP2E1 being the most active CYP enzymes. 3. In rat and man, microsomal oxidation of allylmethyl sulphide to allylmethyl sulphoxide and allylmethyl sulphone also occurred, although at a low rate. Diallyl disulphide w…

MaleLIVERHealth Toxicology and MutagenesisToxicologyBiochemistryGARLICchemistry.chemical_compoundDisulfides0303 health sciencesbiologyDADS030302 biochemistry & molecular biologyCytochrome P-450 CYP2E1General MedicineCYP2E1Middle Agedfoie3. Good healthEnzymesAllyl CompoundsPerfusionBiochemistryArea Under CurveMicrosomes LiverFemaleAryl Hydrocarbon HydroxylasesOxidation-Reductionailcomposé soufrexénobiotique[SDV.BID]Life Sciences [q-bio]/BiodiversityIn Vitro Techniques03 medical and health sciencesAnimalsHumansmétabolisme030304 developmental biologyAgedPharmacologySulfur CompoundsEX VIVOCytochrome P450SULFUR COMPOUNDMetabolismGlutathioneMonooxygenaseRatschemistryDADS;EX VIVO;SULFUR COMPOUND;XENOBIOTIC METABOLISM;GARLIC;LIVER;RATCytochrome P-450 CYP2B1Steroid HydroxylasesMicrosomebiology.proteinRATAllyl MercaptanXENOBIOTIC METABOLISMDrug metabolism
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Chronic hydrogen peroxide intake and peroxide metabolizing enzyme activities in some tissues of mice and rats

1986

Chronic daily intake of 0.5% H2O2 in drinking water decreased Se-dependent glutathione peroxidase (Se-GSHPx) activity in rat skeletal muscle, kidney and liver. Non-Se GSHPx activity decreased in kidney. Deprivation of drinking water decreased Se-GSHPx activity in kidney and non-Se GSHPx activity in kidney and liver. H2O2 intake decreased activity of catalase in rat skeletal muscle. H2O2 intake or water deprivation caused no changes in these enzyme activities in mice.

MaleLipid Peroxidesmedicine.medical_specialtyAntioxidantmedicine.medical_treatmentKidneyMiceSeleniumCellular and Molecular Neurosciencechemistry.chemical_compoundOral administrationInternal medicinemedicineAnimalsHydrogen peroxideMolecular BiologyPharmacologychemistry.chemical_classificationGlutathione PeroxidaseKidneyWater DeprivationbiologyMusclesMyocardiumGlutathione peroxidaseSkeletal muscleHydrogen PeroxideCell BiologyCatalaseEndocrinologymedicine.anatomical_structureLiverchemistryCatalaseToxicitybiology.proteinMolecular MedicineExperientia
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