Search results for "GLUTATHIONE"

showing 10 items of 743 documents

A multiplex polymerase chain reaction protocol for the simultaneous analysis of the glutathione S-transferase GSTM1 and GSTT1 polymorphisms.

1996

Polymorphism GeneticbiologyBase Sequencebusiness.industryMolecular Sequence DataBiophysicsCell BiologyBiochemistryMolecular biologyPolymerase Chain ReactionReverse transcription polymerase chain reactionGlutathione S-transferaseReal-time polymerase chain reactionMultiplex polymerase chain reactionbiology.proteinMedicineHumansbusinessMolecular BiologyNested polymerase chain reactionDNA PrimersGlutathione TransferaseAnalytical biochemistry
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Oxidative stress and mitochondrial dysfunction in Kindler syndrome

2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License.-- et al.

Premature agingMaleKeratinocytesAdolescentComputingMilieux_LEGALASPECTSOFCOMPUTINGMitochondrionmedicine.disease_causePathogenesisKindler syndrome03 medical and health scienceschemistry.chemical_compound0302 clinical medicineBlistermedicineHumansGenetics(clinical)Pharmacology (medical)Photosensitivity DisordersGenodermatosisChildGenetics (clinical)Cells CulturedPeriodontal Diseases030304 developmental biologyAged 80 and overMedicine(all)0303 health sciencesintegumentary systemResearchGeneral MedicineGlutathioneMiddle Agedmedicine.diseaseMalondialdehydeMolecular biology3. Good healthMitochondriaOxidative StresschemistryOxidative stress030220 oncology & carcinogenesisChild PreschoolFemaleSkin cancerEpidermolysis BullosaKindlin1Oxidative stressOrphanet Journal of Rare Diseases
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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Glutathione content, glutathione S-transferase and γ-glutamyltranspeptidase activities in mid-gut gland of Procambarus clarkii: time course in the pr…

1988

Procambarus clarkiiCadmiumbiologyγ glutamyltranspeptidasechemistry.chemical_elementMidgutGlutathionebiology.organism_classificationBiochemistrychemistry.chemical_compoundGlutathione S-transferasechemistryBiochemistryTime coursebiology.proteinBiochemical Society Transactions
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Regulation of tumour cell sensitivity to TNF-induced oxidative stress and cytotoxicity: Role of glutathione

1998

Glutathione (GSH) and the rate of cellular proliferation determine tumour cell sensitivity to tumour necrosis factor (TNF). Buthionine sulphoximine (BSO), a selective inhibitor of GSH synthesis, inhibits tumour growth and increases recombinant human TNF (rhTNF)-alpha cytoxicity in vitro. Administration of sublethal doses of rhTNF-alpha to Ehrlich ascites-tumour (EAT)-bearing mice induces oxidative stress (as measured by increases in intracellular peroxide levels, O2.- generation and mitochondrial GSSG). ATP-induced selective GSH depletion, when combined with rhTNF-alpha administration, affords a 61% inhibition of tumour growth and results in a significant extent of host survival. Administra…

Programmed cell deathCell SurvivalClinical BiochemistryMitochondrionPharmacologyBiologymedicine.disease_causeBiochemistryMicechemistry.chemical_compoundSuperoxidesmedicineAnimalsHumansCarcinoma Ehrlich TumorGlutathione DisulfideTumor Necrosis Factor-alphaGeneral MedicineGlutathioneGlutathioneRecombinant ProteinsOxidative StresschemistryBiochemistryCancer cellMolecular MedicineGlutathione disulfideTumor necrosis factor alphaOxidative stressIntracellularBioFactors
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Glutathione in Cancer Biology and Therapy

2006

The glutathione (GSH) content of cancer cells is particularly relevant in regulating mutagenic mechanisms, DNA synthesis, growth, and multidrug and radiation resistance. In malignant tumors, as compared with normal tissues, that resistance associates in most cases with higher GSH levels within these cancer cells. Thus, approaches to cancer treatment based on modulation of GSH should control possible growth-associated changes in GSH content and synthesis in these cells. Despite the potential benefits for cancer therapy of a selective GSH-depleting strategy, such a methodology has remained elusive up to now. Metastatic spread, not primary tumor burden, is the leading cause of cancer death. Fo…

Programmed cell deathClinical BiochemistryApoptosisBiologyGeneral Biochemistry Genetics and Molecular BiologyProinflammatory cytokinechemistry.chemical_compoundCancer stem cellNeoplasmsmedicineAnimalsHumansNeoplasm MetastasisButhionine SulfoximineBiochemistry (medical)CancerGlutathionemedicine.diseaseGlutathionePrimary tumorExtravasationGenes bcl-2chemistryCancer cellImmunologyCancer researchCritical Reviews in Clinical Laboratory Sciences
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Targeting the mitochondrial pathway to induce apoptosis/necrosis through ROS by a newly developed Schiff’s base to overcome MDR in cancer

2011

Abstract Multidrug resistance (MDR) in cancer, a major obstacle to successful application of cancer chemotherapy, is often characterized by over-expression of multidrug resistance-related proteins such as MRP1, P-gp or elevated glutathione (GSH) level. Efflux of drugs by functional P-gp, MRP1 and elevated GSH level can confer resistance to apoptosis induced by a range of different stimuli. Therefore, it is necessary to develop new cell death inducers with relatively lower toxicity toward non-malignant cells that can overcome MDR by induction of apoptotic or non-apoptotic cell death pathways. Herein we report the synthesis and spectroscopic characterization of a GSH depleting, redox active S…

Programmed cell deathMagnetic Resonance SpectroscopyNecrosisApoptosisMitochondrionBiologymedicine.disease_causeBiochemistryEhrlich ascites carcinomaMiceNecrosisCell Line TumorNeoplasmsSpectroscopy Fourier Transform InfraredmedicineAnimalsCytotoxic T cellCytotoxicitySchiff BasesCalpainCaspase 3General MedicineFlow CytometryGlutathioneMitochondriaBiochemistryDrug Resistance NeoplasmApoptosisCancer researchCalciumSpectrophotometry Ultravioletmedicine.symptomReactive Oxygen SpeciesOxidative stressBiochimie
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Tumor Cytotoxicity by Endothelial Cells

2003

High GSH content associates with high metastatic activity in B16-F10 melanoma cells cultured to low density (LD B16M). GSH homeostasis was investigated in LD B16M cells that survive after adhesion to the hepatic sinusoidal endothelium (HSE). Invasive B16M (iB16M) cells were isolated using anti-Met-72 monoclonal antibodies and flow cytometry-coupled cell sorting. HSE-derived NO and H(2)O(2) caused GSH depletion and a decrease in gamma-glutamylcysteine synthetase activity in iB16M cells. Overexpression of gamma-glutamylcysteine synthetase heavy and light subunits led to a rapid recovery of cytosolic GSH, whereas mitochondrial GSH (mtGSH) further decreased during the first 18 h of culture. NO …

Programmed cell deathmedicine.diagnostic_testLiver cytologyCell BiologyGlutathioneBiologymedicine.disease_causeBiochemistryIn vitroCell biologyFlow cytometrychemistry.chemical_compoundCytosolchemistrymedicineMolecular BiologyHomeostasisOxidative stressJournal of Biological Chemistry
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Evolutionary and structural analyses of GDAP1, involved in Charcot-Marie-Tooth disease, characterize a novel class of glutathione transferase-related…

2003

Mutations in the Ganglioside-induced differentiation-associated protein-1 (GDAP1) gene cause autosomal recessive Charcot-Marie-Tooth disease type 4A. The protein encoded by GDAP1 shows clear similarity to glutathione transferases (also known as glutathione S-transferases or GSTs). The human genome contains a paralog of GDAP1 called GDAP1L1. Using comparative genomics, we show that orthologs of GDAP1 and GDAP1L1 are found in mammals, birds, amphibians, and fishes. Likely orthologs of those genes in invertebrates and a low but consistent similarity with some plant and eubacterial genes have also been found. We demonstrate that GDAP1 and GDAP1L1 do not belong to any of the known classes of GST…

Protein ConformationMolecular Sequence DataSequence alignmentNerve Tissue ProteinsBiologyEvolution MolecularProtein structurePhylogeneticsCharcot-Marie-Tooth DiseaseDatabases GeneticGeneticsCluster AnalysisHumansAmino Acid SequenceMolecular BiologyPeptide sequenceGeneEcology Evolution Behavior and SystematicsPhylogenyGlutathione TransferaseComparative genomicsGeneticsTransmembrane domainMultigene FamilyHuman genomeSequence AlignmentMolecular biology and evolution
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Two amino acid residues determine the low substrate affinity of human cationic amino acid transporter-2A.

2003

Mammalian cationic amino acid transporters (CAT) differ in their substrate affinity and sensitivity to trans-stimulation. The apparent Km values for cationic amino acids and the sensitivity to trans-stimulation of CAT-1, -2B, and -3 are characteristic of system y+. In contrast, CAT-2A exhibits a 10-fold lower substrate affinity and is largely independent of substrate at the trans-side of the membrane. CAT-2A and -2B demonstrate such divergent transport properties, even though their amino acid sequences differ only in a stretch of 42 amino acids. Here, we identify two amino acid residues within this 42-amino acid domain of the human CAT-2A protein that are responsible for the apparent low af…

Protein ConformationRecombinant Fusion ProteinsBlotting WesternGreen Fluorescent ProteinsMolecular Sequence DataGene ExpressionArginineTransfectionBiochemistryStructure-Activity RelationshipXenopus laevisExtracellularAnimalsHumansBiotinylationAmino acid transporterAmino Acid SequenceAmino AcidsCationic Amino Acid Transporter 2Molecular BiologyGlutathione Transferasechemistry.chemical_classificationBinding SitesSubstrate (chemistry)Biological TransportCell BiologyPhoto-reactive amino acid analogAmino acidTransmembrane domainLuminescent ProteinsS-tagchemistryBiochemistryMutagenesis Site-DirectedOocytesElectrophoresis Polyacrylamide GelFemaleIntracellularThe Journal of biological chemistry
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