Search results for "SUPEROXIDE DISMUTASE"

showing 10 items of 296 documents

Age-dependent regulation of antioxidant genes by p38α MAPK in the liver

2018

p38α is a redox sensitive MAPK activated by pro-inflammatory cytokines and environmental, genotoxic and endoplasmic reticulum stresses. The aim of this work was to assess whether p38α controls the antioxidant defense in the liver, and if so, to elucidate the mechanism(s) involved and the age-related changes. For this purpose, we used liver-specific p38α-deficient mice at two different ages: young-mice (4 months-old) and old-mice (24 months-old). The liver of young p38α knock-out mice exhibited a decrease in GSH levels and an increase in GSSG/GSH ratio and malondialdehyde levels. However, old mice deficient in p38α had higher hepatic GSH levels and lower GSSG/GSH ratio than young p38α knock-…

ROS Reactive oxygen species;RSK1 Ribosomal S6 kinase10301 basic medicineMAPK/ERK pathwayAgingHPLC High-performance liquid chromatographyAntioxidantmedicine.medical_treatmentTBP TATA-binding proteinClinical BiochemistryDEN Diethyl nitrosamine;MKP-1 MAPK phosphatase-1IκB kinaseGCLc Glutamate cysteine ligase catalytic subunitp38 Mitogen-Activated Protein KinasesG6PDH Glucose-6-phosphate dehydrogenaseBiochemistryAntioxidantsMicechemistry.chemical_compoundSuperoxide Dismutase-1Akt Protein kinase B0302 clinical medicineNrf2 Nuclear factor erythroid 2-related factor-2IL InterleukinSOD1 Cu/Zn-superoxide dismutaselcsh:QH301-705.5Mice KnockoutMK2 MAP-activated protein kinase 2;PGC-1α Peroxisome proliferator-activated receptor gamma coactivator 1-alphachemistry.chemical_classificationlcsh:R5-920Trx ThioredoxinGlutathione DisulfideTNF-α Tumor necrosis factor-alphabiologyLPS Lipopolysaccharide;GSSG Oxidized glutathione;MEF Mouse embryonic fibroblastsNF-kappa BGstm1 Glutathione S-transferase mu 1CatalaseEndoplasmic Reticulum StressGlutathioneLiverGSH Reduced glutathione;Catalase030220 oncology & carcinogenesisJNK c-Jun N-terminal kinaselcsh:Medicine (General)Research Papermedicine.medical_specialtyNF-E2-Related Factor 2Glutamate-Cysteine LigaseMKK MAPK kinaseAP-1 Activator protein-1IKK IƙB KinaseGene Expression Regulation EnzymologicSuperoxide dismutase03 medical and health sciencesInternal medicineGlutamate cysteine ligaseEGFR Epidermal growth factor receptormedicineAnimalsNuclear factor ƙBAnd catalaseChIP Chromatin immunoprecipitation;Protein kinase BNF-ƙB Nuclear factor kappa BSuperoxide DismutaseSuperoxide dismutase 1Superoxide dismutase 2Organic ChemistryGlutathioneASK1 Apoptosis signal-regulating kinase 1ATF2 activating transcription factor 2;030104 developmental biologyEndocrinologyEnzymeHsp Heat shock proteinlcsh:Biology (General)chemistrybiology.proteinSOD2 Mn-superoxide dismutaseMAPK mitogen activated protein kinaseNEM N-ethyl maleimide;Redox Biology
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Glycine-functionalized copper(ii) hydroxide nanoparticles with high intrinsic superoxide dismutase activity

2017

Superoxide dismutases (SOD) are a group of enzymes that catalyze the dismutation of superoxide (O2−) radicals into molecular oxygen (O2) and H2O2 as a first line of defense against oxidative stress. Here, we show that glycine-functionalized copper(II) hydroxide nanoparticles (Gly-Cu(OH)2 NPs) are functional SOD mimics, whereas bulk Cu(OH)2 is insoluble in water and catalytically inactive. In contrast, Gly-Cu(OH)2 NPs form water-dispersible mesocrystals with a SOD-like activity that is larger than that of their natural CuZn enzyme counterpart. Based on this finding, we devised an application where Gly-Cu(OH)2 NPs were incorporated into cigarette filters. Cigarette smoke contains high concent…

RadicalInorganic chemistryGlycine02 engineering and technology010402 general chemistrymedicine.disease_cause01 natural sciencesSuperoxide dismutasechemistry.chemical_compoundSmokeHydroxidesmedicineHumansGeneral Materials ScienceReactive nitrogen specieschemistry.chemical_classificationCopper(II) hydroxideReactive oxygen speciesbiologySuperoxide DismutaseSuperoxideHydrogen PeroxideTobacco Products021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical scienceschemistryA549 Cellsbiology.proteinNanoparticlesHydroxideReactive Oxygen Species0210 nano-technologyCopperOxidative stressNanoscale
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Unveiling the reaction mechanism of novel copper N-alkylated tetra-azacyclophanes with outstanding superoxide dismutase activity.

2020

Quantum chemical and multiscale calculations reveal the mechanistic pathway of two superoxide dismutase mimetic N-alkylated tetra-azacyclophane copper complexes with remarkable activity. The arrangement of the binding site afforded by the bulky alkyl substituents and the coordinated water molecule as a proton source play key roles in the reaction mechanism.

Reaction mechanismAlkylationStereochemistrychemistry.chemical_elementAlkylationMolecular Dynamics SimulationCrystallography X-RayCatalysisSuperoxide dismutaseCoordination ComplexesEthers CyclicMaterials ChemistryMoleculeHumansBinding siteAlkylchemistry.chemical_classificationbiologySuperoxide DismutaseMetals and AlloysGeneral Chemistrybiology.organism_classificationCopperSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryCeramics and Compositesbiology.proteinTetraQuantum Theorylipids (amino acids peptides and proteins)CopperChemical communications (Cambridge, England)
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Chemiluminescence response of ß-glucan stimulated leukocytes isolated from different tissues and peritoneal cavity of Dicentrarchus labrax

2003

Abstract The respiratory burst of leukocytes isolated from sea bass ( Dicentrarchus labrax ) pronephros, peritoneal cavity (P.C.), spleen and blood, was measured by a chemiluminescence (CL) assay after stimulation with β-glucan. The CL response by P.C. and pronephros leukocytes was significantly higher than that expressed by a similar number of cells separated from spleen and blood. This probably reflects the observation that the proportion of macrophages and neutrophils was highest in the populations of leukocytes from peritoneal cavity and pronephros. Comparative observations showed a higher degree of yeast phagocytosis by leukocytes taken from peritoneal cavity than the pronephros. Moreo…

Respiratory burstChemiluminescenceNeutrophilsPhagocytosisSettore BIO/05 - ZoologiaSpleenSaccharomyces cerevisiaeTeleosteiAquatic ScienceOuabainSuperoxide dismutasePeritoneal cavityPhagocytosismedicineAnimalsEnvironmental ChemistryGlucansPeritoneal CavitybiologyD. labraxGeneral MedicinePronephrosRespiratory burstmedicine.anatomical_structureBiochemistryMyeloperoxidaseLuminescent MeasurementsMicroscopy Electron Scanningbiology.proteinBassIndicators and ReagentsLuminolReactive Oxygen Speciesmedicine.drug
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Resuscitation with room air instead of 100% oxygen prevents oxidative stress in moderately asphyxiated term neonates.

2001

Background. Traditionally, asphyxiated newborn infants have been ventilated using 100% oxygen. However, a recent multinational trial has shown that the use of room air was just as efficient as pure oxygen in securing the survival of severely asphyxiated newborn infants. Oxidative stress markers in moderately asphyxiated term newborn infants resuscitated with either 100% oxygen or room air have been studied for the first time in this work. Methods. Eligible term neonates with perinatal asphyxia were randomly resuscitated with either room air or 100% oxygen. The clinical parameters recorded were those of the Apgar score at 1, 5, and 10 minutes, the time of onset of the first cry, and the tim…

ResuscitationRespiratory TherapyResuscitationmedicine.disease_causeSeverity of Illness IndexSuperoxide dismutaseRespirationmedicineHumansAsphyxiaAsphyxia Neonatorumbiologybusiness.industryAirInfant NewbornOxygen Inhalation TherapyOxidative StressTreatment OutcomeAnesthesiaPediatrics Perinatology and Child HealthBreathingbiology.proteinRoom air distributionApgar ScoreApgar scoremedicine.symptombusinessOxidative stress
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Oxidative stress in asphyxiated term infants resuscitated with 100% oxygen

2003

Although room air is adequate for resuscitating asphyxiated newborn infants, guidelines recommend using 100% oxygen. Hyperoxemia, as has been noted in animal studies, could cause delayed breathing, increased oxygen consumption, and disordered cerebral circulation. In addition, 100% oxygen has caused prolonged oxidation of blood glutathione in neonates. In this study, 51 asphyxiated neonates born at term were randomly assigned to resuscitation with room air (RAR) and 55 to resuscitation with 100% oxygen (OxR). The goal was to learn whether using oxygen for resuscitation triggers oxidative stress. Critical criteria were the Apgar score, the time of the first cry, and sustained respiration. Si…

ResuscitationResuscitationGlutathione reductasemedicine.disease_causechemistry.chemical_compoundDouble-Blind MethodmedicineHumansAcidosisAsphyxiachemistry.chemical_classificationAsphyxia NeonatorumGlutathione DisulfideSuperoxide Dismutasebusiness.industryGlutathione peroxidaseInfant NewbornOxygen Inhalation TherapyObstetrics and GynecologyApneaHyperoxemiaGeneral MedicineGlutathioneCarbon DioxideFetal BloodGlutathioneOxygenOxidative StressGlutathione ReductasechemistryAnesthesiaPediatrics Perinatology and Child HealthBreathingApgar ScoreRoom air distributionApgar scoremedicine.symptombusinessOxidative stressThe Journal of Pediatrics
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A new vicious cycle involving glutamate excitotoxicity, oxidative stress and mitochondrial dynamics

2011

Glutamate excitotoxicity leads to fragmented mitochondria in neurodegenerative diseases, mediated by nitric oxide and S-nitrosylation of dynamin-related protein 1, a mitochondrial outer membrane fission protein. Optic atrophy gene 1 (OPA1) is an inner membrane protein important for mitochondrial fusion. Autosomal dominant optic atrophy (ADOA), caused by mutations in OPA1, is a neurodegenerative disease affecting mainly retinal ganglion cells (RGCs). Here, we showed that OPA1 deficiency in an ADOA model influences N-methyl-D-aspartate (NMDA) receptor expression, which is involved in glutamate excitotoxicity and oxidative stress. Opa1enu/+mice show a slow progressive loss of RGCs, activation …

Retinal Ganglion CellsCancer ResearchReceptor expressionExcitotoxicityApoptosisNeurodegenerativeMitochondrionEyemedicine.disease_causeGTP PhosphohydrolasesMice0302 clinical medicineReceptorsoxidative stressPhosphorylationbcl-2-Associated X Protein0303 health sciencesbiologyGlutamate receptorMitochondriaUp-RegulationCell biologymitochondrial fusionAutosomal DominantOriginal Articlebcl-Associated Death ProteinMitochondrial fissionN-Methyl-D-AspartateBiotechnologymitochondrial fragmentationOncology and CarcinogenesisImmunologybcl-X ProteinSOD2Glutamic AcidReceptors N-Methyl-D-AspartateNMDA receptorsCell Line03 medical and health sciencesCellular and Molecular NeuroscienceBcl-2-associated X proteinOptic Atrophy Autosomal DominantmedicineAnimalsEye Disease and Disorders of Vision030304 developmental biologySuperoxide DismutaseNeurosciencesCell BiologyMolecular biologyeye diseasesOxidative StressOptic AtrophyMutationbiology.proteinOPA1 mutationBiochemistry and Cell Biologysense organsglutamate excitotoxicity030217 neurology & neurosurgeryCell Death & Disease
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Altered antioxidant-oxidant status in the aqueous humor and peripheral blood of patients with retinitis pigmentosa.

2013

Retinitis Pigmentosa is a common form of hereditary retinal degeneration constituting the largest Mendelian genetic cause of blindness in the developed world. It has been widely suggested that oxidative stress possibly contributes to its pathogenesis. We measured the levels of total antioxidant capacity, free nitrotyrosine, thiobarbituric acid reactive substances (TBARS) formation, extracellular superoxide dismutase (SOD3) activity, protein, metabolites of the nitric oxide/cyclic GMP pathway, heme oxygenase-I and inducible nitric oxide synthase expression in aqueous humor or/and peripheral blood from fifty-six patients with retinitis pigmentosa and sixty subjects without systemic or ocular …

Retinal degenerationAdultMalePathologymedicine.medical_specialtygenetic structuresSOD3lcsh:MedicineGene ExpressionPharmacologymedicine.disease_causeNitric OxideAntioxidantsNitric oxideAqueous Humorchemistry.chemical_compoundRetinitis pigmentosaTBARSmedicineCluster AnalysisHumanslcsh:ScienceCyclic GMPMultidisciplinarybiologySuperoxide DismutaseNitrotyrosinelcsh:RMiddle Agedmedicine.diseaseOxidantseye diseasesNitric oxide synthasechemistryCase-Control Studiesbiology.proteinLeukocytes MononuclearMetabolomelcsh:QFemalesense organsOxidative stressBiomarkersHeme Oxygenase-1Retinitis PigmentosaResearch ArticlePloS one
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Study of enzymatic activity in human neuroblastoma cells SH-SY5Y exposed to zearalenone's derivates and beauvericin.

2021

Abstract Beauvericin (BEA), α-zearalenol (α-ZEL) and β-zearalenol (β-ZEL), are produced by several Fusarium species that contaminate cereal grains. These mycotoxins can cause cytotoxicity and neurotoxicity in various cell lines and they are also capable of produce oxidative stress at molecular level. However, mammalian cells are equipped with a protective endogenous antioxidant system formed by no-enzymatic antioxidant and enzymatic protective systems such as glutathione peroxidase (GPx), glutathione S-transferase (GST), catalase (CAT) and superoxide dismutase (SOD). The aim of this study was evaluating the effects of α-ZEL, β-ZEL and BEA, on enzymatic GPx, GST, CAT and SOD activity in huma…

SH-SY5YAntioxidantmedicine.medical_treatmentToxicologymedicine.disease_causeSuperoxide dismutase03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyCell Line TumorDepsipeptidesmedicineHumans030304 developmental biologyEnzyme AssaysGlutathione Transferasechemistry.chemical_classification0303 health sciencesGlutathione PeroxidasebiologySuperoxide DismutaseGlutathione peroxidase04 agricultural and veterinary sciencesGeneral MedicineGlutathioneMycotoxinsCatalase040401 food scienceMolecular biologyBeauvericinchemistryPeroxidasesCatalasebiology.proteinZeranolOxidative stressFood ScienceFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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Expression of the ALS-causing variant hSOD1G93A leads to an impaired integrity and altered regulation of claudin-5 expression in an in vitro blood–sp…

2015

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive paralysis due to the loss of primary and secondary motor neurons. Mutations in the Cu/Zn-superoxide dismutase (SOD1) gene are associated with familial ALS and to date numerous hypotheses for ALS pathology exist including impairment of the blood–spinal cord barrier. In transgenic mice carrying mutated SOD1 genes, a disrupted blood–spinal cord barrier as well as decreased levels of tight junction (TJ) proteins ZO-1, occludin, and claudin-5 were detected. Here, we examined TJ protein levels and barrier function of primary blood–spinal cord barrier endothelial cells of presymptomatic hSOD1G93…

SOD1FOXO1Mice TransgenicBiologyOccludinCell LineMiceGene expressionAnimalsClaudin-5ClaudinProtein kinase BBarrier functionCells CulturedTight Junction ProteinsTight junctionSuperoxide DismutaseAmyotrophic Lateral SclerosisEndothelial CellsCell biologyDisease Models AnimalNeurologyGene Expression RegulationSpinal CordImmunologyOriginal ArticleNeurology (clinical)Cardiology and Cardiovascular MedicineSignal Transduction
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