Search results for "Reductase"

showing 10 items of 798 documents

Carbamazepine, cadmium chloride and polybrominated diphenyl ether-47, synergistically modulate the expression of antioxidants and cell cycle biomarke…

2019

Abstract A wide range of contaminants, industrial by-products, plastics, and pharmaceutics belonging to various categories, have been found in sea water. Although these compounds are detected at concentrations that might be considered as sub-lethal, under certain conditions they could act synergistically producing unexpected effects in term of toxicity or perturbation of biochemical markers leading to standard pathway. In this study, the Sparus aurata fibroblast cell line SAF-1, was exposed to increasing concentrations of carbamazepine (CBZ), polybrominated diphenyl ether 47 (BDE-47) and cadmium chloride (CdCl2) until 72 h, to evaluate the cytotoxicity and the expression of genes related to…

0106 biological sciencesAntioxidantmedicine.medical_treatmentAquatic ScienceCadmium chlorideOceanographymedicine.disease_cause010603 evolutionary biology01 natural sciencesCell LinePolybrominated diphenyl-etherchemistry.chemical_compoundCadmium ChlorideSettore AGR/20 - ZoocoltureSettore BIO/10 - BiochimicaHalogenated Diphenyl EthersmedicineAnimalsoxidative stressSparus aurata fibroblastSettore BIO/06 - Anatomia Comparata E CitologiaCytotoxicity010604 marine biology & hydrobiologyCell CycleDiphenyl etherbiomarkersBiomarkerGeneral MedicineCell cycleCadmium chloridePollutionEnzyme ActivationOxidative StressCarbamazepineGene Expression RegulationchemistryBiochemistry:5 - Ciencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citología [CDU]Cell culturecarbamazepineToxicityOxidative streEnergy MetabolismOxidoreductasespolybrominated diphenyl-etherBiomarkersWater Pollutants ChemicalOxidative stressMarine Environmental Research
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Iron acquisition from Fe-pyoverdine by Arabidopsis thaliana.

2007

Taking into account the strong iron competition in the rhizosphere and the high affinity of pyoverdines for Fe(III), these molecules are expected to interfere with the iron nutrition of plants, as they do with rhizospheric microbes. The impact of Fe-pyoverdine on iron content of Arabidopsis thaliana was compared with that of Fe-EDTA. Iron chelated to pyoverdine was incorporated in a more efficient way than when chelated to EDTA, leading to increased plant growth of the wild type. A transgenic line of A. thaliana overexpressing ferritin showed a higher iron content than the wild type when supplemented with Fe-EDTA but a lower iron content when supplemented with Fe-pyoverdine despite its inc…

0106 biological sciencesChlorophyll[ SDV.BV ] Life Sciences [q-bio]/Vegetal BiologyFMN ReductasePhysiologyIronArabidopsisReductasePseudomonas fluorescens01 natural sciencesPlant Roots03 medical and health scienceschemistry.chemical_compoundFMN reductaseArabidopsis thaliana[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyChelationRELATION PLANTE-MICROORGANISMECation Transport ProteinsEdetic Acid030304 developmental biology0303 health sciencesPyoverdinebiologyArabidopsis ProteinsACLWild typeARABIDOPSIS THALIANAGeneral Medicinebiology.organism_classificationPlants Genetically ModifiedFerritinchemistryBiochemistryChlorophyllFerritinsbiology.proteinAgronomy and Crop ScienceOligopeptides010606 plant biology & botany
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Deletion of GLX3 in Candida albicans affects temperature tolerance, biofilm formation and virulence.

2018

Candida albicans is a predominant cause of fungal infections in mucosal tissues as well as life-threatening bloodstream infections in immunocompromised patients. Within the human body, C. albicans is mostly embedded in biofilms, which provides increased resistance to antifungal drugs. The glyoxalase Glx3 is an abundant proteomic component of the biofilm extracellular matrix. Here, we document phenotypic studies of a glx3Δ null mutant concerning its role in biofilm formation, filamentation, antifungal drug resistance, cell wall integrity and virulence. First, consistent with its function as glyoxalase, the glx3 null mutant showed impaired growth on media containing glycerol as the carbon sou…

0106 biological sciencesHot TemperatureMutantAntifungal drugHyphaeVirulence01 natural sciencesApplied Microbiology and BiotechnologyMicrobiologyMicrobiology03 medical and health sciencesFilamentationCell Wall010608 biotechnologyCandida albicansAnimalsCandida albicans030304 developmental biology0303 health sciencesMice Inbred BALB CbiologyVirulenceBiofilmWild typeCandidiasisGeneral Medicinebiology.organism_classificationAldehyde OxidoreductasesSurvival AnalysisCorpus albicansDisease Models AnimalBiofilmsGene DeletionHeat-Shock ResponseFEMS yeast research
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Can Indirect Herbicide Exposure Modify the Response of the Colorado Potato Beetle to an Organophosphate Insecticide?

2018

AbstractOrganisms live in complex multivariate environments. In agroecosystems, this complexity is often human-induced as pest individuals can be exposed to many xenobiotics simultaneously. Predicting the effects of multiple stressors can be problematic, as two or more stressors can have interactive effects. Our objective was to investigate whether indirect glyphosate-based herbicide (GBH) exposure of the host plant has interactive effects in combination with an insecticide (azinphos-methyl) on an invasive pest Colorado potato beetle (Leptinotarsa decemlineata Say). We tested the effects of GBH and insecticide on the survival, insecticide target genes expression (acetylcholinesterase genes)…

0106 biological sciencesInsecticidesCarbamateColoradomedicine.medical_treatmentGlutathione reductase010501 environmental sciencesPharmacology010603 evolutionary biology01 natural sciencesSuperoxide dismutasechemistry.chemical_compoundmedicineAnimalsGlutathione TransferaseSolanum tuberosum0105 earth and related environmental scienceschemistry.chemical_classificationEcologybiologyHerbicidesGlutathione peroxidaseOrganophosphateColorado potato beetlefood and beveragesGeneral MedicineGlutathionebiology.organism_classificationOrganophosphatesColeopterachemistryInsect Sciencebiology.proteinAzinphos-methylJournal of Economic Entomology
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Nitric Oxide in Plants: Production and Cross-talk with Ca2+ Signaling

2008

International audience; Nitric oxide (NO) is a diatomic gas that performs crucial functions in a wide array of physiological processes in animals. The past several years have revealed much about its roles in plants. It is well established that NO is synthesized from nitrite by nitrate reductase (NR) and via chemical pathways. There is increasing evidence for the occurrence of an alternative pathway in which NO production is catalysed from L-arginine by a so far non-identified enzyme. Contradictory results have been reported regarding the respective involvement of these enzymes in specific physiological conditions. Although much remains to be proved, we assume that these inconsistencies can …

0106 biological sciencesMAPK/ERK pathwayArabidopsisPlant ScienceCalcium-Transporting ATPasesBiologyNitrate reductaseArginine01 natural sciencesPlant Physiological PhenomenaNitrate ReductaseNitric oxide03 medical and health scienceschemistry.chemical_compoundNitrateProtein kinasesNitrilesAnimals[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyNitriteMolecular BiologyNitritesPlant Physiological Phenomena030304 developmental biologyMammals0303 health sciencesKinasefungiNitric oxidechemistryBiochemistrySecond messenger systemCitrullineCalciumCryptogeinNitric Oxide SynthaseGenome Plant010606 plant biology & botanySignal Transduction
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Kinetic studies on protoporphyrinogen oxidase inhibition by diphenyl ether herbicides

1991

Diphenyl ethers (DPEs) and related herbicides are powerful inhibitors of protoporphyrinogen oxidase, an enzyme involved in the biosynthesis of haems and chlorophylls. The inhibition kinetics of protoporphyrinogen oxidase of various origins by four DPEs, (methyl)-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (acifluorfen and its methyl ester, acifluorfen-methyl), methyl-5-[2-chloro-4-(trifluoromethyl) phenoxy]-2-chlorobenzoate (LS 820340) and methyl-5-[2-chloro-5-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (RH 5348), were studied. The inhibitions of the enzymes from maize (Zea mays) mitochondrial and etiochloroplastic membranes and mouse liver mitochondrial membranes were com…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]Carboxylic acidMitochondria LiverEtherSaccharomyces cerevisiaeAcifluorfen01 natural sciencesBiochemistryMitochondrial ProteinsMiceStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEPhenolsAnimalsProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesTrifluoromethylFlavoproteinsHerbicidesDiphenyl etherIntracellular MembranesCell BiologyPlantsMitochondriaProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryProtoporphyrinogen oxidaseOxidoreductasesEthersResearch Article010606 plant biology & botanyBiochemical Journal
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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Synthesis and properties of a photoaffinity labeling reagent for protoporphyrinogen oxidases, the target enzymes of diphenyl ether herbicides

1994

A diazoketone 3 has been synthesized in two steps from acifluorfen 1, a diphenyl ether herbicide. Like the parent compound 1, the diazoketone 3 is toxic to plant cells and inhibits protoporphyrinogen oxidase, the molecular target of diphenyl ether herbicides. On photolysis of 3 in methanol, the generated carbene mainly undergoes the Wolff rearrangement to a ketene which further adds methanol, but many other products are observed. A tritiated derivative of 3 has been prepared which is suitable for photoaffinity labeling experiments.

0106 biological sciencesOxidoreductases Acting on CH-CH Group Donors[SDV]Life Sciences [q-bio]Clinical BiochemistryPharmaceutical ScienceKeteneAcifluorfen01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundDrug DiscoveryOrganic chemistryProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesPhotolysisPhotoaffinity labelingMolecular StructureBIOCHIMIEHerbicidesOrganic ChemistryDiphenyl etherWolff rearrangementAffinity Labels[SDV] Life Sciences [q-bio]chemistryTOXICOLOGIEReagentMolecular MedicineProtoporphyrinogen oxidaseIndicators and ReagentsMethanolSoybeansOxidoreductases010606 plant biology & botany
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NADPH Oxidase-Mediated Reactive Oxygen Species Production: Subcellular Localization and Reassessment of Its Role in Plant Defense

2009

International audience; Chemiluminescence detection of reactive oxygen species (ROS) triggered in tobacco BY-2 cells by the fungal elicitor cryptogein was previously demonstrated to be abolished in cells transformed with an antisense construct of the plasma membrane NADPH oxidase, NtrbohD. Here, using electron microscopy, it has been confirmed that the first hydrogen peroxide production occurring a few minutes after challenge of tobacco cells with cryptogein is plasma membrane located and NtrbohD mediated. Furthermore, the presence of NtrbohD in detergent-resistant membrane fractions could be associated with the presence of NtrbohD-mediated hydrogen peroxide patches along the plasma membran…

0106 biological sciencesPhysiologyBiology01 natural sciencesDNA AntisenseFungal Proteins03 medical and health sciencesMicroscopy Electron TransmissionNtrbohDTobaccoGene expressionNADPHPlant defense against herbivory[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCells CulturedPlant Proteins030304 developmental biologychemistry.chemical_classification0303 health sciencesReactive oxygen speciesOxidase testNADPH oxidaseHydrogen PeroxideGeneral MedicinePlants Genetically ModifiedSubcellular localizationElicitorPlant LeavesEnzymechemistryBiochemistrybiology.proteinREACTIVE OXYGEN SPECIES (ROS)OxidoreductasesReactive Oxygen SpeciesAgronomy and Crop Science010606 plant biology & botanyMolecular Plant-Microbe Interactions®
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Glutathione deficiency of the Arabidopsis mutant pad2-1 affects oxidative stress-related events, defense gene expression and hypersensitive response

2011

L'article original est publié par The American Society of Plant Biologists; International audience; The Arabidopsis (Arabidopsis thaliana) phytoalexin-deficient mutant pad2-1 displays enhanced susceptibility to a broad range of pathogens and herbivorous insects that correlates with deficiencies in the production of camalexin, indole glucosinolates, and salicylic acid (SA). The pad2-1 mutation is localized in the GLUTAMATE-CYSTEINE LIGASE (GCL) gene encoding the first enzyme of glutathione biosynthesis. While pad2-1 glutathione deficiency is not caused by a decrease in GCL transcripts, analysis of GCL protein level revealed that pad2-1 plants contained only 48% of the wild-type protein amoun…

0106 biological sciencesPhysiologyMutantGlutathione reductaseArabidopsisOligosaccharidesPlant Science01 natural scienceschemistry.chemical_compoundAnti-Infective AgentsGene Expression Regulation PlantCamalexinArabidopsis thaliana0303 health sciencesGlutathioneBiochemistryHost-Pathogen InteractionsDisease SusceptibilitySalicylic AcidOxidation-ReductionSignal TransductionHypersensitive responsePhytophthoradisease resistanceBiologyNitric Oxiderespiratory burst oxidase homolog d[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesStress PhysiologicalGeneticsPlants Interacting with Other Organismsglutathione reductase030304 developmental biologyPlant DiseasesArabidopsis ProteinsCell MembraneWild typeGlutathioneHydrogen Peroxidebiology.organism_classificationMolecular biologyPlant LeavesOxidative StresschemistryMutationglutathione-s-transferaseIsochorismate synthasebiology.proteinglutamate-cysteine ligaseReactive Oxygen Species010606 plant biology & botany
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