Search results for " Group D"

showing 10 items of 31 documents

Polyamine Oxidase 5 loss-of-function mutations in Arabidopsis thaliana trigger metabolic and transcriptional reprogramming and promote salt stress to…

2017

The family of polyamine oxidases (PAO) in Arabidopsis (AtPAO1-5) mediates polyamine (PA) back-conversion, which reverses the PA biosynthetic pathway from spermine, and its structural isomer thermospermine (tSpm), into spermidine and then putrescine. Here, we have studied the involvement of PA back-conversion in Arabidopsis salinity tolerance. AtPAO5 is the Arabidopsis PAO gene member most transcriptionally induced by salt stress. Two independent loss-of-function mutants (atpao5-2 and atpao5-3) were found to exhibit constitutively higher tSpm levels, with associated increased salt tolerance. Using global transcriptional and metabolomic analyses, the underlying mechanisms were studied. Stimul…

0106 biological sciences0301 basic medicineTranscription GeneticArabidopsis thalianaPhysiologyArabidopsisSperminePlant ScienceSodium Chloride01 natural scienceschemistry.chemical_compoundGene Expression Regulation PlantLoss of Function MutationArabidopsisPolyaminesMetabolitesArabidopsis thalianaPoliaminesAbscisic acidPrincipal Component AnalysisbiologyAgricultural SciencesSalt ToleranceMetabòlitsmetabolomicsPhenotypeBiochemistryMultigene FamilyMetabolomeCitric Acid CycleSalsCyclopentanes03 medical and health sciencesStress PhysiologicalOxylipinsRNA MessengerIonssalt toleranceArabidopsis ProteinsGene Expression ProfilingSodiumHydrogen PeroxideAgriculture Forestry and Fisheriesbiology.organism_classificationSpermidineGene Ontology030104 developmental biologychemistrythermosperminePutrescineSpermineSaltsOxidoreductases Acting on CH-NH2 Group DonorsTranscriptomejasmonatesPolyaminePolyamine oxidaseAbscisic Acid010606 plant biology & botany
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Ability of Kocuria varians LTH 1540 To Degrade Putrescine: Identification and Characterization of a Novel Amine Oxidase.

2015

This work describes the identification and characterization of an amine oxidase from Kocuria varians LTH 1540 (syn. Micrococcus varians) primarily acting on putrescine. Data from MALDI-TOF MS/MS and the identification of Δ(1)-pyrroline as degradation product from putrescine indicate that the enzyme is a flavin-dependent putrescine oxidase (PuO). Properties of partially purified enzyme have been determined. The enzyme oxidizes diamines, putrescine and cadaverine, and, to a lesser extent, polyamines, such as spermidine, but not monoamines. The kinetic constants (Km and Vmax) for the two major substrates were 94 ± 10 μM and 2.3 ± 0.1 μmol/min·mg for putrescine and 75 ± 5 μM and 0.15 ± 0.02 μmo…

chemistry.chemical_classificationAmine oxidaseCadaverineOxidoreductases Acting on CH-NH Group DonorsChromatographyKocuria variansGeneral ChemistryBiologyHydrogen-Ion ConcentrationAmine oxidase inhibitorsMicrococcusSpermidinePutrescine oxidasechemistry.chemical_compoundKineticsEnzymeBiodegradation EnvironmentalchemistryBacterial ProteinsEnzyme StabilityPutrescinePutrescineGeneral Agricultural and Biological SciencesJournal of agricultural and food chemistry
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Association of vitamin D serum levels and its common genetic determinants, with severity of liver fibrosis in genotype 1 chronic hepatitis C patients.

2013

Background and aims: Lower 25-Hydroxyvitamin D (25[OH]D) serum lev- els have been associated with the severity of liver fibrosis in genotype 1 chronic hepatitis C patients (G1CHC). In addition, a recent genome-wide study identified genetic variants (rs12785878, near dehydrocholesterol reduc- tase, DHCR7; rs10741657, near CYP2R1; and rs7041, near vitamin D binding protein, GC) affecting 25(OH)D serum levels in healthy populations. We aimed to assess the association between vitamin D serum levels and its genetic determinants, with the severity of liver fibrosis. Material and methods: Two hundred sixty patients with biopsy-proven G1CHC were consecutively evaluated. The 25(OH)D serum levels wer…

VitaminAdultLiver CirrhosisMaleSerummedicine.medical_specialtyOxidoreductases Acting on CH-CH Group DonorsGenotypeHepatitis C virusSingle-nucleotide polymorphismHepacivirusBiologyReductasemedicine.disease_causeGastroenterologychemistry.chemical_compoundFibrosisVirologyInternal medicineGenotypemedicineVitamin D and neurologyHumansVitamin DCytochrome P450 Family 2Chromatography High Pressure LiquidHCV VITAMIN D DHCR7Settore MED/12 - GastroenterologiaPolymorphism GeneticHepatologyVitamin D-Binding ProteinHepatitis C ChronicMiddle Agedmedicine.diseaseInfectious DiseaseschemistryImmunologyCholestanetriol 26-MonooxygenaseFemaleSteatosisJournal of viral hepatitis
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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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Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1—evidence for direct and …

2009

Heme oxygenase-1 (HO-1) is highly protective in various pathophysiological states such as cardiovascular and neurodegenerative diseases. HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS). It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells. RONS scavenging activities of biliverdin versus bilirubin were assessed by different RONS generating systems and detection techniques. We also silenced the biliverdin reductase (BVR) or HO-1 gene in cultured primary human endothelial cells (HUVECs) and measured the effect on RONS formation upon stimulation with lipopolys…

LipopolysaccharidesOxidoreductases Acting on CH-CH Group DonorsUmbilical VeinsXanthine OxidaseNeutrophilsBilirubinNitrosationModels BiologicalAntioxidantschemistry.chemical_compoundPeroxynitrous AcidLeukocytespolycyclic compoundsHumansGene SilencingMolecular BiologyHemeReactive nitrogen speciesRespiratory BurstBiliverdinAngiotensin IIBiliverdineBiliverdin reductaseEndothelial CellsBilirubinFree Radical ScavengersAngiotensin IIMitochondriaEndothelial stem cellHeme oxygenasechemistryBiochemistryCytoprotectionGene Knockdown TechniquesTyrosineReactive Oxygen SpeciesCardiology and Cardiovascular MedicineHeme Oxygenase-1Journal of Molecular and Cellular Cardiology
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Rev-Erb modulates retinal visual processing and behavioral responses to light

2016

International audience; The circadian clock is thought to adjust retinal sensitivity to ambient light levels, yet the involvement of specific clock genes is poorly understood. We explored the potential role of the nuclear receptor subfamily 1, group D, member 1 (REV-ERB; or NR1D1) in this respect. In light-evoked behavioral tests, compared with wild-type littermates, Rev-Erb(-/-) mice showed enhanced negative masking at low light levels (0.1 lx). Rev-Erb(-/-) mouse retinas displayed significantly higher numbers of intrinsically photosensitive retinal ganglion cells (ipRGCs; 62% more compared with wild-type) and more intense melanopsin immunostaining of individual ipRGCs. In agreement with a…

0301 basic medicineRetinal Ganglion CellsLight[SDV]Life Sciences [q-bio]Circadian clockelectroretinogramBiochemistrychemistry.chemical_compound0302 clinical medicinecircadian clockskin and connective tissue diseasesComputingMilieux_MISCELLANEOUSMice KnockoutipRGCsBehavior AnimalphotoreceptorsorganizationCircadian Rhythmmedicine.anatomical_structurerodtranscriptionBiotechnologyPhotopic visionMelanopsinnegative maskingrat retinaBiologyRetina03 medical and health sciences[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyCircadian ClocksGeneticsmedicineAnimalsCircadian rhythmScotopic visionmelanopsin-knockout miceMolecular BiologymouseRetinaIntrinsically photosensitive retinal ganglion cellsRod OpsinsRetinalganglion-cellsbody regionsmammalian retina030104 developmental biologychemistryNuclear Receptor Subfamily 1 Group D Member 1sense organsNeuroscience030217 neurology & neurosurgeryPhotic Stimulation[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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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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Multiple activation pathways of benzene leading to products with varying genotoxic characteristics.

1989

Abstract Benzene and 13 potential metabolites were investigated for genotoxicity in Salmonella typhimurium and V79 Chinese hamster cells. In the presence of NADPH-fortified hepatic postmitochondrial fraction (S9 mix), benzene reverted his- S. typhimurium strains. The effect was strongest in strain TA1535. Among the potential metabolites, only the trans-1,2-dihydrodiol, in the presence of S9 mix, and the diol epoxides, in the presence and absence of S9 mix, proved mutagenic in this strain. The anti-diol epoxide was more potent than the syn-diastereomer. Both enantiomers of the anti-diastereomer showed similar activities. S9 mix did not appreciably affect the mutagenicity of the anti-diol epo…

Oxidoreductases Acting on CH-CH Group DonorsHealth Toxicology and MutagenesisEpoxideSister chromatid exchangeGene mutationIn Vitro Techniquesmedicine.disease_causechemistry.chemical_compoundmedicinepolycyclic compoundsAnimalsBiotransformationCatecholHydroquinoneMutagenicity TestsPublic Health Environmental and Occupational HealthBenzeneQuinoneAlcohol OxidoreductaseschemistryBiochemistryMicronucleus testOxidoreductasesGenotoxicityResearch ArticleMutagensEnvironmental Health Perspectives
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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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A novel mutation of the DHCR7 gene in a sicilian compound heterozygote with Smith-Lemli-Opitz Syndrome

2005

Introduction: Smith-Lemli-Opitz syndrome (SLOS) is an autosomal recessive disorder of cholesterol biosynthesis, resulting from deficient 7-dehydrocholesterol reductase (3β-hydroxysterol Δ7-reductase) activity, the enzyme responsible for conversion of 7-dehydrocholesterol to cholesterol. SLOS is most common among people of European descent, with a reported incidence of 1 per 20 000–60 000 newborns, depending on the diagnostic criteria and the reference population. More than 80 different mutations have been identified in several hundred patients. In Italy, SLOS appears to be a rare condition, probably because of underdiagnosis. Method: We analyzed by direct sequencing the 7-dehydrocholesterol…

Malecongenital hereditary and neonatal diseases and abnormalitiesHeterozygoteOxidoreductases Acting on CH-CH Group DonorsMutation MissenseBiologyReductaseCompound heterozygosityExonmedicineMissense mutationHumansGeneSicilyGeneticsnutritional and metabolic diseasesInfantGeneral Medicinemedicine.diseaseHuman geneticsPedigreeSmith-Lemli-Opitz SyndromeOxidoreductases Acting on CH-CH Group DonorSmith–Lemli–Opitz syndromeMutation (genetic algorithm)Human
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