Search results for "OXIDASE"

showing 10 items of 927 documents

Inhibition of the myosin light chain kinase prevents hypoxia-induced blood-brain barrier disruption

2007

Increased mortality after stroke is associated with development of brain edema. The aim of the present study was to examine the contribution of endothelial myosin light chain (MLC) phosphorylation to hypoxia-induced blood-brain barrier (BBB) opening. Measurements of trans-endothelial electrical resistance (TEER) were performed to analyse BBB integrity in an in vitro co-culture model (bovine brain microvascular endothelial cells (BEC) and rat astrocytes). Brain fluid content was analysed in rats after stroke induction using a two-vein occlusion model. Dihydroethidium was used to monitor intracellular generation of reactive oxygen species (ROS) in BEC. MLC phosphorylation was detected using i…

Myosin light-chain kinaseNADPH oxidasebiologyEndotheliumBlood–brain barriermedicine.diseaseBiochemistryCell biologyCerebral edemaCellular and Molecular Neurosciencechemistry.chemical_compoundmedicine.anatomical_structurechemistryNAD(P)H oxidaseExtracellular fluidApocyninmedicinebiology.proteinNeuroscienceJournal of Neurochemistry
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β-Aminobutyric Acid Primes an NADPH Oxidase–Dependent Reactive Oxygen Species Production During Grapevine-Triggered Immunity

2010

International audience; The molecular mechanisms underlying the process of priming are poorly understood. In the present study, we investigated the early signaling events triggered by β-aminobutyric acid (BABA), a well-known priming-mediated plant resistance inducer. Our results indicate that, in contrast to oligogalacturonides (OG), BABA does not elicit typical defense-related early signaling events nor defense-gene expression in grapevine. However, in OG-elicited cells pretreated with BABA, production of reactive oxygen species (ROS) and expression of the respiratory-burst oxidase homolog RbohD gene were primed. In response to the causal agent of downy mildew Plasmopara viticola, a strong…

NADPH OXIDASE-DEPENDENTPhytophthora0106 biological sciencesACIDE β-AMINOBUTYRIQUEPhysiologyArabidopsisBiology01 natural sciencesAminobutyric acid03 medical and health sciencesImmunityTobaccoGene expression[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyVitisDNA Primers030304 developmental biologychemistry.chemical_classification0303 health sciencesReactive oxygen speciesOxidase testNADPH oxidaseReverse Transcriptase Polymerase Chain ReactionAminobutyratesNADPH OxidasesHydrogen PeroxideGeneral MedicineKineticsEnzymeBiochemistrychemistryBABAbiology.proteinCalciumSignal transductionReactive Oxygen SpeciesAgronomy and Crop ScienceRESISTANCE010606 plant biology & botanyMolecular Plant-Microbe Interactions®
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An

2020

Intracellular acid stress inhibits plant growth by unknown mechanisms and it occurs in acidic soils and as consequence of other stresses. In order to identify mechanisms of acid toxicity, we screened activation-tagging lines of Arabidopsis thaliana for tolerance to intracellular acidification induced by organic acids. A dominant mutant, sbt4.13-1D, was isolated twice and shown to over-express subtilase SBT4.13, a protease secreted into endoplasmic reticulum. Activity measurements and immuno-detection indicate that the mutant contains less plasma membrane H+-ATPase (PMA) than wild type, explaining the small size, electrical depolarization and decreased cytosolic pH of the mutant but not orga…

NADPH oxidaseArabidopsis ProteinsArabidopsisNADPH OxidasesGerminationROSArticleOxidative StressProton-Translocating ATPasesMutationorganic acidsactivation-taggingH+-ATPaseSubtilisinsProtonsInternational journal of molecular sciences
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Short‐term e‐cigarette vapor exposure causes vascular oxidative stress and dysfunction ‐ evidence for a close connection to brain damage and a key ro…

2020

NADPH oxidasebiologyChemistryBrain damagemedicine.disease_causeBiochemistryCell biologyConnection (mathematics)Geneticsmedicinebiology.proteinmedicine.symptomMolecular BiologyOxidative stressNOxBiotechnologyThe FASEB Journal
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Phytochemical indicaxanthin suppresses 7-ketocholesterol-induced THP-1 cell apoptosis by preventing cytosolic Ca++ increase and oxidative stress

2013

7-Ketocholesterol (7-KC)-induced apoptosis of macrophages is considered a key event in the development of human atheromas. In the present study, the effect of indicaxanthin (Ind), a bioactive pigment from cactus pear fruit, on 7-KC-induced apoptosis of human monocyte/macrophage THP-1 cells was investigated. A pathophysiological condition was simulated by using amounts of 7-KC that can be reached in human atheromatous plaque. Ind was assayed within a micromolar concentration range, consistent with its plasma level after dietary supplementation with cactus pear fruit. Pro-apoptotic effects of 7-KC were assessed by cell cycle arrest, exposure of phosphatidylserine at the plasma membrane, varia…

NADPH oxidase-4MacrophageSettore BIO/10 - BiochimicaApoptosiIndicaxanthin7-Ketocholesterol
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Biomolecular conjugation inside synthetic polymer nanopores via glycoprotein-lectin interactions

2011

We demonstrate the supramolecular bioconjugation of concanavalin A (Con A) protein with glycoenzyme horseradish peroxidase (HRP) inside single nanopores, fabricated in heavy ion tracked polymer membranes. Firstly, the HRP-enzyme was covalently immobilized on the inner wall of the pores using carbodiimide coupling chemistry. The immobilized HRP-enzyme molecules bear sugar (mannose) groups available for the binding of Con A protein. Secondly, the bioconjugation of Con A on the pore wall was achieved through its biospecific interactions with the mannose residues of the HRP enzyme. The immobilization of biomolecules inside the nanopore leads to the reduction of the available area for ionic tran…

NanometresSynthetic membraneTransport equationNanoporesInformation processingRectification propertiesCylinders (shapes)Materials TestingConcanavalin AGeneral Materials ScienceFunctional polymersConical nanoporeschemistry.chemical_classificationChemistryBlocking effectElectric rectifiersComputer simulationEnzymesData processingNanoporeEnzyme moleculesFunctional polymersMolecular imprintingPorosityBio-molecularInner wallsMolecular imprintingSupramolecular chemistryNanotechnologyHorseradish peroxidaseIonic transportsNanocapsulesBio-conjugationMoleculeParticle SizeAqueous solutionsGlycoproteinsBiomoleculesBioconjugationBiomoleculeNanostructuresModel simulationChemical engineeringModels ChemicalPolymer membraneConductance stateFISICA APLICADABiospecific interactionSynthetic polymersSugarsSupramolecular chemistryPore wallCarbodiimide-coupling chemistry
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Redox signaling in acute pancreatitis

2015

Acute pancreatitis is an inflammatory process of the pancreatic gland that eventually may lead to a severe systemic inflammatory response. A key event in pancreatic damage is the intracellular activation of NF-κB and zymogens, involving also calcium, cathepsins, pH disorders, autophagy, and cell death, particularly necrosis. This review focuses on the new role of redox signaling in acute pancreatitis. Oxidative stress and redox status are involved in the onset of acute pancreatitis and also in the development of the systemic inflammatory response, being glutathione depletion, xanthine oxidase activation, and thiol oxidation in proteins critical features of the disease in the pancreas. On th…

NecrosisGSH reduced glutathioneSTAT3 signal transducer and activator of transcription 3ERK extracellular signal-regulated kinasesClinical BiochemistryCCK cholecystokininTRAFs TNF receptor associated factorsReview ArticleIκB kinasePharmacologymedicine.disease_causeBiochemistrySHP small heterodimer partnerSTIM1 stromal interaction molecule 1chemistry.chemical_compoundHATs histone acetyltransferasesMedicineASK1GCL glutamate cysteine ligaseTNF-α tumor necrosis factor alphaIKK IκB kinaseNOS nitric oxide synthaseAcute inflammationHIF hypoxia inducible factorlcsh:QH301-705.5NF-κB nuclear factor kappa BDAMPs damage-associated molecular pattern moleculeslcsh:R5-920biologyGSSG oxidized glutathioneNF-kappa BNLRs nucleotide-binding oligomerization domain (NOD) like receptorsTRADD tumor necrosis factor receptor type 1-associated DEATH domain proteinTRPC3 transient receptor potential channel 3VEGF vascular endothelial growth factorGlutathioneTNFR tumor necrosis factor receptorHMGB1 high-mobility group Box 1 proteinIP3R inositol 145-trisphosphate receptor type 3VCAM-1 Vascular Cell adhesion protein 1Acute DiseaseJNK c-Jun N-terminal kinaseAcute pancreatitisTLRs toll-like receptorsmedicine.symptomlcsh:Medicine (General)Oxidation-ReductionAP-1 activator protein-1Signal TransductionmRNA messenger ribonucleic acidHMGB1ASC apoptosis-associated speck-like protein containing a carboxy-terminal CARDRNS reactive nitrogen speciesPTPs protein tyrosine phosphatasesROS reactive oxygen speciesNADH nicotinamide adenine dinucleotidepHe extracellular pHFAEE fatty acid ethyl estersAP acute pancreatitisHumansXanthine oxidaseCBP CREB-binding proteinRyR endoplasmic reticulum membrane ryanodine receptorsMDA malondialdehydeNO nitric oxideXO xanthine oxidaseASK1 apoptosis signal-regulating kinase-1business.industryOrganic ChemistryAutophagyNADPH nicotinamide adenine dinucleotide phosphateHDACs histone deacetylasesmedicine.diseaseCARS compensatory anti-inflammatory response syndromeXDH xanthine dehydrogenaseIL interleukinIκB inhibitor of kappa BAcute pancreatitisETC Electron transport chainPancreatitisMKPs MAPK phosphatasesSAP severe acute pancreatitischemistrylcsh:Biology (General)DTT dithiothreitolOxidative stressNAC N-acetyl cysteineImmunologybiology.proteinCalciumLysosomesReactive Oxygen SpeciesbusinessMAPK mitogen-activated protein kinaseOxidative stressERCP endoscopic retrograde cholangiopancreatographyRedox Biology
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Mechanism of Reaction of Melatonin with Human Myeloperoxidase

2001

Recently, it was suggested that melatonin (N-acetyl-5-methoxytryptamine) is oxidized by activated neutrophils in a reaction most probably involving myeloperoxidase (Biochem. Biophys. Res. Commun. (2000) 279, 657-662). Myeloperoxidase (MPO) is the most abundant protein of neutrophils and is involved in killing invading pathogens. To clarify if melatonin is a substrate of MPO, we investigated the oxidation of melatonin by its redox intermediates compounds I and II using transient-state spectral and kinetic measurements at 25 degrees C. Spectral and kinetic analysis revealed that both compound I and compound II oxidize melatonin via one-electron processes. The second-order rate constant measur…

NeutrophilsStereochemistryBiophysicsElectron donorIn Vitro TechniquesBiochemistryRedoxMedicinal chemistrySubstrate SpecificityElectron TransportSuperoxide dismutaseMelatoninchemistry.chemical_compoundReaction rate constantChloridesmedicineHumansMolecular BiologySodium cyanideMelatoninPeroxidasebiologyCyclohexanonesChemistryCell BiologyHydrogen-Ion ConcentrationKineticsSpectrophotometryMyeloperoxidasebiology.proteinFerricOxidation-Reductionmedicine.drugBiochemical and Biophysical Research Communications
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Diterpenoids from Tetraclinis articulata that Inhibit Various Human Leukocyte Functions

2003

Ten new compounds, eight of them pimarane derivatives (1-8), together with a menthane dimer (9) and a totarane diterpenoid (10), were isolated from the leaves and wood of Tetraclinis articulata. The structures of 1-10 were established by using spectroscopic techniques, including 2D NMR spectra. Pimaranes 1-5 were found to possess an unusual cis interannular union of the B and C rings, which, from a biogenetic perspective, could be derived from the hydration of a carbocation at C-8. Compounds 4-6 and a mixture of 7 and 11 modulated different human leukocyte functions at a concentration of 10 microM, mainly the degranulation process measured as myeloperoxidase release and, to a lesser extent,…

NeutrophilsStereochemistryMonoterpenePharmaceutical ScienceTetraclinisAnalytical Chemistryboatschemistry.chemical_compoundboats.ship_classDrug DiscoveryLeukocytesArticulataHumansPhenolsNuclear Magnetic Resonance BiomolecularPeroxidasePharmacologyPlants MedicinalMolecular StructurePancreatic ElastasebiologyChemistryOrganic ChemistryCupressaceaeStereoisomerismBiological activitybiology.organism_classificationWoodTerpenoidPlant LeavesMoroccoComplementary and alternative medicineLuminescent MeasurementsMolecular MedicineDiterpenesDiterpeneTwo-dimensional nuclear magnetic resonance spectroscopyJournal of Natural Products
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Competitive interaction of three peroxidizing herbicides with the binding of 3H acifluorfen to corn etioplast membranes

1990

AbstractThe specific binding of the herbicide acifluorfen 5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid to corn etioplast membranes is competitively inhibited by protoporphyrinogen IX, the substrate of protoporphyrinogen oxidase. Three other peroxidizing molecules, oxadiazon [5-ter-butyl-3-(2,4-dichloro-5-isopropoxyphenyl)-1,3,4-oxadiazol-2-one], LS 82556 [(S)3-N-(methylbenzyl)carbamoyl-5-propionyl-2,6-lutidine], and M&B 39279 [5-amino-4-cyano-1-(2,6-dichloro-4-trifluoromethylphenyl)pyrazol], also compete with acifluorfen for its binding site. The four herbicides thus bind to the same site, or to closely located sites, on the enzyme protoporphyrinogen oxidase.

Niacinamide0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistryBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyAcifluorfenBinding CompetitiveZea mays01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundEtioplastStructural BiologyDiphenyletherGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOxadiazoles0303 health sciencesBinding SitesTrifluoromethylHerbicidesCell MembraneCell BiologyPlantsBindingProtoporphyrinogen IXProtoporphyrinogen oxidaseEnzymeMembranechemistryDiuronNitrobenzoatesPyrazolesProtoporphyrinogen oxidaseHerbicideOxidoreductases010606 plant biology & botany
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