Search results for "xanthine"

showing 10 items of 139 documents

Redox regulation of E3 ubiquitin ligases and their role in skeletal muscle atrophy

2015

Muscle atrophy is linked to reactive oxygen species (ROS) production during hindlimb-unloading due, at least in part, to the activation of xanthine oxidase (XO). The major aim of our study was to determine the mechanism by which ROS cause muscle atrophy and its possible prevention by allopurinol, a well-known inhibitor of XO widely used in clinical practice, and indomethacin, a nonsteroidal anti-inflammatory drug. We studied the activation of p38 MAP Kinase and NF-?B pathways, and the expression of two E3 ubiquitin ligases involved in proteolysis, the Muscle atrophy F-Box (MAFb) and Muscle RING Finger-1 (MuRF-1). Male Wistar rats (3 mold) conditioned by 14 days of hindlimb unloading (n=18),…

Soleus musclemedicine.medical_specialtySkeletal muscleAllopurinolHindlimbBiologymedicine.disease_causemedicine.diseaseBiochemistryMuscle atrophychemistry.chemical_compoundmedicine.anatomical_structureEndocrinologyAtrophychemistryBiochemistryPhysiology (medical)Internal medicinemedicinemedicine.symptomXanthine oxidaseOxidative stressmedicine.drugFree Radical Biology and Medicine
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Complex formation of hypoxanthine and 6-mercaptopurine with Cd(II) ion

1984

Reaction of Cd(II) ion with hypoxanthine (H2 Y) and with 6-mercaptopurine (H2 MP) in dioxane-water (50%) leads to the formation of CdY·2H2O and Cd(HMP)2·2H2O, respectively. In methanolic medium Cd(II) and H2 MP give Cd(MP)·H2O. These compounds have been characterized by chemical analysis, IR spectra and thermogravimetric analysis. The stability constant of CdY complex at 25±0.1 °C and 1M ionic strength with NaClO4 in dioxane-water medium is log β=10.25±0.05.

Thermogravimetric analysisChemistryComplex formationInfrared spectroscopyGeneral ChemistryMercaptopurineIonchemistry.chemical_compoundStability constants of complexesIonic strengthmedicineHypoxanthinemedicine.drugNuclear chemistryMonatshefte f�r Chemie Chemical Monthly
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Dihydroquercetin (DHQ) induced HO-1 and NQO1 expression against oxidative stress through the Nrf2-dependent antioxidant pathway.

2013

Dihydroquercetin (DHQ) is a well-known antioxidant agent. In the present investigation, we reported for the first time that DHQ stimulates the expression of phase II detoxifying enzymes through the Nrf2-dependent signaling pathway. The IC50 values of DHQ for reduction of 2,2-diphenyl-1-picrylhydrazol (DPPH), reducing power assay, lipid peroxidation assay, and xanthine oxidase inhibition were 5.96, 4.31, 2.03, and 13.24 μM, respectively. DHQ possessed considerable protective activity from oxidative DNA damage. A luciferase reporter assay also demonstrated that DHQ-activated signaling resulted in the increased transcriptional activity of Nrf2 through binding to the ARE (antioxidant response e…

Transcriptional ActivationAntioxidantNF-E2-Related Factor 2medicine.medical_treatmentLarixmedicine.disease_causeAntioxidantsLipid peroxidationchemistry.chemical_compoundmedicineNAD(P)H Dehydrogenase (Quinone)HumansAntioxidant Response ElementsLuciferaseXanthine oxidaseProtein kinase BChemistryPlant ExtractsGeneral ChemistryHep G2 CellsMolecular biologyAntioxidant Response ElementsUp-RegulationOxidative StressBiochemistryQuercetinNAD+ kinaseGeneral Agricultural and Biological SciencesOxidative stressHeme Oxygenase-1Signal TransductionJournal of agricultural and food chemistry
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Induction of mitochondrial xanthine oxidase activity during apoptosis in the rat mammary gland

2006

Oxidative stress is an important signal for apoptosis to start. So far the mitochondrial respiratory chain has been considered as the major, if not the only, cause of such stress. Here we report that this is not the case. Xanthine oxidase, a O2(-) and H2O2 generating enzyme which is important in causing significant oxidative stress in the cytosol, is also present in the mitochondrial fraction of rat mammary gland. After weaning, during the involution of the mammary gland, massive apoptosis occurs. Mitochondrial xanthine oxidase activity increases and high mitochondrial H2O2 production takes place. Inhibition of xanthine oxidase activity by allopurinol, a specific inhibitor of xanthine oxida…

Xanthine OxidaseAllopurinolRespiratory chainAllopurinolApoptosisWeaningMitochondrionmedicine.disease_causeMitochondrial Proteinschemistry.chemical_compoundMammary Glands AnimalmedicineAnimalsInvolution (medicine)Enzyme InhibitorsXanthine oxidaseChemistryHydrogen PeroxideMitochondriaRatsCell biologyOxidative StressMitochondrial respiratory chainBiochemistryApoptosisOxidative stressmedicine.drugFrontiers in Bioscience
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Flavonols and flavan-3-ols as modulators of xanthine oxidase and manganese superoxide dismutase activity.

2014

Experiments were performed to assess the dose-dependent effects of quercetin, kaempferol, (+) catechin, and (-) epicatechin on superoxide radical production through the modulation of manganese superoxide dismutase and xanthine oxidase activities. The experiments were carried out at flavanoid concentrations ranging from 1 µM to 100 µM. This investigation highlighted that flavonols induced opposite effects on superoxide radical production at different doses, i.e. pro-oxidant at the highest concentration (100 µM) and anti-oxidant at the lowest concentration (1 µM). Similar behaviors were observed for xanthine oxidase with flavan-3ols. The diastereoisomer (the catechin) acted as a stronger radi…

Xanthine OxidaseAntioxidantInhibitorFlavonolsmedicine.medical_treatmentPro-oxidantSettore BIO/09 - FisiologiaSuperoxide dismutasechemistry.chemical_compoundFlavonolsFlavanDose responsemedicineXanthine oxidasechemistry.chemical_classificationFlavonoidsbiologyMolecular StructureSuperoxide DismutaseMedicine (all)Functional foodCatechinPro-oxidantStructure-Activity relationshipchemistryBiochemistrybiology.proteinFlavonoidSettore BIO/14 - FarmacologiaAntioxidantKaempferolFlavonolFood ScienceInternational journal of food sciences and nutrition
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Vascular oxidative stress, nitric oxide and atherosclerosis.

2014

In the vascular wall, reactive oxygen species (ROS) are produced by several enzyme systems including NADPH oxidase, xanthine oxidase, uncoupled endothelial nitric oxide synthase (eNOS) and the mitochondrial electron transport chain. On the other hand, the vasculature is protected by antioxidant enzyme systems, including superoxide dismutases, catalase, glutathione peroxidases and paraoxonases, which detoxify ROS. Cardiovascular risk factors such as hypercholesterolemia, hypertension, and diabetes mellitus enhance ROS generation, resulting in oxidative stress. This leads to oxidative modification of lipoproteins and phospholipids, mechanisms that contribute to atherogenesis. In addition, oxi…

Xanthine OxidaseAntioxidantNitric Oxide Synthase Type IIImedicine.medical_treatmentMice TransgenicOxidative phosphorylationNitric Oxide Synthase Type Imedicine.disease_causeNitric OxideCardiovascular SystemAntioxidantsNitric oxideSuperoxide dismutasechemistry.chemical_compoundMiceSuperoxidesmedicineAnimalsHumansXanthine oxidasechemistry.chemical_classificationReactive oxygen speciesGlutathione PeroxidaseNADPH oxidasebiologyAryldialkylphosphataseSuperoxide DismutaseNADPH OxidasesAtherosclerosisCatalaseMitochondriaOxidative StresschemistryBiochemistrybiology.proteinCardiology and Cardiovascular MedicineReactive Oxygen SpeciesOxidative stressAtherosclerosis
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Preparation of ferulic acid derivatives and evaluation of their xanthine oxidase inhibition activity.

2007

Several ferulic acid ethyl esters (3a-h) were synthesized under the Knoevengel reaction condition and they were further reduced to afford the respective allylic alcohol derivatives (4a-g). Some of them were evaluated for the xanthine oxidase (XO) inhibitory activity. Among them, 3h exhibited a significant inhibitory activity with an IC50 value of 1.35 x 10(-5) M, while the IC50 value of allopurinol used as the positive control was 1.49 x 10(-5) M. The study suggested that the higher acidity of the phenolic OH group in the ferulic acid derivatives might result in improved XO inhibitory activity.

Xanthine OxidaseMagnetic Resonance SpectroscopyCoumaric Acidsmedicine.drug_classAllopurinolPositive controlPlant ScienceIn Vitro TechniquesInhibitory postsynaptic potentialBiochemistryAnalytical ChemistryFerulic acidElectron Transportchemistry.chemical_compoundmedicineOrganic chemistryAnimalsEnzyme InhibitorsXanthine oxidaseXanthine oxidase inhibitorIC50ChemistryOrganic ChemistryEstersNuclear magnetic resonance spectroscopyRatsLiverBenzaldehydesIndicators and Reagentsmedicine.drugNatural product research
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Sildenafil protects epithelial cell through the inhibition of xanthine oxidase and the impairment of ROS production

2009

Recent reports suggest that xanthine oxidase (XO), a modified form of the native xanthine dehydrogenase enzyme, plays an important role in various forms of ischemic and vascular injuries, inflammatory diseases, and chronic heart failure. The XO inhibitors allopurinol and its oxidation product oxypurinol held considerable promises in the treatment of these conditions both in experimental animals and in human clinical trials. More recently, an endothelium-based protective effect of sildenafil, a well-known type-5 phosphodiesterase inhibitor, has been reported in preconditioning prior to ischemia/reperfusion in healthy human subjects. Based on the structural similarities between allopurinol an…

Xanthine OxidasePurinonesEndotheliumCell SurvivalSildenafilIschemiaAllopurinolPharmacologyBiochemistryPiperazinesSildenafil CitrateStructure-Activity Relationshipchemistry.chemical_compoundSettore BIO/10 - BiochimicaTumor Cells CulturedmedicineHumansSulfonesXanthine oxidaseNADPH oxidasebiologybusiness.industryEpithelial CellsGeneral Medicinemedicine.diseasemedicine.anatomical_structurechemistryBiochemistryPurinesCell cultureSettore BIO/14 - Farmacologiabiology.proteinReactive Oxygen SpeciesZaprinastbusinessXanthine oxidase ROS production oxidative stress inhibition sildenafil zaprinast human mammary epithelial cellsmedicine.drugFree Radical Research
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Xanthine oxidase catalyzes the oxidation of retinol.

2007

In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2-5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the recons…

Xanthine OxidaseReceptors Retinoic Acidchemistry.chemical_elementTretinoinHydroxylationLigandsCatalysisHydroxylationchemistry.chemical_compoundRetinoidsDrug DiscoveryHumansXanthine oxidasePurine metabolismVitamin APharmacologychemistry.chemical_classificationHypoxanthinebiologyEthanolRetinol-Binding Proteins CellularGeneral MedicineGlutathioneEnzyme assayOxygenRetinol-Binding ProteinsKineticsEnzymechemistryBiochemistryXanthine dehydrogenaseMolybdenumbiology.proteinXanthine oxidase retinol oxidation retinaldehyde oxidation retinoic acid biosynthesis cellular retinoid binding protein (CRBP) Cellular retinoic acid binding protein (CRABP) retinol binding protein (RBP)Journal of enzyme inhibition and medicinal chemistry
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Estrogen Inhibits Retinoic Acid Biosynthesis In Tumor Breast Epithelial Cell Lines

2008

Xanthine OxidaseRetinolCellular Retinol Binding Protein I (CRBPI)Xanthine DehydrogenaseSettore BIO/10 - BiochimicaRetinoic acid
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