Search results for "aldehyde dehydrogenase"

showing 10 items of 46 documents

Breast cancer cell lines contain functional cancer stem cells with metastatic capacity and a distinct molecular signature.

2009

Abstract Tumors may be initiated and maintained by a cellular subcomponent that displays stem cell properties. We have used the expression of aldehyde dehydrogenase as assessed by the ALDEFLUOR assay to isolate and characterize cancer stem cell (CSC) populations in 33 cell lines derived from normal and malignant mammary tissue. Twenty-three of the 33 cell lines contained an ALDEFLUOR-positive population that displayed stem cell properties in vitro and in NOD/SCID xenografts. Gene expression profiling identified a 413-gene CSC profile that included genes known to play a role in stem cell function, as well as genes such as CXCR1/IL-8RA not previously known to play such a role. Recombinant int…

Cancer ResearchPathologymedicine.medical_specialtyCellular differentiation[SDV.CAN]Life Sciences [q-bio]/CancerBreast Neoplasms[SDV.BC]Life Sciences [q-bio]/Cellular BiologyMice SCIDBiologyStem cell markerArticleCell LineReceptors Interleukin-8AMetastasisMice03 medical and health sciences0302 clinical medicineMice Inbred NODCancer stem cellCell Line TumorBiomarkers TumormedicineAnimalsHomeostasisHumansBreastRNA MessengerRNA NeoplasmNeoplasm MetastasisOligonucleotide Array Sequence Analysis030304 developmental biologySettore MED/04 - Patologia Generale0303 health sciencesReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingStem CellsCancerAldehyde DehydrogenaseFlow Cytometrymedicine.disease3. Good healthOncologyCell culture030220 oncology & carcinogenesisCancer researchFemaleStem cellImmortalised cell lineAldefluor breast cancer cell
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Number of nitrate groups determines reactivity and potency of organic nitrates: a proof of concept study in ALDH-2−/− mice

2007

Background and purpose: Mitochondrial aldehyde dehydrogenase (ALDH-2) has been shown to provide a pathway for bioactivation of organic nitrates and to be prone to desensitization in response to highly potent, but not to less potent, nitrates. We therefore sought to support the hypothesis that bioactivation by ALDH-2 critically depends on the number of nitrate groups within the nitrovasodilator. Experimental approach: Nitrates with one (PEMN), two (PEDN; GDN), three (PETriN; glyceryl trinitrate, GTN) and four (pentaerithrityl tetranitrate, PETN) nitrate groups were investigated. Vasodilatory potency was measured in isometric tension studies using isolated aortic segments of wild type (WT) an…

Pharmacologychemistry.chemical_classificationbiologyAldehyde dehydrogenasePentaerythritol tetranitrateDehydrogenaseNitric oxidechemistry.chemical_compoundEnzymeBiochemistrychemistrymedicinebiology.proteinStructure–activity relationshipPotencyNitrovasodilatormedicine.drugBritish Journal of Pharmacology
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Wine yeast sirtuins and Gcn5p control aging and metabolism in a natural growth medium.

2012

Grape juice fermentation by wine yeast is an interesting model to understand aging under conditions closer to those in nature. Grape juice is rich in sugars and, unlike laboratory conditions, the limiting factor for yeast growth is nitrogen. We tested the effect of deleting sirtuins and several acetyltransferases to find that the role of many of these proteins during grape juice fermentation is the opposite to that under standard laboratory aging conditions using synthetic complete media. For instance, . SIR2 deletion extends maximum chronological lifespan in wine yeasts grown under laboratory conditions, but shortens it in winemaking. Deletions of sirtuin . HST2 and acetyltransferase . GCN…

AgingSaccharomyces cerevisiae ProteinsNitrogenSaccharomyces cerevisiaeWineSaccharomyces cerevisiaeSirtuin 2AutophagySilent Information Regulator Proteins Saccharomyces cerevisiaeWinemakingAcetic AcidHistone AcetyltransferasesFermentation in winemakingWinebiologyfood and beveragesAldehyde Dehydrogenasebiology.organism_classificationYeastCulture MediaYeast in winemakingBiochemistrySirtuinFermentationbiology.proteinFermentationGene DeletionDevelopmental BiologyMechanisms of ageing and development
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EnzymesIn Vitro as indicators for pesticides: An examination

1992

Pesticides—a serious problem especially for drinking water quality—frequently are potent inhibitors of enzymes in their target organisms. As the established chemical analyses of pesticides are time-consuming, complicated, and expensive, so-called screening methods are urgently needed. For this purpose the sensitivity of 13 different enzymes was tested in vitro by inhibiting their kinetic rates and/or substrate conversions by 16 pesticides (herbicides and fungicides). Because of the stabilization and resulting low sensitivity of enzymes commercially available—especially in test kits—it was necessary to vary the test conditions and to develop special methods for detecting enzymatic inhibition…

chemistry.chemical_classificationbiologyChemistryHealth Toxicology and MutagenesisAldehyde dehydrogenasePesticidePesticide pollutionToxicologyIn vitroFungicideEnzymeBiochemistryEnzyme inhibitorToxicitybiology.proteinWater Science and TechnologyEnvironmental Toxicology & Water Quality
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Monitoring White Blood Cell Mitochondrial Aldehyde Dehydrogenase Activity: Implications for Nitrate Therapy in Humans

2009

Recent animal data suggest that reduced lipoic acid (LA) prevents oxidative inhibition of the nitrate bioactivating enzyme, the mitochondrial aldehyde dehydrogenase (ALDH-2), and that pentaerythritol tetranitrate (PETN) does not induce nitrate tolerance because of its intrinsic antioxidative properties, thereby preserving ALDH-2 activity. We sought to determine whether ALDH-2 activity in circulating white blood cells (WBCs) can be used to monitor nitrate tolerance and whether LA can prevent nitroglycerin tachyphylaxis in humans. Eight healthy male volunteers received, in randomized order, a single dose of glyceryl trinitrate (GTN; 0.8 mg), PETN (80 mg), or GTN plus LA (600 mg) orally. GTN (…

MaleMyocardial IschemiaAldehyde dehydrogenasePentaerythritol tetranitrateVasodilationTachyphylaxisPharmacologymedicine.disease_causeMitochondria Heartchemistry.chemical_compoundAnimal dataWhite blood cellLeukocytesmedicineAnimalsHumansRats WistarPharmacologyNitratesbiologyAldehyde DehydrogenaseRatsEnzyme ActivationVasodilationLipoic acidmedicine.anatomical_structurechemistrybiology.proteinMolecular MedicineOxidative stresscirculatory and respiratory physiologyJournal of Pharmacology and Experimental Therapeutics
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Nitroglycerin-induced endothelial dysfunction and tolerance involve adverse phosphorylation and S-glutathionylation of endothelial nitric oxide synth…

2011

Continuous administration of nitroglycerin (GTN) causes tolerance and endothelial dysfunction by inducing reactive oxygen species (ROS) production from various enzymatic sources, such as mitochondria, NADPH oxidase, and an uncoupled endothelial nitric oxide synthase (eNOS). In the present study, we tested the effects of type 1 angiotensin (AT(1))-receptor blockade with telmisartan on GTN-induced endothelial dysfunction in particular on eNOS phosphorylation and S-glutathionylation sites and the eNOS cofactor synthesizing enzyme GTP-cyclohydrolase I.Wistar rats were treated with telmisartan (2.7 or 8 mg/kg per day PO for 10 days) and with GTN (50 mg/kg per day SC for 3 days). Aortic eNOS phos…

MaleNitric Oxide Synthase Type IIIPhysiologyVasodilator AgentsPharmacologyBenzoatesCell LineNitroglycerinmedicineAnimalsHumansTelmisartanEnzyme InhibitorsPhosphorylationRats WistarS-GlutathionylationEndothelial dysfunctionGTP CyclohydrolaseBeneficial effectsNitroglycerinPharmacologyAngiotensin II receptor type 1Dose-Response Relationship DrugEndothelial nitric oxide synthaseChemistryEndothelial CellsDrug ToleranceAldehyde Dehydrogenasemedicine.diseaseGlutathioneMitochondriaRatsVasodilationOxidative StressTetrahydrofolate DehydrogenaseMolecular MedicinePhosphorylationBenzimidazolesEndothelium VascularTelmisartanReactive Oxygen SpeciesAngiotensin II Type 1 Receptor BlockersProtein Processing Post-Translationalmedicine.drugVascular Pharmacology
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Manganese superoxide dismutase and aldehyde dehydrogenase deficiency increase mitochondrial oxidative stress and aggravate age-dependent vascular dys…

2008

AimsImbalance between pro- and antioxidant species (e.g. during aging) plays a crucial role for vascular function and is associated with oxidative gene regulation and modification. Vascular aging is associated with progressive deterioration of vascular homeostasis leading to reduced relaxation, hypertrophy, and a higher risk of thrombotic events. These effects can be explained by a reduction in free bioavailable nitric oxide that is inactivated by an age-dependent increase in superoxide formation. In the present study, mitochondria as a source of reactive oxygen species (ROS) and the contribution of manganese superoxide dismutase (MnSOD, SOD-2) and aldehyde dehydrogenase (ALDH-2) were inves…

Mitochondrial ROSMaleAgingPhysiologyVasodilator AgentsMitochondrionVascular dysfunctionmedicine.disease_causeMitochondria HeartMuscle Smooth Vascularchemistry.chemical_compoundMiceEndothelial dysfunctionAortachemistry.chemical_classificationMice KnockoutbiologySuperoxideAldehyde Dehydrogenase MitochondrialAge FactorsVasodilationBiochemistryCardiology and Cardiovascular MedicineMitochondrial aldehyde dehydrogenasemedicine.medical_specialty8-oxodGOxidative phosphorylationDNA MitochondrialSuperoxide dismutaseManganese superoxide dismutaseddc:570Physiology (medical)Internal medicinemedicineAnimalsReactive oxygen speciesDose-Response Relationship DrugSuperoxide DismutaseMitochondrial oxidative stressOriginal ArticlesAldehyde Dehydrogenasemedicine.diseaseMice Inbred C57BLOxidative StressEndocrinologychemistrybiology.proteinEndothelium VascularReactive Oxygen SpeciesOxidative stressDNA DamageCardiovascular research
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Mitochondrial oxidative stress and nitrate tolerance – comparison of nitroglycerin and pentaerithrityl tetranitrate in Mn-SOD+/- mice

2006

Abstract Background Chronic therapy with nitroglycerin (GTN) results in a rapid development of nitrate tolerance which is associated with an increased production of reactive oxygen species (ROS). According to recent studies, mitochondrial ROS formation and oxidative inactivation of the organic nitrate bioactivating enzyme mitochondrial aldehyde dehydrogenase (ALDH-2) play an important role for the development of nitrate and cross-tolerance. Methods Tolerance was induced by infusion of wild type (WT) and heterozygous manganese superoxide dismutase mice (Mn-SOD+/-) with ethanolic solution of GTN (12.5 μg/min/kg for 4 d). For comparison, the tolerance-free pentaerithrityl tetranitrate (PETN, 1…

Mitochondrial ROSMaleHeterozygotelcsh:Diseases of the circulatory (Cardiovascular) systemVasodilator AgentsAldehyde dehydrogenaseOxidative phosphorylationMitochondrionPharmacologyIn Vitro Techniquesmedicine.disease_causeDrug Administration ScheduleMitochondria HeartCell LineSuperoxide dismutaseMiceNitroglycerinmedicineAnimalsHumansPentaerythritol TetranitrateRNA MessengerRats WistarHeart metabolismAortachemistry.chemical_classificationReactive oxygen speciesbiologybusiness.industrySuperoxide DismutaseAldehyde Dehydrogenase MitochondrialBilirubinDrug ToleranceFree Radical ScavengersAldehyde DehydrogenaseAcetylcholineRatsVasodilationOxidative Stresschemistrylcsh:RC666-701Anesthesiabiology.proteinCardiology and Cardiovascular MedicinebusinessReactive Oxygen SpeciesOxidative stressHeme Oxygenase-1Research ArticleBMC Cardiovascular Disorders
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Understanding the release and metabolism of aroma compounds using micro-volume saliva samples by ex vivo approaches

2018

International audience; This study investigated the behaviour of key aroma compounds in the presence of human saliva (200 mu L) from different individuals (n = 3) submitted or not to centrifugation (whole vs clarified saliva). HS-GC results showed that human saliva strongly decreased the release of carbonyl compounds (aldehydes and ketones). This effect was dependent on i) the structure of the aroma compounds and ii) the saliva composition. Whole saliva exerted a higher effect than clarified saliva on aroma compounds. Moreover, this effect was individual-dependent and related to the total protein content and the total antioxidant capacity of saliva. HS-SPME and LLE-GC/MS analyses revealed t…

Salivaenzymessalivary proteinsperceptionin-vivoGas Chromatography-Mass SpectrometryAnalytical Chemistry0404 agricultural biotechnologyfluids and secretionsstomatognathic systemaldehyde dehydrogenaseHumansCentrifugationwineAromaTotal proteinAldehydessalivaChromatographybiologyretronasal aromaaroma compoundsbeta-lactoglobulinChemistryenzymatic conversionfood and beverages04 agricultural and veterinary sciencesGeneral MedicineMetabolismKetonesbiology.organism_classification040401 food scienceodorant concentrationstomatognathic diseasesartificial salivacarbonyl compoundsSaliva compositionOdorcompositionOdorantstotal antioxidant capacitymouth[SDV.AEN]Life Sciences [q-bio]/Food and NutritionEx vivoFood Science
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Drug-metabolizing enzymes in the skin of man, rat, and pig.

2007

The mammalian skin has long been considered to be poor in drug metabolism. However, many reports clearly show that most drug metabolizing enzymes also occur in the mammalian skin albeit at relatively low specific activities. This review summarizes the current state of knowledge on drug metabolizing enzymes in the skin of human, rat, and pig, the latter, because it is often taken as a model for human skin on grounds of anatomical similarities. However only little is known about drug metabolizing enzymes in pig skin. Interestingly, some cytochromes P450 (CYP) have been observed in the rat skin which are not expressed in the rat liver, such as CYP 2B12 and CYP2D4. As far as investigated most d…

Drugcytochrome P450Swinemedia_common.quotation_subjectMetaboliteAldehyde dehydrogenaseHuman skinEpoxide hydrolaseEsterasechemistry.chemical_compoundOrgan Culture TechniquesCytochrome P-450 Enzyme SystemSpecies SpecificityGlycosyltransferaseAnimalsHumansPharmacology (medical)ratGeneral Pharmacology Toxicology and PharmaceuticsFlavin monooxygenaseCells Culturedmedia_commonSkinchemistry.chemical_classificationquinone reductase [NAD(P)H]biologyintegumentary systemAlcohol dehydrogenaseSulfotransferaseCytochrome P450Aldehyde dehydrogenaseMetabolic Detoxication Phase IIEnzymesRatsGlutathione S-transferaseIsoenzymesEnzymechemistryBiochemistryPharmaceutical PreparationsN-acetyltransferasebiology.proteinMetabolic Detoxication Phase IPig skin drug metabolismDrug metabolismUDP-glucuronosyltransferaseHuman
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