Search results for "ethanol metabolism"

showing 7 items of 17 documents

Local salsolinol modulates dopamine extracellular levels from rat nucleus accumbens: shell/core differences.

2008

Salsolinol (SAL), a condensation product of dopamine and acetaldehyde that appears in the rat and human brain after ethanol ingestion, has been largely implicated in the aetiology of alcoholism. Although the behavioural consequences of systemic or intracerebral SAL administrations have been described, the neurochemical effects of pharmacologically relevant doses of SAL and other tetrahydroisoquinolines (THIQs) in the brain areas involved in alcohol addiction are practically unknown. To gain an insight into this topic, male Wistar rats were stereotaxically implanted with one concentric microdialysis probe in either the shell or the core of the nucleus accumbens (NAc). Treatments involved loc…

MaleMicrodialysisDopamineMicrodialysisDown-RegulationAcetaldehydePharmacologyNucleus accumbensSynaptic TransmissionNucleus AccumbensCellular and Molecular Neurosciencechemistry.chemical_compoundNeurochemicalAlcohol-Induced Disorders Nervous SystemRewardDopamineparasitic diseasesBasal gangliamedicineAnimalsEthanol metabolismRats WistarNeurotransmitterChromatography High Pressure LiquidDose-Response Relationship DrugEthanolChemistryExtracellular FluidCell BiologyIsoquinolinesRatsUp-RegulationAlcoholismCatecholamineNeurosciencemedicine.drugNeurochemistry international
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Catalase-independent early-gene expression in rat brain following acute ethanol exposure

2004

Early-gene expression evoked by acute ethanol treatment was studied in rat brain by quantitative immunocytochemistry, with reference to ethanol metabolism by the enzyme catalase. Colocalization with mu-opioid receptor (MOR) sites was also examined. Ethanol challenges [1, 2.5, and 4 g/kg intraperitoneally (i.p.)] evoked dose-dependent increases in c-Fos expression in several brain regions, but overlap with MOR-rich sites was only partial. Strong inhibition of brain catalase activity (ca. 60%) with 3-amino-1,2,4-triazole (AT, 1 g/kg i.p.) did not alter ethanol-induced c-Fos nor Krox-24 expression in any of the brain regions analyzed. This evidence demonstrates that catalase-mediated metabolis…

MaleNervous systemmedicine.medical_specialtyCentral nervous systemReceptors Opioid muGene ExpressionCell Countc-FosRats Sprague-DawleyInternal medicinemedicineAnimalsEnzyme InhibitorsEthanol metabolismMolecular BiologyAmitroleBrain ChemistryEthanolbiologyGeneral NeuroscienceBrainCentral Nervous System DepressantsColocalizationCatalaseImmunohistochemistryRatsmedicine.anatomical_structureEndocrinologyCatalasebiology.proteinNeurology (clinical)μ-opioid receptorProto-Oncogene Proteins c-fosImmediate early geneDevelopmental BiologyBrain Research
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Brain metabolism of ethanol and alcoholism: an update.

2007

It has long been suggested that some of the neuropharmacological, neurochemical and behavioural effects of ethanol are mediated by its first metabolite, acetaldehyde. In spite of the well documented psychoactivity of acetaldehyde, the precise role of this compound in alcohol abuse remains a matter of intense debate among scientists devoted to the study of alcoholism. Very frequently, the main drawback has been related to the presence of adequate levels of acetaldehyde or its derivatives inside the brain after ethanol ingestion. Since penetration into the central nervous system from blood of peripherically derived acetaldehyde is very low due to the high aldehyde dehydrogenase activity at th…

MetaboliteClinical BiochemistryCentral nervous systemAcetaldehydePharmacologychemistry.chemical_compoundNeurochemicalmedicineAnimalsHumansEthanol metabolismCellular localizationPharmacologyEthanolEthanolDopaminergicAcetaldehydeBrainCentral Nervous System DepressantsCytochrome P-450 CYP2E1CatalaseAlcoholismmedicine.anatomical_structurechemistryEnzyme InductionOxidation-ReductionCurrent drug metabolism
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Ethanol cycle in an ethanologenic bacterium

2002

AbstractA novel redox cycle is suggested, performing interconversion between acetaldehyde and ethanol in aerobically growing ethanologenic bacterium Zymomonas mobilis. It is formed by the two alcohol dehydrogenase (ADH) isoenzymes simultaneously catalyzing opposite reactions. ADH I is catalyzing acetaldehyde reduction. The local reactant ratio at its active site probably is shifted towards ethanol synthesis due to direct channeling of NADH from glycolysis. ADH II is oxidizing ethanol. The net result of the cycle operation is NADH shuttling from glycolysis to the membrane respiratory chain, and ensuring flexible distribution of reducing equivalents between the ADH reaction and respiration.

NADH channelingBiophysicsRespiratory chainBiochemistryZymomonas mobilischemistry.chemical_compoundStructural BiologyGeneticsGlycolysisEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolEthanolbiologyFutile cycleRespirationZymomonas mobilisAlcohol dehydrogenaseAcetaldehydeCell BiologyNADbiology.organism_classificationAerobiosisIsoenzymeschemistryBiochemistryFutile cycleChemostatbiology.proteinOxidation-Reductionhormones hormone substitutes and hormone antagonistsFEBS Letters
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Two-carbon metabolites, polyphenols and vitamins influence yeast chronological life span in winemaking conditions

2012

Abstract Background Viability in a non dividing state is referred to as chronological life span (CLS). Most grape juice fermentation happens when Saccharomyces cerevisiae yeast cells have stopped dividing; therefore, CLS is an important factor toward winemaking success. Results We have studied both the physical and chemical determinants influencing yeast CLS. Low pH and heat shorten the maximum wine yeast life span, while hyperosmotic shock extends it. Ethanol plays an important negative role in aging under winemaking conditions, but additional metabolites produced by fermentative metabolism, such as acetaldehyde and acetate, have also a strong impact on longevity. Grape polyphenols quercet…

NiacinamideAgingSaccharomyces cerevisiaelcsh:QR1-502BioengineeringWineAcetaldehydeSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyNiacinlcsh:Microbiologychemistry.chemical_compoundEthanol metabolismNicotinamideWinemakingFermentation in winemakingMicrobial ViabilityEthanolResearchAcetaldehydefood and beveragesPolyphenolsVitaminsAldehyde DehydrogenaseHydrogen-Ion Concentrationbiology.organism_classificationYeastYeastCarbonYeast in winemakingchemistryBiochemistryResveratrolFermentationFermentationBiotechnologyMicrobial Cell Factories
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Arginase activity is a useful marker of nitrogen limitation during alcoholic fermentations.

2003

Nitrogen deficiency in musts is one of the causes of sluggish or stuck fermentations. In this work we propose that arginase activity determination can be useful for detecting nitrogen starvation early in vinification. CAR1 and YGP1 genes are not specifically induced under conditions of nitrogen starvation. However, a significant increase in the enzymatic activity of arginase, the product of the CAR1 gene, is detected in vinifications carried out with musts containing limiting amounts of nitrogen. Moreover, on adding ammonia to a nitrogen-deficient vinification, even at late stages, this enzymatic activity is repressed, and growth rate is restored simultaneously. We also investigate the role…

Saccharomyces cerevisiae ProteinsTranscription GeneticNitrogenWineSaccharomyces cerevisiaeEthanol fermentationBiologyApplied Microbiology and BiotechnologyMicrobiologyFungal ProteinsAmmoniachemistry.chemical_compoundAmmoniaGene Expression Regulation FungalEthanol metabolismNitrogen cycleEcology Evolution Behavior and SystematicsGlycoproteinsEthanolArginaseEthanolNitrogen deficiencyMembrane ProteinsArginaseGlucoseBiochemistrychemistryFermentationFood MicrobiologyFermentationSystematic and applied microbiology
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Kinetic modelling of the Zymomonas mobilis Entner-Doudoroff pathway: insights into control and functionality.

2013

Zymomonas mobilis, an ethanol-producing bacterium, possesses the Entner-Doudoroff (E-D) pathway, pyruvate decarboxylase and two alcohol dehydrogenase isoenzymes for the fermentative production of ethanol and carbon dioxide from glucose. Using available kinetic parameters, we have developed a kinetic model that incorporates the enzymic reactions of the E-D pathway, both alcohol dehydrogenases, transport reactions and reactions related to ATP metabolism. After optimizing the reaction parameters within likely physiological limits, the resulting kinetic model was capable of simulating glycolysis in vivo and in cell-free extracts with good agreement with the fluxes and steady-state intermediate …

ZymomonasbiologyEthanolATPaseAlcohol DehydrogenaseGene Expression Regulation BacterialCarbon Dioxidebiology.organism_classificationMicrobiologyZymomonas mobilisModels BiologicalMetabolic engineeringAdenosine TriphosphateGlucoseBiochemistrybiology.proteinGlycolysisComputer SimulationEthanol metabolismEntner–Doudoroff pathwayPyruvate DecarboxylasePyruvate decarboxylaseMetabolic Networks and PathwaysAlcohol dehydrogenaseMicrobiology (Reading, England)
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