Search results for "DASE"

showing 10 items of 1891 documents

Oxidative DNA damage and disturbance of antioxidant capacity by alternariol in Caco-2 cells

2015

Oxidative stress occurs as a consequence of an imbalance between the prooxidant/antioxidant systems, causing an increase of intracellular generation of reactive oxygen species. Alternariol (AOH), a mycotoxin produced by Alternaria sp. can alter the action of glutathione (GSH) and the enzymes involved in the redox system, causing damage to cellular macromolecules such as DNA. The aims of this work were to determine the induction of oxidative stress by the antioxidant defenses imbalance in relation to glutathione (GSH), glutathione reductase (GR), glutathione transferase (GST), glutathione peroxidase (GPx) levels and DNA damage in Caco-2 cells derived from adenocarcinoma human colon. Oxidativ…

Time FactorsAntioxidantDNA damagemedicine.medical_treatmentGlutathione reductaseAlternariolBiologyToxicologymedicine.disease_causeAntioxidantsLactoneschemistry.chemical_compoundmedicineHumansGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseDose-Response Relationship DrugGlutathione peroxidaseGeneral MedicineGlutathioneMycotoxinsGlutathioneComet assayOxidative StressGlutathione ReductaseBiochemistrychemistryComet AssayCaco-2 CellsOxidative stressDNA DamageToxicology Letters
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Gold Nanoparticles Supported on Nanoparticulate Ceria as a Powerful Agent against Intracellular Oxidative Stress

2012

Ceria-supported gold nanoparticles are prepared exhibiting peroxidase activity and acting as radical traps. Au/CeO2 shows a remarkable biocompatibility as demonstrated by measuring cellular viability, proliferation, and lack of apoptosis for two human cell lines (Hep3B and HeLa). The antioxidant activity of Au/CeO2 against reactive oxygen species (ROS) is demonstrated by studying the cellular behavior of Hep3B and HeLa in a model of cellular oxidative stress. It is determined that Au/CeO2 exhibits higher antioxidant activity than glutathione, the main cytosolic antioxidant compound, and its CeO2 carrier. Overall the result presented here shows the potential of implementing well-established …

Time FactorsAntioxidantMaterials scienceBiocompatibilityCell SurvivalPolymersPeroxidase activitymedicine.medical_treatmentMetal NanoparticlesApoptosisBiocompatible MaterialsIntracellular oxidative stressmedicine.disease_causeAntioxidantsCatalysisCell LineBiomaterialsHeLachemistry.chemical_compoundCeriaQUIMICA ORGANICAmedicineHumansNanotechnologyGold nanoparticlesGeneral Materials ScienceCell Proliferationchemistry.chemical_classificationReactive oxygen speciesbiologyGeneral ChemistryGlutathionebiology.organism_classificationOxidative StressNanomedicinePeroxidasesBiochemistrychemistryColloidal goldNanoparticlesGoldReactive Oxygen SpeciesIntracellularOxidative stressHeLa CellsBiotechnologySmall
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Alterations of Activities of Ribonucleases and Polyadenylate Polymerase in Synchronized Mouse L Cells

1977

The activities of the three known catabolic and the one anabolic polyadenylate enzymes have been determined in synchronized L5178y cells: endoribonuclease, exoribonuclease, 5'-nucleotidase and poly(A) polymerase (Mg2+-dependent). These four enzymes were found primarily in the nuclear fraction. The activity of poly(A) polymerase remains essentially constant during the transition from G1 to S phase. However, the poly(A) catabolic enzyme activities increase parallel with DNA synthesis; the endoribonuclease activity increases 4-fold during G1 to S phase, the exoribonuclease and the nucleotidase activities increasing 30-fold and 16-fold. During the S phase the poly(A)-degrading enzymes are far m…

Time FactorsEndoribonuclease activityEndoribonucleaseMitosisBiochemistryCell LineStructure-Activity RelationshipL CellsRibonucleasesExoribonucleaseNucleotidasePolyadenylatePolymerasechemistry.chemical_classificationbiologyDNA synthesisPolynucleotide AdenylyltransferaseNucleotidyltransferasesMolecular biologyMolecular WeightKineticsEnzymeBiochemistrychemistrybiology.proteinCell DivisionEuropean Journal of Biochemistry
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Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

2003

Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

Time FactorsLeupeptinsApoptosisRetinoblastoma ProteinAntioxidantsAmino Acid Chloromethyl KetonesMembrane Potentialschemistry.chemical_compoundSettore BIO/10 - BiochimicaMG132Caspase 8OsteosarcomaChemistryCaspase 3Cytochromes cFlow CytometryMitochondriaCysteine EndopeptidasesProto-Oncogene Proteins c-bcl-2CaspasesOsteosarcomamedicine.drugmusculoskeletal diseasesProteasome Endopeptidase ComplexCell SurvivalBlotting Westernbcl-X Proteinmacromolecular substancesTransfectionMultienzyme ComplexesCell Line Tumorparasitic diseasesmedicineHumansProtease InhibitorsneoplasmsMolecular BiologySaos-2 cellsDose-Response Relationship DrugCell Biologymedicine.diseaseAcetylcysteineApoptosis osteosarcoma proteasome inhibitorsMicroscopy FluorescenceApoptosisCancer researchProteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen Specieshuman activities
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Enzymatic, physicochemical, nutritional and phytochemical profile changes of apple (Golden Delicious L.) juice under supercritical carbon dioxide and…

2018

The impact of supercritical carbon dioxide (SCCD) (10-60 MPa/45 °C/30 min) and subsequent 10 weeks storage at 4 °C on polyphenol oxidase (PPO), peroxidase (POD) activities, phenolic profile, vitamin C, sugars, physicochemical properties of cloudy apple juices was investigated. No significant changes in sugars and total polyphenols were observed, whereas significant degradation (≈28%) of vitamin C and individual polyphenols (≈18%) was noted after SCCD treatment. After 4 weeks storage only 34% of vitamin C was retained and no vitamin C was detected after this time. Ten weeks of storage caused hydrolysis of sucrose in 15%, whereas degradation of individual polyphenols ranged from 43 to 50% dep…

Time FactorsSucroseFood HandlingPhytochemicalsColorStorageCold storageAscorbic AcidPolyphenol oxidaseSubstrate SpecificityAnalytical Chemistrychemistry.chemical_compoundSupercritical carbon dioxide0404 agricultural biotechnologyPhenolsChlorogenic acidEnzyme activityVitamin CFood scienceCatechol oxidaseChromatography High Pressure LiquidColor; Enzyme activity; Polyphenols; Storage; Supercritical carbon dioxide; Synergistic effect; Vitamin C; Analytical Chemistry; Food ScienceVitamin CbiologyChemistryPolyphenolsfood and beverages04 agricultural and veterinary sciencesGeneral MedicineCarbon DioxideAscorbic acid040401 food scienceCold TemperatureFruit and Vegetable JuicesPeroxidasesPolyphenolMalusSynergistic effectbiology.proteinNutritive ValueCatechol OxidaseFood ScienceFood Chemistry
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Coordinated Sumoylation and Ubiquitination Modulate EGF Induced EGR1 Expression and Stability

2011

Background Human early growth response-1 (EGR1) is a member of the zing-finger family of transcription factors induced by a range of molecular and environmental stimuli including epidermal growth factor (EGF). In a recently published paper we demonstrated that integrin/EGFR cross-talk was required for Egr1 expression through activation of the Erk1/2 and PI3K/Akt/Forkhead pathways. EGR1 activity and stability can be influenced by many different post-translational modifications such as acetylation, phosphorylation, ubiquitination and the recently discovered sumoylation. The aim of this work was to assess the influence of sumoylation on EGF induced Egr1 expression and/or stability. Methods We …

Time FactorsTranscription GeneticSUMO proteinlcsh:MedicineUbiquitin-conjugating enzymeBiochemistrychemistry.chemical_compoundEpidermal growth factorMG132protein 1lcsh:ScienceMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3MultidisciplinaryProtein translationProtein Stabilitygene expression regulationCell biologyepidermal growth factorResearch Articlemedicine.drugProteasome Endopeptidase Complexendocrine systemkinase 1SUMO-1 ProteinBiologyDNA-binding proteinsGeneticsmedicineHumansBiologySettore BIO/10 - BIOCHIMICAProtein kinase BPI3K/AKT/mTOR pathwayEarly Growth Response Protein 1lcsh:RMitogen-activated proteinProteinsSumoylationRegulatory proteinsenzyme activationRNA stabilityMolecular biologychemistryProteolysisUbiquitin-Conjugating EnzymesProteasome inhibitorlcsh:QEarly growth responseGene expressionCell linePLoS ONE
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α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Insect Immune Evasion by Dauer and Nondauer Entomopathogenic Nematodes

2021

The immune response of animals, including insects, is overcome by some parasites. For example, dauer larvae (DL) of the obligate entomopathogenic nematodes (EPNs) Heterorhabditis and Steinernema can invade insects, evade their defenses, and cause death. Although DL were long assumed to be the only infective stage of nematodes, recent reports suggest that L2-L3 larvae of facultative EPNs are also capable of killing insects. There are no studies, to our knowledge, about the role of nonimmunological barriers (the exoskeleton and its openings) in avoiding infection by DL and L2-L3 larvae, or whether these larval stages evade the host immune system in the same way. The objective of this study wa…

Time Factorsanimal structuresmedia_common.quotation_subjectCobra Cardiotoxin ProteinsInsectMicrobiologyAnimalsEcology Evolution Behavior and SystematicsImmune Evasionmedia_commonStrongyloideaAnalysis of VarianceEnzyme PrecursorsLarvaInnate immune systemVirulencebiologyMonophenol MonooxygenaseHost (biology)fungiProphenoloxidaseHeterorhabditisbiology.organism_classificationLepidopteraGalleria mellonellaNematodeLarvaParasitologyCatechol OxidaseJournal of Parasitology
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A thin layer-based amperometric enzyme immunoassay for the rapid and sensitive diagnosis of respiratory syncytial virus infections

2012

Abstract A simple electrochemical sandwich immunoassay involving a polystyrene microarray slide coated with monoclonal capture antibodies and carbon screen-printed sensors (SPS) was designed for the rapid diagnosis of respiratory syncytial virus (RSV). The detection of the antibody-antigen complex formation relied on the use of a horseradish peroxidase conjugate. Its chronoamperometric measurement detection was performed by confining a droplet of H 2 O 2 /3,3',5,5'-tetramethylbenzidine enzyme substrate/mediator solution within a thin layer between one spot of the microarray and the surface of one screen-printed electrochemical cell. The accumulation of the enzyme product in the thin film of…

Time Factorsrespiratory syncytial virus[SDV]Life Sciences [q-bio]Biosensing TechniquesRespiratory Syncytial Virus Infectionsscreen-printed sensorSensitivity and SpecificityHorseradish peroxidaseVirusAnalytical ChemistryImmunoenzyme TechniquesElectrochemistrymedicineHumans[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyimmunoassayAntigens ViralHorseradish PeroxidaseChromatographybiologymedicine.diagnostic_testChemistryAntibodies MonoclonalRespiratory infectionSubstrate (chemistry)Molecular biologyAmperometryRespiratory Syncytial VirusesHRP labelImmunoassay[SDE]Environmental Sciencesbiology.proteinColorimetrythin layer amperometric detectionAntibodyConjugate
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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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