Search results for " enzymes"

showing 10 items of 240 documents

Benzo[a]pyrene represses DNA repair through altered E2F1/E2F4 function marking an early event in DNA damage-induced cellular senescence

2020

AbstractTranscriptional regulation of DNA repair is of outmost importance for the restoration of DNA integrity upon genotoxic stress. Here we report that the potent environmental carcinogen benzo[a]pyrene (B[a]P) activates a cellular DNA damage response resulting in transcriptional repression of mismatch repair (MMR) genes (MSH2, MSH6, EXO1) and of RAD51, the central homologous recombination repair (HR) component, ultimately leading to downregulation of MMR and HR. B[a]P-induced gene repression is caused by abrogated E2F1 signalling. This occurs through proteasomal degradation of E2F1 in G2-arrested cells and downregulation of E2F1 mRNA expression in G1-arrested cells. Repression of E2F1-me…

Cyclin-Dependent Kinase Inhibitor p21SenescenceAcademicSubjects/SCI00010DNA repairDNA damageRAD51E2F4 Transcription FactorBiologyDNA Mismatch Repair03 medical and health sciences0302 clinical medicineCell Line TumorBenzo(a)pyreneGeneticsHumansCellular SenescenceCell Line Transformed030304 developmental biology0303 health sciencesGene regulation Chromatin and EpigeneticsRecombinational DNA RepairEpithelial CellsKv Channel-Interacting ProteinsCell Cycle CheckpointsDNAFibroblastsCell biologyDNA-Binding ProteinsRepressor ProteinsMSH6DNA Repair EnzymesExodeoxyribonucleasesMutS Homolog 2 ProteinGamma RaysMSH2030220 oncology & carcinogenesisCarcinogensMCF-7 CellsDNA mismatch repairRad51 RecombinaseCell agingE2F1 Transcription FactorDNA DamageSignal TransductionNucleic Acids Research
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All-Atom simulations disclose how cytochrome reductase reshapes the substrate access/egress routes of its partner cyp450s

2020

Cytochromes P450 enzymes (CYP450s) promote the oxidative metabolism of a variety of substrates via the electrons supplied by the cytochrome P450 reductase (CPR) and upon formation of a CPR/CYP450 adduct. In spite of the pivotal regulatory importance of this process, the impact of CPR binding on the functional properties of its partner CYP450 remains elusive. By performing multiple microsecond-long all-Atom molecular dynamics simulations of a 520â »000-Atom model of a CPR/CYP450 adduct embedded in a membrane mimic, we disclose the molecular terms for their interactions, considering the aromatase (HA) enzyme as a proxy of the CYP450 family. Our study strikingly unveils that CPR binding alters…

CytochromeStereochemistryeducationPlasma protein binding-ReductaseMolecular Dynamics Simulation010402 general chemistry01 natural sciencesSubstrate SpecificityElectron Transport03 medical and health sciencesAromataseCytochrome P-450 Enzyme Systemhealth services administrationHumansddc:530General Materials Sciencecardiovascular diseasesP450 EnzymesPhysical and Theoretical Chemistryhealth care economics and organizations030304 developmental biologyNADPH-Ferrihemoprotein Reductase0303 health sciencesOxidative metabolismbiologyChemistrySubstrate (chemistry)Cytochrome P450 reductaseElectron transport chain0104 chemical sciencesAromatase; Cytochrome P-450 Enzyme System; Electron Transport; Humans; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Protein Binding; Substrate SpecificitySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteintherapeuticsProtein Binding
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Nuclear Translocation of Mismatch Repair Proteins MSH2 and MSH6 as a Response of Cells to Alkylating Agents

2000

Mammalian mismatch repair has been implicated in mismatch correction, the prevention of mutagenesis and cancer, and the induction of genotoxicity and apoptosis. Here, we show that treatment of cells specifically with agents inducing O(6)-methylguanine in DNA, such as N-methyl-N'-nitro-N-nitrosoguanidine and N-methyl-N-nitrosourea, elevates the level of MSH2 and MSH6 and increases GT mismatch binding activity in the nucleus. This inducible response occurs immediately after alkylation, is long-lasting and dose-dependent, and results from translocation of the preformed MutSalpha complex (composed of MSH2 and MSH6) from the cytoplasm into the nucleus. It is not caused by an increase in MSH2 gen…

CytoplasmDNA RepairBase Pair MismatchRNA StabilityChromosomal translocationmedicine.disease_causeBiochemistrychemistry.chemical_compoundMismatch Repair Endonuclease PMS2Adenosine TriphosphatasesNuclear ProteinsMethylnitrosoureaNeoplasm ProteinsDNA-Binding ProteinsMutS Homolog 2 ProteinDNA mismatch repairMutL Protein Homolog 1Protein BindingAlkylating AgentsMethylnitronitrosoguanidinecongenital hereditary and neonatal diseases and abnormalitiesGuanineActive Transport Cell NucleusBiologyCell LineO(6)-Methylguanine-DNA MethyltransferaseProto-Oncogene ProteinsDNA Repair ProteinmedicineHumansRNA MessengerneoplasmsMolecular BiologyAdaptor Proteins Signal TransducingCell NucleusMutagenesisnutritional and metabolic diseasesDNACell BiologyDNA MethylationMolecular biologydigestive system diseasesMSH6DNA Repair EnzymesGene Expression RegulationchemistryMSH2Carrier ProteinsGenotoxicityDNADNA DamageHeLa CellsJournal of Biological Chemistry
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Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein

2003

Activation of poly(ADP-ribose)polymerases 1 and 2 (PARP-1 and PARP-2) is one of the earliest responses of mammalian cells to DNA damage by numerous genotoxic agents. We have analysed the influence of PARP inhibition, either achieved by over-expression of the DNA binding domain of PARP-1 or by treatment with 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinolinone, on the repair of single-strand breaks (SSB), pyrimidine dimers and oxidative base modifications sensitive to Fpg protein (mostly 8-hydroxyguanine) in mammalian cells at very low, non-cytotoxic levels of DNA damage. The data show that the repair rates of all three types of DNA damage are significantly lower in PARP-inhibited c…

DNA RepairDNA damageDNA repairPoly ADP ribose polymerase[SDV]Life Sciences [q-bio]Pyrimidine dimerBiologyPoly(ADP-ribose) Polymerase InhibitorsPoly (ADP-Ribose) Polymerase InhibitorCockayne syndromeDexamethasone03 medical and health sciencesMice0302 clinical medicinePiperidinesCricetinaeGeneticsmedicineAnimalsPoly-ADP-Ribose Binding ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyCell Line TransformedMice Knockout0303 health sciencesDNA HelicasesArticlesDNADNA repair protein XRCC4Fibroblastsmedicine.diseaseIsoquinolinesMolecular biology3. Good healthDNA Repair Enzymes030220 oncology & carcinogenesisPoly(ADP-ribose) PolymerasesNucleotide excision repairDNA DamageSignal Transduction
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APE/Ref-1 and the mammalian response to genotoxic stress.

2003

Human apurinic/apyrimidinic endonuclease/redox factor-1 (hAPE/Ref-1) is a multifunctional protein involved in the repair of DNA damaged by oxidative or alkylating compounds as well as in the regulation of stress inducible transcription factors such as AP-1, NF-kappaB, HIF-1 and p53. With respect to transcriptional regulation, both redox dependent and independent mechanisms have been described. APE/Ref-1 also acts as a transcriptional repressor. Recent data indicate that APE/Ref-1 negatively regulates the activity of the Ras-related GTPase Rac1. How these different physiological activities of APE/Ref-1 are coordinated is poorly understood. So far, convincing evidence is available that the ex…

DNA RepairDNA repairRAC1Genotoxic StressTransfectionBiologyToxicologymedicine.disease_causeMolecular biologyCell biologyCell killingDNA Repair EnzymesGene Expression RegulationNeoplasmsmedicineTranscriptional regulationDNA-(Apurinic or Apyrimidinic Site) LyaseAnimalsHumansAmino Acid SequenceTranscription factorOxidative stressMutagensToxicology
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Cockayne syndrome: varied requirement of transcription-coupled nucleotide excision repair for the removal of three structurally different adducts fro…

2014

Hereditary defects in the transcription-coupled nucleotide excision repair (TC-NER) pathway of damaged DNA cause severe neurodegenerative disease Cockayne syndrome (CS), however the origin and chemical nature of the underlying DNA damage had remained unknown. To find out, to which degree the structural properties of DNA lesions determine the extent of transcription arrest in human CS cells, we performed quantitative host cell reactivation analyses of expression vectors containing various synthetic adducts. We found that a single 3-(deoxyguanosin-N 2-yl)-2-acetylaminofluorene adduct (dG(N 2)-AAF) constitutes an unsurmountable obstacle to transcription in both CS-A and CS-B cells and is remov…

DNA RepairTranscription GeneticGenetic ToxicologyDNA damagelcsh:MedicineBiologyToxicologyHost-Cell ReactivationBiochemistryCockayne syndromeCell LineDNA Adductschemistry.chemical_compoundGenes ReporterTranscription (biology)Nucleic AcidsMolecular Cell BiologyGene expressionmedicineHumansGene SilencingCockayne SyndromePoly-ADP-Ribose Binding Proteinslcsh:ScienceFluorenesMultidisciplinaryBiology and life sciencesOligonucleotidelcsh:RDNA HelicasesDeoxyguanosineDNACell Biologymedicine.diseaseMolecular biologyDNA Repair EnzymesGene Expression RegulationchemistryBiochemistrylcsh:QDNAResearch ArticleNucleotide excision repairPLoS ONE
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Late activation of stress kinases (SAPK/JNK) by genotoxins requires the DNA repair proteins DNA-PKcs and CSB.

2005

Although genotoxic agents are powerful inducers of stress kinases (SAPK/JNK), the contribution of DNA damage itself to this response is unknown. Therefore, SAPK/JNK activation of cells harboring specific defects in DNA damage-recognition mechanisms was studied. Dual phosphorylation of SAPK/JNK by the genotoxin methyl methanesulfonate (MMS) occurred in two waves. The early response (≤2 h after exposure) was similar in cells knockout for ATM, PARP, p53, and CSB or defective in DNA-PKcscompared with wild-type cells. The late response however (≥4 h), was drastically reduced in DNA-PKcsand Cockayne's syndrome B (CSB)-deficient cells. Similar results were obtained with human cells lacking DNA-PKc…

DNA ReplicationAlkylationDNA RepairDNA damageDNA repairPoly ADP ribose polymeraseDNA-Activated Protein KinaseBiologyModels Biologicalchemistry.chemical_compoundMiceAnimalsHumansPhosphorylationPoly-ADP-Ribose Binding ProteinsMolecular BiologyDNA-PKcsCells CulturedKinaseDNA HelicasesJNK Mitogen-Activated Protein KinasesNuclear ProteinsCell BiologyBase excision repairDNAArticlesMethyl MethanesulfonateMolecular biologyMethyl methanesulfonateDNA-Binding ProteinsEnzyme Activationenzymes and coenzymes (carbohydrates)DNA Repair EnzymeschemistryPhosphorylationProtein Processing Post-TranslationalDNA DamageMutagensSignal TransductionMolecular biology of the cell
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Effect of natamycin on the enumeration, genetic structure and composition of bacterial community isolated from soils and soybean rhizosphere

2004

Natamycin is commonly used to control fungal growth on agar media used for bacterial enumeration or strain isolation. However, there is no conclusive report on the possible effect of this antibiotic on bacterial growth or on the diversity of the recovered soil bacteria. Therefore, the possible effects of natamycin on the numbers of bacteria isolated at 12 degrees C from three different soils and soybean rhizosphere soil were investigated using natamycin concentrations ranging from 0 to 200 mg l(-1). Our results demonstrate that natamycin concentrations, which inhibit the growth of fungi on the media, have a small but significant inhibitory effect on the number of bacterial colony forming un…

DNA BacterialMicrobiology (medical)Antifungal Agentsfood.ingredientNatamycinRibosomal Intergenic Spacer analysisColony Count MicrobialBacterial growthBiologyPlant RootsMicrobiologyMicrobiologyBacterial genetics03 medical and health sciencesNatamycinfoodRNA Ribosomal 16SDNA Ribosomal SpacermedicineAgar[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyMolecular BiologySoil MicrobiologyComputingMilieux_MISCELLANEOUS030304 developmental biologyPrincipal Component Analysis0303 health sciencesRhizosphereBacteria030306 microbiologyGenetic VariationDNA Restriction Enzymesbiology.organism_classificationDNA Fingerprinting[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologySoybeansSoil microbiologyBacteriamedicine.drugJournal of Microbiological Methods
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Manipulating mtDNA in vivo reprograms metabolism via novel response mechanisms.

2019

Mitochondria have been increasingly recognized as a central regulatory nexus for multiple metabolic pathways, in addition to ATP production via oxidative phosphorylation (OXPHOS). Here we show that inducing mitochondrial DNA (mtDNA) stress in Drosophila using a mitochondrially-targeted Type I restriction endonuclease (mtEcoBI) results in unexpected metabolic reprogramming in adult flies, distinct from effects on OXPHOS. Carbohydrate utilization was repressed, with catabolism shifted towards lipid oxidation, accompanied by elevated serine synthesis. Cleavage and translocation, the two modes of mtEcoBI action, repressed carbohydrate rmetabolism via two different mechanisms. DNA cleavage activ…

DYNAMICSLife CyclesSTRESSMITOCHONDRIAL-DNAADN mitocondrialQH426-470BiochemistryOxidative PhosphorylationLarvaeAdenosine TriphosphateTRANSCRIPTIONPost-Translational ModificationEnergy-Producing OrganellesProtein MetabolismOrganic CompoundsDrosophila MelanogasterChemical ReactionsMETHYLATIONEukaryotaAcetylationAnimal ModelsDNA Restriction EnzymesKetonesCellular ReprogrammingMitochondrial DNAMitochondriaTRANSLOCATIONNucleic acidsInsectsChemistryDROSOPHILAExperimental Organism SystemsPhysical SciencesSURVIVALCarbohydrate MetabolismCellular Structures and OrganellesMetabolic Networks and PathwaysResearch ArticlePyruvateArthropodaForms of DNAeducationCarbohydratesBioenergeticsResearch and Analysis MethodsDNA MitochondrialBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biologyModel OrganismsGenetiikka kehitysbiologia fysiologia - Genetics developmental biology physiologyGeneticsAnimalsHumansBiology and life sciencesOrganic ChemistryOrganismsChemical CompoundsProteinsDNACell BiologyInvertebratesDELETIONSOxidative StressMetabolismMAINTENANCEDiabetes Mellitus Type 2Animal Studies1182 Biochemistry cell and molecular biologyAcidsDevelopmental BiologyPLoS Genetics
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Halloysite nanotubes for efficient loading, stabilization and controlled release of insulin

2018

Hypothesis: Oral insulin administration is not actually effective due to insulin rapid degradation, inactivation and digestion by proteolytic enzymes which results in low bioavailability. Moreover insulin is poorly permeable and lack of lipophilicity. These limits can be overcome by the loading of protein in some nanostructured carrier such as halloysite nanotubes (HNTs). Experiments: Herein we propose an easy strategy to obtain HNT hybrid materials for the delivery of insulin. We report a detailed description on the thermal behavior and stability of insulin loaded and released from the HNTs hybrid by the combination of several techniques. Findings: Release experiments of insulin from the H…

Dichroismmedicine.medical_treatmentHalloysite nanotube02 engineering and technology01 natural sciencesBiochemistryNanocompositesChitosanchemistry.chemical_compoundColloid and Surface ChemistryDrug StabilityProtein stabilityHalloysite nanotube (HNTs)InsulinTransdermalSettore CHIM/02 - Chimica FisicaDrug CarriersNanotubesProteolytic enzymes021001 nanoscience & nanotechnologyControlled releaseSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsEnzyme inhibitionAluminum SilicatesBionanocomposite film0210 nano-technologyHybrid materialBionanocomposite hybridSurface PropertiesDrug Compoundingengineering.materialCircular dichroism data010402 general chemistrySustained release InsulinAdministration CutaneousHalloysiteBiomaterialsKaolinitemedicineParticle SizeHybrid materialChitosanInsulinBiomedical applicationMedical applicationYarn Bio-nanocompositeMembranes Artificial0104 chemical sciencesNanotubeDrug LiberationHalloysite nanotubes Insulin Protein stability Sustained release Bionanocomposite hybridchemistryChemical engineeringDelayed-Action PreparationsengineeringClayNanocarriersSustained release
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