Search results for "HISTONE DEACETYLASE"

showing 10 items of 152 documents

Yeast contains multiple forms of histone acetyltransferase.

1989

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-Co…

Saccharomyces cerevisiae ProteinsIon chromatographySaccharomyces cerevisiaeBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesAcetyltransferasesEnzyme StabilityHistone octamerMolecular BiologyHistone AcetyltransferasesHistone AcetyltransferasesChromatographybiologyChemistryAcetylationCell BiologyHistone acetyltransferaseChromatography Ion ExchangeYeastChromatinChromatinIsoenzymesKineticsHistoneBiochemistryAcetylationbiology.proteinThe Journal of biological chemistry
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Yeast HAT1 and HAT2 deletions have different life-span and transcriptome phenotypes

2005

AbstractHAT-B is a yeast histone acetyltransferase composed of Hat1, Hat2 and Hif1 proteins. We demonstrate that a hat2 mutant or a hat1hat2 double mutant, but not a hat1 mutant, have an extended life-span. Transcriptome analysis shows that the single hat mutants are not very different from wild type. However, the comparison of the hat1 and hat2 transcriptomes shows that they are different. The hat1hat2 double mutant shows a transcriptional phenotype similar to that of the hat1 mutant but strongly enhanced. These results indicate that Hat2p could have additional functions in the cell to those of Hat1p.

Saccharomyces cerevisiae ProteinsTranscription GeneticHAT-BMutantBiophysicsSaccharomyces cerevisiaeBiochemistryTranscriptomeDNA-chipAcetyltransferasesStructural BiologyHat2Life-spanGeneticsImmunoprecipitationSirtuinsMolecular BiologyHistone AcetyltransferasesGeneticsbiologyWild typeCell BiologyHistone acetyltransferaseTelomereHat1PhenotypeYeastPhenotypebiology.proteinHistone deacetylaseHAT1Gene DeletionFEBS Letters
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Regulation of the p19(Arf)/p53 pathway by histone acetylation underlies neural stem cell behavior in senescence-prone SAMP8 mice.

2015

Brain aging is associated with increased neurodegeneration and reduced neurogenesis. B1/neural stem cells (B1-NSCs) of the mouse subependymal zone (SEZ) support the ongoing production of olfactory bulb interneurons, but their neurogenic potential is progressively reduced as mice age. Although age-related changes in B1-NSCs may result from increased expression of tumor suppressor proteins, accumulation of DNA damage, metabolic alterations, and microenvironmental or systemic changes, the ultimate causes remain unclear. Senescence-accelerated-prone mice (SAMP8) relative to senescence-accelerated-resistant mice (SAMR1) exhibit signs of hastened senescence and can be used as a model for the stud…

SenescenceMaleAgingHistonesMiceNeural Stem CellsNeurospheremedicineSubependymal zoneAnimalsstem cell nicheCyclin-Dependent Kinase Inhibitor p19Mice KnockoutNeuronsbiologyNeurodegenerationNeurogenesishistone acetyltransferasesBrainAcetylationCell BiologyOriginal Articlesmedicine.diseaseGenes p53Neural stem cellChromatinCell biologyadult neurogenesisOxidative StressHistoneImmunologybiology.proteinProtein Processing Post-TranslationalSAMP8 micehistone deacetylasesAging cell
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The synergistic effect of SAHA and parthenolide in MDA-MB231 breast cancer cells

2014

Abstract: The sesquiterpene lactone Parthenolide (PN) exerted a cytotoxic effect on MDA-MB231 cells, a triple-negative breast cancer (TNBC) cell line, but its effectiveness was scarce when employed at low doses. This represents an obstacle for a therapeutic utilization of PN. In order to overcome this difficulty we associated to PN the suberoylanilide hydroxamic acid (SAHA), an histone deacetylase inhibitor. Our results show that SAHA synergistically sensitized MDA-MB231 cells to the cytotoxic effect of PN. It is noteworthy that treatment with PN alone stimulated the survival pathway Akt/mTOR and the consequent nuclear translocation of Nrf2, while treatment with SAHA alone induced autophagi…

SesquiterpenePhysiologyClinical BiochemistryDown-RegulationApoptosisBreast NeoplasmsApoptosis; Autophagy; Breast Neoplasms; Cell Line Tumor; Down-Regulation; Drug Synergism; Female; Histone Deacetylase Inhibitors; Humans; Hydroxamic Acids; NF-kappa B; Sesquiterpenes; Clinical Biochemistry; Cell Biology; Physiology; Medicine (all)Hydroxamic AcidsHydroxamic AcidSettore BIO/10 - BiochimicaCell Line TumorHistone Deacetylase InhibitorAutophagyHumansBiologyVorinostatMedicine (all)NF-kappa BApoptosiDrug SynergismCell BiologyHistone Deacetylase InhibitorsFemaleHuman medicineSesquiterpenesBreast NeoplasmHumanJournal of cellular physiology
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Gene and protein signatures associated to treatment of MDA-MB231 breast cancer cells with JAHA, a novel histone deacetylase inhibitor

2014

Settore BIO/06 - Anatomia Comparata E Citologiabreast cancer cells histone deacetylase inhibitor
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The effect of the HDACi JAHA on DNA methylation of breast cancer cells by down-regulating DNMT1 through ERK signaling

2014

Settore BIO/06 - Anatomia Comparata E Citologiahistone deacetylase inhibitor breast cancer cells DNMT1 ERK
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Epigenetic agents as an adjunct to active chemotherapy in hematological tumor cell lines

2012

Epigenetic therapy is a new promising area in cancer research that is based on the use of a series of molecules capable of affecting tumor cell growth, differentiation and death by modifying the cellular mechanisms underlying the control of gene expression. Significant enhancement of traditional anticancer drug effects has been also reported by several authors. Our recent research focused on the identification of new epigenetic agent-containing drug combinations to be employed in the therapy of leukemia. The results showed that the new combination of an histone deacetylase (HDAC) inhibitor and the ribonucleotide reductase (RR) inhibitor 3’-methyl-adenosine (3’-Me-Ado) is endowed with a sign…

Settore BIO/14 - Farmacologiaepigenetics leukemia histone deacetylase inhibitors ribonucleotide reductase inhibitors bifunctional agents
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Cytotoxic effect of the HDAC3 inhibitor Pojamide and its variants on MDA-MB231 breast cancer cells

2018

Settore BIO/18 - Geneticahistone deacetylase inhibitor breast cancer cytotoxicitySettore BIO/06 - Anatomia Comparata E Citologia
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Hepatocellular carcinoma treatment over sorafenib: epigenetics, microRNAs and microenvironment. Is there a light at the end of the tunnel?

2015

Introduction: Sorafenib is currently the only approved therapy in hepatocellular carcinoma (HCC). Alternative first- and second-line treatments are a significant unmet medical need, and several biologic agents have been tested in recent years, with poor results. Therefore, angiogenic pathways and the cytokine cascade remain possible targets in HCC. Recent studies suggest a role of epigenetic processes, associated with the initiation and development of HCC. In this field, DNA methylation, micro-RNAs (miRNAs) and tumor microenvironment cells became a possible new target for HCC treatment. Areas covered: This review explains the possible role of DNA methylation and histone deacetylase inhibito…

Settore MED/06 - Oncologia MedicaClinical BiochemistrytivantinibEpigenesis GeneticAntineoplastic Agentchemistry.chemical_compoundHistone Deacetylase InhibitorDrug DiscoveryTumor MicroenvironmentMolecular Targeted TherapyplateletmicroRNALiver Neoplasmshepatocellular carcinomaSorafenibVEGFLiver NeoplasmHepatocellular carcinomaDNA methylationMolecular MedicineepigeneticHumanmedicine.drugPhenylurea CompoundSorafenibNiacinamideCarcinoma HepatocellularAntineoplastic AgentsBiologymicroRNAmedicineAnimalsHumansEpigeneticsTivantinibPharmacologyTumor microenvironmentAnimalDrug Discovery3003 Pharmaceutical SciencePhenylurea CompoundsDNA Methylationmedicine.diseasedigestive system diseasesHistone Deacetylase InhibitorsMicroRNAschemistryDrug DesignImmunologyCancer researchHistone deacetylaseExpert opinion on therapeutic targets
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Chromatin modifiers and recombination factors promote a telomere fold-back structure, that is lost during replicative senescence.

2020

Telomeres have the ability to adopt a lariat conformation and hence, engage in long and short distance intra-chromosome interactions. Budding yeast telomeres were proposed to fold back into subtelomeric regions, but a robust assay to quantitatively characterize this structure has been lacking. Therefore, it is not well understood how the interactions between telomeres and non-telomeric regions are established and regulated. We employ a telomere chromosome conformation capture (Telo-3C) approach to directly analyze telomere folding and its maintenance in S. cerevisiae. We identify the histone modifiers Sir2, Sin3 and Set2 as critical regulators for telomere folding, which suggests that a dis…

TelomeraseProtein Folding:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination Protein [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins [Medical Subject Headings]Gene ExpressionYeast and Fungal ModelsArtificial Gene Amplification and ExtensionQH426-470BiochemistryPolymerase Chain ReactionChromosome conformation captureHistonesCromatina0302 clinical medicineSirtuin 2Macromolecular Structure AnalysisSilent Information Regulator Proteins Saccharomyces cerevisiaeCellular Senescence:Organisms::Eukaryota::Fungi::Yeasts::Saccharomyces::Saccharomyces cerevisiae [Medical Subject Headings]0303 health sciencesChromosome BiologyEukaryota:Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Replication [Medical Subject Headings]TelomereSubtelomere:Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Chromosomes::Chromosome Structures::Telomere [Medical Subject Headings]Chromatin3. Good healthChromatinCell biologyNucleic acidsTelomeres:Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Cycle::Cell Division::Telomere Homeostasis [Medical Subject Headings]Experimental Organism SystemsDaño del ADNEpigeneticsResearch ArticleSenescenceDNA Replication:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Amidohydrolases::Histone Deacetylases [Medical Subject Headings]Chromosome Structure and FunctionProtein StructureSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyResearch and Analysis MethodsHistone DeacetylasesChromosomes03 medical and health sciencesSaccharomycesModel Organisms:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Intracellular Signaling Peptides and Proteins::Sirtuins::Sirtuin 2 [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins::Silent Information Regulator Proteins Saccharomyces cerevisiae [Medical Subject Headings]DNA-binding proteinsGenetics:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Recombinases::Rec A Recombinases::Rad51 Recombinase [Medical Subject Headings]Molecular Biology TechniquesMolecular Biology030304 developmental biologyCromosomasSenescencia celularOrganismsFungiBiology and Life SciencesProteinsTelomere HomeostasisCell BiologyDNAMethyltransferasesG2-M DNA damage checkpointProteína recombinante y reparadora de ADN Rad52YeastTelomereRad52 DNA Repair and Recombination ProteinRepressor ProteinsAnimal Studies:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Transcription Factors::Repressor Proteins [Medical Subject Headings]DNA damageRad51 RecombinaseHomologous recombination030217 neurology & neurosurgeryTelómeroDNA DamagePLoS Genetics
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