Search results for "Hydroxamic Acids"

showing 10 items of 40 documents

SAHA induces apoptosis in hepatoma cells and synergistically interacts with the proteasome inhibitor Bortezomib.

2007

Histone deacetylase (HDAC) inhibitors represent a promising group of anticancer agents. This paper shows that the HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) stimulated at 5-10 microM apoptosis in human hepatoma HepG2 and Huh6 cells, but was ineffective in primary human hepatocytes (PHH). In HepG2 cells SAHA induced the extrinsic apoptotic pathway, increasing the expression of both FasL and FasL receptor and causing the activation of caspase-8. Moreover, SAHA enhanced the level of Bim proteins, stimulated alternative splicing of the Bcl-X transcript with the expression of the proapoptotic Bcl-Xs isoform, induced degradation of Bid into the apoptotic factor t-Bid and dephosphorylat…

Cancer ResearchCarcinoma HepatocellularFas Ligand ProteinClinical BiochemistryPharmaceutical ScienceApoptosisHydroxamic AcidsFas ligandHistone DeacetylasesBortezomibCell Line TumormedicineHumansProtease InhibitorsProtein kinase BVorinostatHDAC inhibitors . HepG2 cells . PHH . Extrinsic and intrinsic apoptotic pathwaysbcl-2-Associated X ProteinPharmacologyMembrane Potential MitochondrialCaspase 8VorinostatbiologyChemistryBortezomibCytochrome cBiochemistry (medical)Cell BiologyBoronic AcidsHistone Deacetylase InhibitorsProteasomeApoptosisPyrazinesProteasome inhibitorbiology.proteinCancer researchApoptosis Regulatory ProteinsProteasome Inhibitorsmedicine.drug
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Holo-APP and G-protein-mediated signaling are required for sAPPa-induced activation of the Akt survival pathway

2014

International audience; Accumulating evidence indicates that loss of physiologic amyloid precursor protein (APP) function leads to reduced neuronal plasticity, diminished synaptic signaling and enhanced susceptibility of neurons to cellular stress during brain aging. Here we investigated the neuroprotective function of the soluble APP ectodomain sAPPa (soluble APPa), which is generated by cleavage of APP by a-secretase along the non-amyloidogenic pathway. Recombinant sAPPa protected primary hippocampal neurons and SH-SY5Y neuroblastoma cells from cell death induced by trophic factor deprivation. We show that this protective effect is abrogated in neurons from APP-knockout animals and APP-de…

Cancer ResearchCell SurvivalADAM10Amino Acid MotifsImmunology[SDV.BC]Life Sciences [q-bio]/Cellular BiologyIn Vitro TechniquesHydroxamic AcidsHippocampusNeuroprotectionCell LineADAM10 ProteinAmyloid beta-Protein PrecursorMicePhosphatidylinositol 3-Kinases03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemental disordersAmyloid precursor proteinAnimalsHumansProtein kinase BPI3K/AKT/mTOR pathwayPhosphoinositide-3 Kinase Inhibitors030304 developmental biologyMice Knockout0303 health sciencesbiologyBiochemistry and Molecular BiologyMembrane ProteinsDipeptidesCell BiologyMolecular biologyRecombinant ProteinsMice Inbred C57BLADAM ProteinsPertussis Toxinbiology.proteinOriginal ArticleSynaptic signalingAmyloid Precursor Protein SecretasesNeuron deathProto-Oncogene Proteins c-aktAmyloid precursor protein secretase030217 neurology & neurosurgeryBiokemi och molekylärbiologiSignal Transduction
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Histone deacetylase inhibitors induce in human hepatoma HepG2 cells acetylation of p53 and histones in correlation with apoptotic effects

2007

This report shows that histone deacetylase inhibitors (HDACIs) induced apoptosis in human hepatoma HepG2 cells in a dose- and time-dependent manner. Trichostatin A (TSA), ITF2357 and suberoylanilide hydroxamic acid (SAHA), which were very effective agents, caused apoptotic effects after a lag phase of 12-16 h. In order to elucidate the mechanism of HDACIs action in HepG2 cells we have studied the effects of TSA, ITF2357 and SAHA on acetylation of p53 and histones H2A, H2B, H3 and H4. It was observed that HDACIs rapidly induced acetylation of these proteins, being the effects clearly visible already at 30 min of treatment at the same doses which caused apoptosis. Analysis of the immunocomple…

Cancer ResearchProgrammed cell deathCarcinoma Hepatocellularmedicine.drug_classAntineoplastic AgentsApoptosisBiologyHydroxamic AcidsHistonesCell Line TumorSettore BIO/10 - BiochimicamedicineHumansBenzothiazolesEnzyme InhibitorsRNA Small InterferingHistone AcetyltransferasesVorinostatHistone deacetylase inhibitors acetylation p53 histones apoptosis hepatoma cells.Liver NeoplasmsHistone deacetylase inhibitorAcetylationProto-Oncogene Proteins c-mdm2Molecular biologyHistone Deacetylase InhibitorsTrichostatin AHistoneOncologyPCAFAcetylationbiology.proteinHistone deacetylaseTumor Suppressor Protein p53DNA DamageToluenemedicine.drugInternational Journal of Oncology
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The role of oxidative stress in apoptosis induced by the histone deacetylase inhibitor suberoylanilide hydroxamic acid in human colon adenocarcinoma …

2008

Histone deacetylase inhibitors (HDACIs) activate genes that promote cell cycle arrest and apoptosis in a number of tumor cells. This study showed that suberoylanilide hydroxamic acid (SAHA), a potent and commonly used HDACI, induced apoptosis in human colon adenocarcinoma HT-29 cells in a time- and dose-dependent manner. This effect was accompanied by the induction of oxidative stress, dissipation of mitochondrial transmembrane potential and activation of executioner caspases. Moreover, SAHA increased the levels of phosphorylated active forms of p38 and JNK. The addition of either the antioxidant N-acetylcysteine or the specific inhibitor of NADPH oxidase diphenylene iodonium chloride reduc…

Cancer ResearchProgrammed cell deathmedicine.drug_classCell Survivalp38 mitogen-activated protein kinasesBlotting WesternApoptosisAdenocarcinomamedicine.disease_causeHydroxamic AcidsAntioxidantsSettore BIO/10 - BiochimicamedicineHumansEnzyme InhibitorsProtein kinase BCaspaseMembrane Potential MitochondrialVorinostatbiologyHistone deacetylase inhibitorEnzyme ActivationHistone Deacetylase InhibitorsOxidative StressOncologyBiochemistryApoptosisCaspasesColonic NeoplasmsCancer researchbiology.proteinHistone deacetylaseReactive Oxygen Speciescolon adenomacarcinoma cells histone deacetylase inhibitors apoptosisHT29 CellsOxidative stressSignal TransductionInternational journal of oncology
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Histone deacetylase inhibitors: apoptotic effects and clinical implications (Review).

2008

It has been shown that epigenetic modifications play an important role in tumorigenesis. Thus, affecting epigenetic tumorigenic alterations can represent a promising strategy for anticancer targeted therapy. Among the key chromatin modifying enzymes which influence gene expression, histone acetyltransferases (HATs) and histone deacetylases (HDACs) have recently attracted interest because of their impact on tumor development and progression. Increased expression of HDACs and disrupted activities of HATs have been found in several tumor types, with a consequent hypoacetylated state of chromatin that can be strictly correlated with low expression of either tumor suppressor or pro-apoptotic gen…

Cancer Researchmedicine.drug_classAntineoplastic AgentsApoptosisBiologyHydroxamic AcidsModels BiologicalRomidepsinEpigenesis Geneticchemistry.chemical_compoundDepsipeptidesNeoplasmsSettore BIO/10 - BiochimicamedicineHumansEpigeneticsVorinostatSulfonamidesVorinostatHistone deacetylase inhibitorHDACI apoptosisChromatinChromatinProtein Structure TertiaryGene Expression Regulation NeoplasticHistone Deacetylase InhibitorsHistoneOncologychemistryModels ChemicalCancer researchbiology.proteinHistone deacetylaseBelinostatmedicine.drug
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Properties of the yeast nuclear histone deacetylase.

1994

A nuclear histone deacetylase from yeast was partially purified and some of its characteristics were studied. Histone deacetylase activity was stimulated in vitro by high-mobility-group nonhistone chromatin proteins 1 and 2 and ubiquitin and inhibited by spermine and spermidine, whereas n-butyrate had no significant inhibitory effect. Like the mammalian enzyme, partially purified histone deacetylase from yeast was strongly inhibited by trichostatin A. However, in crude extract preparations the yeast enzyme was not inhibited and treatment with trichostatin in vivo did not show any effect, either on the histone acetylation level or on cell viability. At low ionic strength, the enzyme can be i…

Cell NucleusHistone deacetylase 5HDAC11ChemistryHistone deacetylase 2HDAC10Cell BiologySaccharomyces cerevisiaeHydroxamic AcidsBiochemistryHistone DeacetylasesSubstrate SpecificityHistone Deacetylase InhibitorsMolecular WeightTrichostatin ABiochemistrymedicineChromatography GelHistone deacetylase activityHistone deacetylaseMolecular Biologymedicine.drugDeacetylase activityResearch ArticleThe Biochemical journal
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Curcumin effectively inhibits oncogenic NF-κB signaling and restrains stemness features in liver cancer

2015

Background & Aims The cancer stem cells (CSCs) have important therapeutic implications for multi-resistant cancers including hepatocellular carcinoma (HCC). Among the key pathways frequently activated in liver CSCs is NF-κB signaling. Methods We evaluated the CSCs-depleting potential of NF-κB inhibition in liver cancer achieved by the IKK inhibitor curcumin, RNAi and specific peptide SN50. The effects on CSCs were assessed by analysis of side population (SP), sphere formation and tumorigenicity. Molecular changes were determined by RT-qPCR, global gene expression microarray, EMSA, and Western blotting. Results HCC cell lines exposed to curcumin exhibited differential responses to curcumin a…

CurcuminAntineoplastic AgentsIκB kinaseBiologyHydroxamic AcidsArticleHistone DeacetylasesMicechemistry.chemical_compoundSide populationCancer stem cellCell Line TumormedicineAnimalsHumansHepatologyLiver NeoplasmsNF-kappa BNF-κBmedicine.diseaseMolecular biologychemistryCell cultureNeoplastic Stem CellsCancer researchCurcuminSignal transductionLiver cancerSignal TransductionJournal of Hepatology
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Influences of histone deacetylase inhibitors and resveratrol on DNA repair and chromatin compaction

2013

Accessibility of DNA is a prerequisite for both DNA damage and repair. Therefore, the chromatin structure is expected to have major impact on both processes, with opposite consequences for the stability of the genome. To analyse the influence of chromatin compaction on the generation and repair of various types of DNA modifications, we modulated the global chromatin structure of AS52 Chinese hamster ovary cells and HeLa cells by treatment with either histone deacetylase inhibitors or resveratrol and measured the repair kinetics of (i) pyrimidine dimers induced by ultraviolet B, (ii) oxidised purines generated by photosensitisation and (iii) single-strand breaks induced by H2O2, using an alk…

DNA RepairUltraviolet RaysDNA damageDNA repairHealth Toxicology and MutagenesisCarbazolesCHO CellsHydroxamic AcidsToxicologyChromatin remodelingCricetulusStilbenesHistone H2AGeneticsmedicineAnimalsDeoxyribonuclease IHumansDNA Breaks Single-StrandedGenetics (clinical)EpigenomicsbiologyChemistryMolecular biologyChromatinCell biologyProliferating cell nuclear antigenChromatinHistone Deacetylase InhibitorsButyratesTrichostatin APyrimidine DimersResveratrolbiology.proteinHeLa Cellsmedicine.drugMutagenesis
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In Vitro Assessment of the Genotoxic Hazard of Novel Hydroxamic Acid- and Benzamide-Type Histone Deacetylase Inhibitors (HDACi)

2020

Histone deacetylase inhibitors (HDACi) are already approved for the therapy of leukemias. Since they are also emerging candidate compounds for the treatment of non-malignant diseases, HDACi with a wide therapeutic window and low hazard potential are desirable. Here, we investigated a panel of 12 novel hydroxamic acid- and benzamide-type HDACi employing non-malignant V79 hamster cells as toxicology guideline-conform in vitro model. HDACi causing a &ge

DNA damageApoptosisHydroxamic AcidsDNA damage responseArticleCatalysisCell LineHistonesInorganic Chemistrylcsh:Chemistrychemistry.chemical_compoundHDAC inhibitorsCricetinaeDNA strand breaksmedicineAnimalsHumansDNA Breaks Double-StrandedDNA Breaks Single-StrandedPhosphorylationPhysical and Theoretical Chemistrynormal tissue toxicityMolecular BiologyVorinostatlcsh:QH301-705.5SpectroscopyVorinostatMicronucleus TestsHydroxamic acidMutagenicity TestsEntinostatOrganic ChemistryHistone H2AXgenetic instabilityGeneral MedicineComputer Science ApplicationsHistone Deacetylase Inhibitorschemistrylcsh:Biology (General)lcsh:QD1-999BenzamidesCancer researchComet AssayHistone deacetylasegenotoxic hazardDNAMutagensNucleotide excision repairmedicine.drugInternational Journal of Molecular Sciences
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The histone deacetylase inhibitor suberoylanilide hydroxamic acid sensitizes human hepatocellular carcinoma cells to TRAIL-induced apoptosis by TRAIL…

2009

Abstract This paper shows that the histone deacetylase inhibitor SAHA sensitised at sub-toxic doses human hepatocellular carcinoma cells (HepG2, Hep3B and SK-Hep1) to TRAIL-induced apoptosis, while it was ineffective in primary human hepatocytes (PHHs). In particular in HCC cells SAHA increased the expression of death receptor 5 (DR5) and caused a decrement of c-Flip. These two modifications provoked in the presence of TRAIL the rapid production of TRAIL-DISC and the activation of caspase-8. Consequently SAHA/TRAIL combination induced many apoptotic events, such as a cleavage of Bid into tBid, dissipation of mitochondrial membrane potential, activation of caspase-3 with the consequent cleav…

Death Domain Receptor Signaling Adaptor ProteinsCancer Researchmedicine.medical_specialtyProgrammed cell deathCarcinoma Hepatocellularmedicine.drug_classmedicine.medical_treatmentBlotting WesternCASP8 and FADD-Like Apoptosis Regulating ProteinDown-RegulationAntineoplastic AgentsApoptosisBiologyHydroxamic AcidsHDACI TRAIL apoptosisInternal medicineSettore BIO/10 - BiochimicamedicineHumansProtein kinase BVorinostatLiver NeoplasmsHistone deacetylase inhibitorNF-kappa Bmedicine.diseaseReceptors TNF-Related Apoptosis-Inducing LigandCytokineEndocrinologyOncologyDrug Resistance NeoplasmApoptosisHepatocellular carcinomaCancer researchTumor necrosis factor alphaSignal transductionProto-Oncogene Proteins c-akt
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