Search results for "DNA Topoisomerases"

showing 9 items of 29 documents

New alkaloid antibiotics that target the DNA topoisomerase I of Streptococcus pneumoniae

2011

16 pags, 3 figs, 3 tabs

Models MolecularTopoisomerase-I Inhibitormedicine.disease_causeMicrobiologyBiochemistryCell LineMicrobiology03 medical and health scienceschemistry.chemical_compoundAlkaloidsBacterial ProteinsStreptococcus pneumoniaemedicineHumansAporphineMolecular BiologyEscherichia coli030304 developmental biologychemistry.chemical_classification0303 health sciencesDose-Response Relationship Drugbiology030306 microbiologyTopoisomeraseCell BiologyPhenanthrenesProtein Structure TertiaryAnti-Bacterial Agents3. Good healthStreptococcus pneumoniaeEnzymeDNA Topoisomerases Type IchemistryBiochemistrybiology.proteinDNA supercoilTopoisomerase I InhibitorsGrowth inhibitionJournal of Biological Chemistry 286: 6402-6413 (2011)
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Nalidixic acid-resistant V79 cells with reduced DNA topoisomerase II activity and amplification prone phenotype

1992

Spontaneously nalidixic acid-resistant lines (NAr lines) were selected from a V79 Chinese hamster cell line and phenotypically characterized. NAr lines showed an increased doubling time, a higher number of spontaneous SCE, and more interestingly, decreased DNA topoisomerase II activity. These lines were also cross-resistant to the eukaryotic topoisomerase II inhibitors etoposide and adriamycin, but showed the same level of sensitivity as the parental line to the DNA topoisomerase I inhibitor camptothecin. NAr lines were cross-resistant to other drugs, such as PALA, MTX and MPA, resistance to which has been shown to arise by amplification of the target genes. This last feature, together with…

Nalidixic acidCell SurvivalHealth Toxicology and MutagenesisDrug ResistanceAntineoplastic AgentsBiologyCell LineNalidixic Acidchemistry.chemical_compoundCricetulusCricetinaeGeneticsmedicineAnimalsTopoisomerase II InhibitorsMolecular BiologyGeneEtoposideEtoposideCell NucleusMesocricetusTopoisomeraseGene AmplificationNucleic Acid HybridizationDNADNA topoisomerase II activityMolecular biologyDNA Topoisomerases Type IIPhenotypeDNA Topoisomerases Type IchemistryDoxorubicinbiology.proteinTopoisomerase-II InhibitorSister Chromatid ExchangeDNACamptothecinmedicine.drugMutation Research/Fundamental and Molecular Mechanisms of Mutagenesis
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Water-soluble isoindolo[2,1-a]quinoxalin-6-imines: In vitro antiproliferative activity and molecular mechanism(s) of action

2015

Abstract Water-soluble isoindoloquinoxalin (IIQ) imines and the corresponding acetates were conveniently prepared from the key intermediates 2-(2′-aminophenyl)-2H-isoindole-1-carbonitriles obtained by a Strecker reaction between substituted 1,2-dicarbaldehydes and 1,2-phenylenediamines. Both series were screened by the National Cancer Institute (Bethesda, MD) and showed potent antiproliferative activity against a panel of 60 human tumor cell lines. Several of the novel compounds showed GI50 values at a nanomolar level on the majority of the tested cell lines. Among IIQ derivatives, methoxy substituents at positions 3 and 8 or/and 9 were especially effective in impairing cell cycle progressi…

StereochemistryStrecker amino acid synthesisAntineoplastic AgentsApoptosisIsoindolo[21-a]quinoxalin-6-imineTopoisomerase I inhibitorsTopoisomerase-I InhibitorMicrotubulesTubulinCell Line TumorQuinoxalinesDrug DiscoveryHumansCytotoxic T cellCell ProliferationPharmacologyTopoisomerase I inhibitorChemistryAntitubulin agents; G-quadruplex interaction; Isoindolo[2; 1-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; PharmacologyAntitubulin agentsDrug Discovery3003 Pharmaceutical ScienceCell CycleOrganic ChemistryWaterGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaIn vitroTelomereAntitubulin agentAntitubulin agents; G-quadruplex interaction; Isoindolo[21-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; Pharmacology1-a]quinoxalin-6-iminesDNA Topoisomerases Type ISolubilityBiochemistryCell cultureApoptosisIsoindolo[2Cancer cellIminesG-quadruplex interactionDrug Screening Assays Antitumor
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Alteration of DNA topoisomerase II activity during infection of H9 cells by human immunodeficiency virus type 1 in vitro: a target for potential ther…

1990

Infection of H9 cells with human immunodeficiency virus type 1 (HIV-1) was found to decrease the phosphorylation of DNA topoisomerase II during the initial phase of infection. Simultaneously, with a later overshoot of phosphorylation and the subsequent activation of DNA topoisomerase II, the production of HIV-1 started. Applying three new protein kinase C inhibitors from the class of O-alkylglycerophospholipids we demonstrated that inhibition of protein kinase C-mediated phosphorylation of DNA topoisomerase II resulted in an inhibition of HIV-1 production. Based on the differential effect of the two protein kinase C activators, phorbol ester and bryostatin, we conclude that phosphorylation …

T-LymphocytesMitogen-activated protein kinase kinaseIn Vitro TechniquesMAP2K7Cell LineLactonesVirologyAnimalsPhosphorylationProtein kinase AProtein kinase CProtein Kinase CPharmacologybiologyCyclin-dependent kinase 2LysophosphatidylcholinesRats Inbred StrainsDNA topoisomerase II activityBryostatinsProtein kinase RMolecular biologyRatsDNA Topoisomerases Type Ibiology.proteinHIV-1Tetradecanoylphorbol AcetateCyclin-dependent kinase 9Electrophoresis Polyacrylamide GelMacrolidesAntiviral research
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pRb suppresses camptothecin-induced apoptosis in human osteosarcoma Saos-2 cells by inhibiting c-Jun N-terminal kinase

2001

AbstractThis paper studies the cytotoxic effect induced by the topoisomerase I inhibitor camptothecin in human osteosarcoma Saos-2 cells, which lack p53 and contain a non-functional form of the product of the retinoblastoma gene, pRb. Cytotoxicity induced by camptothecin was dose- and time-dependent; the treatment with 100 nM camptothecin reduced cell viability by 50% at 32 h and by 75% at 72 h of exposure. The cytotoxic effect was caused by apoptosis, as ascertained by morphological evidence, acridine orange-ethidium bromide staining and flow cytometric analysis. Apoptosis was accompanied by both the activation of caspase-3 and the fragmentation of poly(ADP-ribose) polymerase. Treatment wi…

Time FactorsCell SurvivalProto-Oncogene Proteins c-junBlotting WesternBiophysicsApoptosisBiologyTransfectionRetinoblastoma ProteinBiochemistryStructural BiologyTumor Cells CulturedpRb JNK topoisomerase I inhibitors osteosarcomaGeneticsmedicineHumansCytotoxic T cellViability assayPhosphorylationFragmentation (cell biology)neoplasmsMolecular BiologySaos-2 cellsc-Jun N-terminal kinaseCell SizeDose-Response Relationship DrugCaspase 3Cell growthCell Cyclec-junJNK Mitogen-Activated Protein KinasesHydrogen PeroxideCell BiologyFlow CytometryGlutathioneMolecular biologyEnzyme ActivationOxidative StresspRbDNA Topoisomerases Type IApoptosisCaspasesCamptothecinMitogen-Activated Protein KinasesPoly(ADP-ribose) PolymerasesTopoisomerase I InhibitorsCamptothecinmedicine.drugFEBS Letters
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A method for genome-wide analysis of DNA helical tension by means of psoralen-DNA photobinding

2010

The helical tension of chromosomal DNA is one of the epigenetic landmarks most difficult to examine experimentally. The occurrence of DNA crosslinks mediated by psoralen photobinding (PB) stands as the only suitable probe for assessing this problem. PB is affected by chromatin structure when is done to saturation; but it is mainly determined by DNA helical tension when it is done to very low hit conditions. Hence, we developed a method for genome-wide analysis of DNA helical tension based on PB. We adjusted in vitro PB conditions that discern DNA helical tension and applied them to Saccharomyces cerevisiae cells. We selected the in vivo cross-linked DNA sequences and identified them on DNA …

Transcription GeneticUltraviolet RaysSaccharomyces cerevisiaeMutantADNSaccharomyces cerevisiaeBiologyDNA sequencingGenètica molecularchemistry.chemical_compoundGeneticsTrioxsalenDNA FungalOligonucleotide Array Sequence AnalysisProbabilityTopoisomeraseChromosomeDNAGenomicsbiology.organism_classificationMolecular biologyChromatinNucleosomesChromatinDNA-Binding ProteinsGenòmicaCross-Linking ReagentschemistryNaked DNAbiology.proteinBiophysicsNucleic Acid ConformationMethods OnlineChromosomes FungalDNA TopoisomerasesDNA
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WRN protects against topo I but not topo II inhibitors by preventing DNA break formation

2008

The Werner syndrome helicase/3′-exonuclease (WRN) is a major component of the DNA repair and replication machinery. To analyze whether WRN is involved in the repair of topoisomerase-induced DNA damage we utilized U2-OS cells, in which WRN is stably down-regulated (wrn-kd), and the corresponding wild-type cells (wrn-wt). We show that cells not expressing WRN are hypersensitive to the toxic effect of the topoisomerase I inhibitor topotecan, but not to the topoisomerase II inhibitor etoposide. This was shown by mass survival assays, colony formation and induction of apoptosis. Upon topotecan treatment WRN deficient cells showed enhanced DNA replication inhibition and S-phase arrest, whereas af…

congenital hereditary and neonatal diseases and abnormalitiesWerner Syndrome HelicaseDNA RepairCell SurvivalDNA damageDNA repairBlotting WesternApoptosisBone NeoplasmsBiologyTopoisomerase-I InhibitorBiochemistryArticleWerner Syndrome HelicaseColony-Forming Units AssayHistonesTumor Cells CulturedmedicineHumansTopoisomerase II InhibitorsEnzyme InhibitorsRNA Small InterferingeducationMolecular BiologyEtoposideOsteosarcomaeducation.field_of_studyRecQ HelicasesTopoisomeraseCell CycleDNA Breaksnutritional and metabolic diseasesCell BiologyAntineoplastic Agents PhytogenicMolecular biologyDNA Topoisomerases Type IIExodeoxyribonucleasesBromodeoxyuridineDNA Topoisomerases Type IDNA Replication InhibitionCancer researchbiology.proteinTopoisomerase I InhibitorsTopoisomerase-II InhibitorTopotecanCamptothecinmedicine.drugDNA Repair
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Inhibition of Rac1 signaling by lovastatin protects against anthracycline-induced cardiac toxicity

2011

Normal tissue damage limits the efficacy of anticancer therapy. For anthracyclines, the clinically most relevant adverse effect is cardiotoxicity. The mechanisms involved are poorly understood and putative cardioprotectants are controversially discussed. Here, we show that the lipid-lowering drug lovastatin protects rat H9c2 cardiomyoblasts from doxorubicin in vitro. Protection by lovastatin is related to inhibition of the Ras-homologous GTPase Rac1. It rests on a reduced formation of DNA double-strand breaks, resulting from the inhibition of topoisomerase II by doxorubicin. Doxorubicin transport and reactive oxygen species are not involved. Protection by lovastatin was confirmed in vivo. I…

rac1 GTP-Binding ProteinCancer ResearchAnthracyclineDoxorubicin transportCardiac fibrosismedicine.medical_treatmentImmunologyPharmacologyBiologyDNA damage responsestatinsMiceCellular and Molecular NeuroscienceRho GTPasespolycyclic compoundsmedicineAnimalsDNA Breaks Double-StrandedMyocytes CardiacDoxorubicinLovastatinanthracyclinesCardiotoxicityAntibiotics AntineoplasticTroponin IConnective Tissue Growth FactorCell Biologymedicine.diseaseRatsCTGFDNA Topoisomerases Type IICytokinenormal tissue damageDoxorubicinOriginal Articlelipids (amino acids peptides and proteins)LovastatinAtrial Natriuretic FactorSignal Transductionmedicine.drugCell Death & Disease
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Rac1 protein signaling is required for DNA damage response stimulated by topoisomerase II poisons.

2012

To investigate the potency of the topoisomerase II (topo II) poisons doxorubicin and etoposide to stimulate the DNA damage response (DDR), S139 phosphorylation of histone H2AX (γH2AX) was analyzed using rat cardiomyoblast cells (H9c2). Etoposide caused a dose-dependent increase in the γH2AX level as shown by Western blotting. By contrast, the doxorubicin response was bell-shaped with high doses failing to increase H2AX phosphorylation. Identical results were obtained by immunohistochemical analysis of γH2AX focus formation, comet assay-based DNA strand break analysis, and measuring the formation of the topo II-DNA cleavable complex. At low dose, doxorubicin activated ataxia telangiectasia m…

rac1 GTP-Binding Proteinrho GTP-Binding ProteinsDNA damageAntineoplastic AgentsBiochemistryPoisonsCell LineHistonesNeoplasmsmedicineAnimalsTopoisomerase II InhibitorsDoxorubicinMolecular BiologyEtoposidebiologyCell DeathTopoisomeraseCell BiologyMolecular biologyImmunohistochemistryRatsComet assayHistoneDNA Topoisomerases Type IIDNA Topoisomerases Type Ibiology.proteinPhosphorylationTopoisomerase-II InhibitorHydroxymethylglutaryl-CoA Reductase Inhibitorsmedicine.drugDNA DamageSignal TransductionThe Journal of biological chemistry
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