Search results for "Topoisomerase-II Inhibitor"

showing 10 items of 11 documents

Resistance of p53 knockout cells to doxorubicin is related to reduced formation of DNA strand breaks rather than impaired apoptotic signaling

2003

The anthracycline doxorubicin (adriamycin) is an important chemotherapeutic agent used in the treatment of solid epithelial and mesenchymal tumors as well as leukemias. A variety of mechanisms has been proposed to be involved in doxorubicin-induced cytotoxicity such as DNA intercalation, oxidative stress, DNA strand breakage by inhibition of topoisomerase II, activation of death receptors, and altered p53 expression. Concerning doxorubicin resistance and p53 status data reported are contradictory. Here, we show that mouse fibroblasts deficient in p53 (p53(-/-)) are more resistant to doxorubicin than p53 wild-type (p53 wt) cells. This is in contrast to other genotoxic agents (UV-light, alkyl…

AnthracyclineApoptosisIn Vitro TechniquesBiochemistryCell LineMicemedicineAnimalsTopoisomerase II InhibitorsDoxorubicinMolecular BiologyEtoposideMice KnockoutbiologyTopoisomeraseCell BiologyFas receptorMolecular biologyDoxorubicinDrug Resistance NeoplasmCell cultureApoptosisCancer researchbiology.proteinTumor Suppressor Protein p53Topoisomerase-II InhibitorDNA DamageSignal Transductionmedicine.drugDNA Repair
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Lovastatin protects human endothelial cells from the genotoxic and cytotoxic effects of the anticancer drugs doxorubicin and etoposide

2006

Background and purpose: 3-Hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors (statins) are frequently used lipid-lowering drugs. Moreover, they exert pleiotropic effects on cellular stress responses and death. Here, we analysed whether lovastatin affects the sensitivity of primary human endothelial cells (HUVEC) to the anticancer drug doxorubicin. Experimental approach: We investigated whether pretreatment of HUVEC with low dose of lovastatin influences the cellular sensitivity to doxorubicin. To this end, cell viability, proliferation and apoptosis as well as DNA damage-triggered stress response were analysed. Key results: Lovastatin reduced the cytotoxic potency of doxorub…

DNA ReplicationCell SurvivalDNA damageApoptosisBiologyPharmacologypolycyclic compoundsmedicineHumansTopoisomerase II InhibitorsDoxorubicinLovastatinEtoposideEtoposideFluorescent DyesPharmacologyAntibiotics AntineoplasticReverse Transcriptase Polymerase Chain ReactionTopoisomeraseCell CycleEndothelial Cellsnutritional and metabolic diseasesAntimutagenic AgentsFibroblastsCell cycleResearch PapersAntineoplastic Agents PhytogenicDoxorubicinDrug Resistance NeoplasmHMG-CoA reductasebiology.proteinlipids (amino acids peptides and proteins)LovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsTopoisomerase-II InhibitorReactive Oxygen SpeciesFluorescein-5-isothiocyanateDNA Damagemedicine.drugBritish Journal of Pharmacology
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Identification of Gip as a novel phage‐encoded gyrase inhibitor protein of Corynebacterium glutamicum

2021

By targeting key regulatory hubs of their host, bacteriophages represent a powerful source for the identification of novel antimicrobial proteins. Here, a screening of small cytoplasmic proteins encoded by the CGP3 prophage of Corynebacterium glutamicum resulted in the identification of the gyrase-inhibiting protein Cg1978, termed Gip. Pull-down assays and surface plasmon resonance revealed a direct interaction of Gip with the gyrase subunit A (GyrA). The inhibitory activity of Gip was shown to be specific to the DNA gyrase of its bacterial host C. glutamicum. Overproduction of Gip in C. glutamicum resulted in a severe growth defect as well as an induction of the SOS response. Furthermore, …

DNA Replicationendocrine systemProtein subunitProphagesBiologyMicrobiologyDNA gyraseCorynebacterium glutamicum03 medical and health scienceschemistry.chemical_compoundViral Proteinsddc:570Topoisomerase II InhibitorsSOS responseMolecular BiologyProphage030304 developmental biology0303 health sciences030306 microbiologyDNA replicationAnti-Bacterial AgentsHigh-Throughput Screening AssaysCorynebacterium glutamicumchemistryBiochemistrybacteriaTopoisomerase-II InhibitorDNAhormones hormone substitutes and hormone antagonistsMolecular Microbiology
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Cisplatin-induced endoreduplication in CHO cells: DNA damage and inhibition of topoisomerase II.

2006

It has been proposed that polyploid cells that arise during a variety of pathological conditions and as a result of exposure to genotoxicants, typically in the liver, become aneuploid through genetic instability. Aneuploidy contributes to, or even drives, tumour development. We have assessed the capacity of the drug cisplatin, one of the most commonly used compounds for the treatment of malignancies, to induce endoreduplication, a particular type of polyploidy, in cultured Chinese hamster AA8 cells. Taking into account that any interference with DNA topoisomerase II (topo II) function leads to endoreduplication, we have found that treatment of the cells with this platinum compound results i…

DNA damageHealth Toxicology and MutagenesisAntineoplastic AgentsCHO CellsPolyploidychemistry.chemical_compoundCricetinaeGeneticsmedicineEndoreduplicationAnimalsHumansTopoisomerase II InhibitorsEnzyme InhibitorsMolecular BiologyCisplatinbiologySettore BIO/16 - Anatomia UmanaTopoisomeraseChinese hamster ovary cellNeoplasms Second PrimaryCell cycleAneugensAneuploidyMolecular biologychemistryTopoisomerase II cisplatinbiology.proteinCancer researchTopoisomerase-II InhibitorCisplatinDNAmedicine.drugDNA Damage
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Topoisomerase II inhibition and high yield of endoreduplication induced by the flavonoids luteolin and quercetin

2006

Luteolin and quercetin are widely distributed plant flavonoids that possess a variety of chemical and biological activities, including free-radical scavenging and antioxidant activity. Recently, both flavonoids have been reported to inhibit DNA topoisomerases I and II (topo I and topo II), a property that, together with their ability to induce DNA and chromosome damage, has made them candidate anticancer compounds. In the present study, we confirmed that both compounds are topo II inhibitors by conducting a comparative study of their effect on topo II activity from Chinese hamster ovary AA8 cells. Because interference with the function of topo II to resolve DNA entanglement at the end of re…

Health Toxicology and MutagenesisFlavonoidAntineoplastic AgentsToxicologyTopoisomerase II InhibitorModels BiologicalPolyploidychemistry.chemical_compoundChromosome SegregationCricetinaeGeneticsTopoisomerase II InhibitorsAnimalsEndoreduplicationheterocyclic compoundsEnzyme InhibitorsLuteolinCells CulturedGenetics (clinical)Chromosome AberrationsFlavonoidsEnzyme Inhibitors/pharmacologychemistry.chemical_classificationbiologyTopoisomeraseChinese hamster ovary cellAntineoplastic Agents/adverse effectsDNA Topoisomerases Type IIchemistryBiochemistryDNA Damage/drug effectsFlavonoidbiology.proteinQuercetinDNA Topoisomerases Type II/metabolismTopoisomerase-II InhibitorChromosome Segregation/drug effectsQuercetinAntineoplastic Agents/pharmacologyLuteolinDNADNA DamageMutagenesis
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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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Acrylamide catalytically inhibits topoisomerase II in V79 cells.

2010

The vinyl monomer acrylamide is characterized by the presence of an alpha,beta-unsaturated carbonyl group that makes it reactive towards thiol, hydroxyl or amino groups and towards the nucleophilic centers in DNA. The ability of acrylamide to chemically modify protein thiols has prompted us to consider topoisomerase II as one possible target of acrylamide, since agents targeting protein sulfhydryl groups act as either catalytic inhibitors or poisons of topoisomerase II. Nuclear extracts from V79 Chinese hamster cells incubated with acrylamide reduced topoisomerase II activity as inferred by an inability to convert kinetoplast DNA to the decatenated form. Nuclear extracts incubated with acry…

ToxicologyCleavage (embryo)Cell LineColony-Forming Units AssayV79 cellchemistry.chemical_compoundCell Line TumorCricetinaemedicineAnimalsTopoisomerase II InhibitorsDNA CleavageEtoposideEtoposideNucleic Acid Synthesis Inhibitorschemistry.chemical_classificationCell NucleusAcrylamidebiologyTopoisomeraseDNA KinetoplastGeneral MedicineTopoisomerase IIAntineoplastic Agents PhytogenicSettore BIO/18 - GeneticaEnzymechemistryBiochemistryKinetoplastAcrylamidebiology.proteinTopoisomerase-II InhibitorDNAmedicine.drugToxicology in vitro : an international journal published in association with BIBRA
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Endoreduplication induced in cultured Chinese hamster cells by different anti-topoisomerase II chemicals

2005

With the ultimate purpose of testing the hypothesis that, as shown in yeast mutants, any malfunction of DNA topoisomerase II might result in aberrant mitosis due to defective chromosome segregation, we have chosen three chemicals of different nature, recently reported to catalytically inhibit the enzyme. The endpoint selected to assess any negative effect on the ability of topoisomerase II to properly carry out decatenation of fully replicated chromosomes in the G2/M phase of the cell cycle was the presence of metaphases showing diplochromosomes as a result of endoreduplication, i.e. two successive rounds of DNA replication without intervening mitosis. The anti-topoisomerase drugs selected …

biologyHealth Toxicology and MutagenesisTopoisomeraseDNA replicationCell cycleMolecular biologyCell biologyChromosome segregationchemistry.chemical_compoundchemistryGeneticsbiology.proteinEndoreduplicationTopoisomerase-II InhibitorMitosisDNAMutation Research/Genetic Toxicology and Environmental Mutagenesis
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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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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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