Search results for "dam"

showing 10 items of 3828 documents

The in vitro metabolic activation of dibenz[a,h]anthracene, catalyzed by by rat liver microsomes and examined by 32P-postlabelling.

1991

DNA has been incubated in vitro with dibenz[a,h]anthracene (DB[a,H]A) and the related 5,6-diol and 3,4-diol in the presence of 3-methylcholanthrene- or Aroclor 1254-induced rat liver microsomes. After incubation, the DNA was extracted and examined for the presence of aromatic adducts using the nuclease P1 modification of the 32P-postlabelling technique. The maps of PEI-cellulose plates and autoradiography showed that 92% of the radioactivity contained in DB[a,h]A-DNA adduct spots is derived from the related 3,4-diol and that about 50% of the adducts may be formed following the conversion of this diol to the bay-region anti- and syn-3,4-diol 1,2-oxides.

Cancer ResearchAroclorsDNA damageDiolIn Vitro TechniquesAdductchemistry.chemical_compoundpolycyclic compoundsBenz(a)AnthracenesDibenz(ah)anthraceneAnimalsheterocyclic compoundsCarcinogenBiotransformationAnthraceneChromatographyintegumentary systemorganic chemicalsRatsOncologychemistryBiochemistryMethylcholanthreneMicrosomeMicrosomes LiverEpoxy CompoundsDNA DamageMethylcholanthreneCancer letters
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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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Ionizing radiation but not anticancer drugs causes cell cycle arrest and failure to activate the mitochondrial death pathway in MCF-7 breast carcinom…

2001

There is considerable evidence that ionizing radiation (IR) and chemotherapeutic drugs mediate apoptosis through the intrinsic death pathway via the release of mitochondrial cytochrome c and activation of caspases -9 and -3. Here we show that MCF-7 cells that lack caspase-3 undergo a caspase-dependent apoptotic cell death in the absence of DNA fragmentation and alpha-fodrin cleavage following treatment with etoposide or doxorubicin, but not after exposure to IR. Re-expression of caspase-3 restored DNA fragmentation and alpha-fodrin cleavage following drug treatment, but it did not alter the radiation-resistant phenotype of these cells. In contrast to the anticancer drugs, IR failed to induc…

Cancer ResearchCell cycle checkpointAntineoplastic AgentsApoptosisBreast NeoplasmsDNA FragmentationMitochondrionHeLaTransformation GeneticRadiation IonizingGeneticsTumor Cells CulturedHumansMolecular BiologyCaspaseEtoposidebiologyCaspase 3CarcinomaCell CycleMicrofilament ProteinsDNA NeoplasmCell cyclebiology.organism_classificationCaspase 9MitochondriaApoptosisCell cultureDoxorubicinCaspasesImmunologyCancer researchbiology.proteinDNA fragmentationFemaleCarrier ProteinsDNA DamageHeLa CellsOncogene
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Abstract 4662: Shikonin causes cancer cell death by inducing mitochondrial dysfunction

2012

Abstract Shikonin, a naturally occurring napthoquinone, has been used in herbal formulations for the treatment of several inflammatory diseases in Traditional Chinese Medicine since decades. In recent studies, shikonin revealed remarkable anticancer activities and thereby is a promising candidate for cancer chemotherapy. However, the underlying cellular mechanisms and targets of shikonin are still unknown. Here, we showed that shikonin indeed exhibits strong cytotoxic effects on a panel of 15 different cancer cell lines also containing multi-drug resistant cells. The strongest effects were obtained on U937 leukemia cells. To better understand the underlying mechanisms, we performed a whole …

Cancer ResearchCell cycle checkpointDNA damageRespiratory chainCancerCaspase 3BiologyMitochondrionmedicine.diseaseOncologyApoptosisCancer cellBotanymedicineCancer researchCancer Research
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Influence of nitric oxide on the generation and repair of oxidative DNA damage in mammalian cells

2002

We have analysed the effects of endogenously and exogenously generated nitric oxide (NO) in cultured mammalian fibroblasts on: (i) the steady-state (background) levels of oxidative DNA base modifications; (ii) the susceptibility of the cells to the induction of additional DNA damage and micronuclei by H(2)O(2); and (iii) the repair kinetics of various types of DNA modifications. Steady-state levels of oxidative DNA base modifications, measured by means of an alkaline elution assay in combination with the repair endonuclease Fpg protein, were similar in NO-overproducing B6 mouse fibroblasts stably transfected with an inducible NO synthase (iNOS) and in control cells. Increased oxidative dama…

Cancer ResearchDNA RepairDNA damageDNA repairNitric Oxide Synthase Type IIMutagenAlkenesBiologyNitric OxideTransfectionmedicine.disease_causeMicechemistry.chemical_compoundmedicineAnimalsNitric Oxide DonorsDose-Response Relationship DrugHydrogen PeroxideGeneral MedicineTransfectionFibroblastsCell biologyBiochemistrychemistryNitric Oxide SynthaseDNAGenotoxicityPeroxynitriteOxidative stressDNA DamageCarcinogenesis
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R-Roscovitine (Seliciclib) prevents DNA damage-induced cyclin A1 upregulation and hinders non-homologous end-joining (NHEJ) DNA repair.

2010

Abstract Background CDK-inhibitors can diminish transcriptional levels of cell cycle-related cyclins through the inhibition of E2F family members and CDK7 and 9. Cyclin A1, an E2F-independent cyclin, is strongly upregulated under genotoxic conditions and functionally was shown to increase NHEJ activity. Cyclin A1 outcompetes with cyclin A2 for CDK2 binding, possibly redirecting its activity towards DNA repair. To see if we could therapeutically block this switch, we analyzed the effects of the CDK-inhibitor R-Roscovitine on the expression levels of cyclin A1 under genotoxic stress and observed subsequent DNA damage and repair mechanisms. Results We found that R-Roscovitine alone was unable …

Cancer ResearchDNA RepairDNA repairDNA damageSettore MED/06 - Oncologia MedicaCyclin DCyclin ACyclin BSettore BIO/11 - Biologia Molecolarelcsh:RC254-282RoscovitineProtein Kinase InhibitorsBIO/10 Biochimicaroscovitine doxorubicinbiologyResearchCyclin A1; Doxorubicin; Protein Kinase Inhibitors; Purines; Up-Regulation; DNA Damage; DNA Repair; Hydrogen-Ion Concentration; Cancer Research; Molecular Medicine; OncologyG2-M DNA damage checkpointHydrogen-Ion Concentrationlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensUp-RegulationOncologyDoxorubicinPurinesCancer researchbiology.proteinMolecular MedicineCyclin A1biological phenomena cell phenomena and immunityCyclin A1Cyclin A2DNA DamageMolecular cancer
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Ultraviolet light-induced DNA damage triggers apoptosis in nucleotide excision repair-deficient cells via Bcl-2 decline and caspase-3/-8 activation.

2001

Ultraviolet (UV) light is a potent mutagenic and genotoxic agent. Whereas DNA damage induced by UV light is known to be responsible for UV-induced genotoxicity, its role in triggering apoptosis is still unclear. We addressed this issue by comparing nucleotide excision repair (NER) deficient 27-1 and 43-3B Chinese hamster (CHO) cells with the corresponding wild-type and ERCC-1 complemented cells. It is shown that NER deficient cells are dramatically hypersensitive to UV-C induced apoptosis, indicating that DNA damage is the major stimulus for the apoptotic response. Apoptosis triggered by UV-C induced DNA damage is related to caspase- and proteosome-dependent degradation of Bcl-2 protein. Th…

Cancer ResearchDNA RepairDNA repairDNA damageUltraviolet RaysPoly ADP ribose polymeraseFas-Associated Death Domain ProteinApoptosisCHO CellsBiologyCysteine Proteinase InhibitorsCaspase 8TransfectionFas ligandMembrane PotentialsCricetinaeGeneticsUltraviolet lightAnimalsRNA MessengerMolecular BiologyAdaptor Proteins Signal TransducingCaspase 8Caspase 3Fas receptorMolecular biologyCaspase InhibitorsCaspase 9MitochondriaEnzyme ActivationProto-Oncogene Proteins c-bcl-2CaspasesPoly(ADP-ribose) PolymerasesCarrier ProteinsNucleotide excision repairDNA DamageOncogene
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Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1

1999

The DNA repair protein apurinic endonuclease (APE/Ref-1) exerts several physiological functions such as cleavage of apurinic/apyrimidinic sites and redox regulation of the transcription factor AP-1, whose activation is part of the cellular response to DNA damaging treatments. Here we demonstrate that APE/Ref-1 is phosphorylated by casein kinase II (CKII). This was shown for both the recombinant APE/Ref-1 protein (Km=0.55 mM) and for APE/Ref-1 expressed in COS cells. Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1. Inhibition of CKII mediated phosphorylation of A…

Cancer ResearchDNA RepairProto-Oncogene Proteins c-junDNA repairDNA damageCarbon-Oxygen LyasesCHO CellsProtein Serine-Threonine KinasesBiologyTransfectionSubstrate SpecificityCricetinaeDNA Repair ProteinDNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsAnimalsHumansAP sitePhosphorylationCasein Kinase IIProtein kinase AMolecular BiologyMethyl MethanesulfonateCyclic AMP-Dependent Protein KinasesMolecular biologyDNA-(apurinic or apyrimidinic site) lyaseTranscription Factor AP-1COS CellsPhosphorylationCasein kinase 2Oxidation-ReductionDNA DamageHeLa CellsMutagensOncogene
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The DNA damage-induced decrease of Bcl-2 is secondary to the activation of apoptotic effector caspases.

2003

Apoptosis induced by DNA-damaging agents or radiation mainly proceeds through death receptor-independent caspase activation. The release of mitochondrial apoptogenic proteins, such as cytochrome c, into the cytoplasm leading to Apaf1-dependent activation of caspase-9 is a key event in this pathway. The permeability of the mitochondrial outer membrane is regulated by the various pro- and antiapoptotic Bcl-2 family proteins, and it is thought that DNA damage triggers apoptosis through the downregulation of antiapoptotic Bcl-2. Using murine embryonic fibroblasts (MEF) deficient and proficient in Apaf1, we show that DNA-damaging agents and radiation lead to a decline in Bcl-2 protein only in wt…

Cancer ResearchDNA damageCell TransplantationUltraviolet RaysTransplantation HeterologousApoptosisMice SCIDAdenocarcinomamedicine.disease_causeAdenoviridaeAmino Acid Chloromethyl KetonesMiceDownregulation and upregulationGeneticsmedicineTumor Cells CulturedAnimalsHumansAPAF1Enzyme InhibitorsMolecular BiologyCaspaseEtoposidebiologyDose-Response Relationship DrugCytochrome cProteinsDose-Response Relationship RadiationFibroblastsMolecular biologyCaspase InhibitorsCell biologyEnzyme ActivationPancreatic NeoplasmsApoptotic Protease-Activating Factor 1Proto-Oncogene Proteins c-bcl-2ApoptosisCytoplasmCaspasesbiology.proteinDactinomycinCarcinogenesisGene DeletionDNA DamageOncogene
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Spontaneous mutagenesis in Csb(m/m)Ogg1⁻(/)⁻ mice is attenuated by dietary resveratrol.

2010

Oxidative DNA modifications such as 7,8-dihydro-8-oxoguanine (8-oxoG) are generated endogenously in apparently all living cells. The defect of the repair of 8-oxoG in Csb m/m Ogg1 ―/― mice results in elevated basal levels of these lesions and increased frequencies of spontaneous mutations, which initiate tumorigenesis in the liver if cell proliferation is stimulated. Here, we describe that the phytoalexin resveratrol, applied either for 7 days per gavage (100 mg/kg body wt) or for 3―9 months in the diet (0.04% ad libitum), reduces the endogenous oxidative DNA base damage in the livers of the Csb m/m Ogg1 ―/― mice by 20―30% (P < 0.01). A small but consistent effect is also observed in the wi…

Cancer ResearchDNA damageSOD1SOD2Gene ExpressionMice TransgenicBiologyResveratrolSuperoxide dismutasechemistry.chemical_compoundMiceStilbenesAnimalschemistry.chemical_classificationReverse Transcriptase Polymerase Chain ReactionGlutathione peroxidaseMutagenesisAntimutagenic AgentsGeneral MedicineMolecular biologyDietOxidative StressCell killingchemistryBiochemistryLiverMutagenesisResveratrolbiology.proteinDNA DamageCarcinogenesis
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