Search results for "Cell Cycle"

showing 10 items of 804 documents

Enhanced oxidative stress and increased mitochondrial mass during Efavirenz-induced apoptosis in human hepatic cells

2010

BACKGROUND AND PURPOSE Efavirenz (EFV) is widely used in the treatment of HIV-1 infection. Though highly efficient, there is growing concern about EFV-related side effects, the molecular basis of which remains elusive. EXPERIMENTAL APPROACH In vitro studies were performed to address the effect of clinically relevant concentrations of EFV (10, 25 and 50 mu M) on human hepatic cells. KEY RESULTS Cellular proliferation and viability were reduced in a concentration-dependent manner. Analyses of the cell cycle and several cell death parameters (chromatin condensation, phosphatidylserine exteriorization, mitochondrial proapoptotic protein translocation and caspase activation) revealed that EFV tr…

CyclopropanesMalehepatotoxicityCarcinoma HepatocellularTime FactorsAnti-HIV AgentsCell SurvivalApoptosisMitochondria LiverPhosphatidylserinesAntioxidantsSuperoxidesHumansChromansantiretroviral drugsCell Proliferationreactive oxygen speciesDose-Response Relationship DrugCell CycleLiver NeoplasmsChromatin Assembly and DisassemblyResearch PapersGlutathioneBenzoxazinesmitochondriaOxidative Stressside effectscell deathLiverAlkynesFemaleEfavirenzApoptosis Regulatory ProteinsHeLa Cells
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Glutathione is recruited into the nucleus in early phases of cell proliferation.

2007

We have studied the possible correlation between nuclear glutathione distribution and the progression of the cell cycle. The former was studied by confocal microscopy using 5-chloromethyl fluorescein diacetate and the latter by flow cytometry and protein expression of Id2 and p107. In proliferating cells, when 41% of them were in the S+G(2)/M phase of the cell cycle GSH was located mainly in the nucleus. When cells reached confluence (G(0)/G(1)) GSH was localized in the cytoplasm with a perinuclear distribution. The nucleus/cytoplasm fluorescence ratio for GSH reached a maximal mean value of 4.2 +/- 0.8 at 6 h after cell plating. A ratio higher than 2 was maintained during exponential cell …

CytoplasmCellActive Transport Cell NucleusRetinoblastoma-Like Protein p107BiologyBiochemistry3T3 cellsFlow cytometrychemistry.chemical_compoundMicemedicineAnimalsMolecular BiologyInhibitor of Differentiation Protein 2Cell NucleusMicroscopy Confocalmedicine.diagnostic_testCell growthCell CycleCell BiologyGlutathione3T3 CellsCell cycleFlow CytometryMolecular biologyGlutathioneCell biologymedicine.anatomical_structurechemistryGene Expression RegulationCytoplasmNucleusThe Journal of biological chemistry
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Translocation of cdk2 to the nucleus during G1-phase in PDGF-stimulated human fibroblasts.

1997

We studied the subcellular distribution of cdk2 in synchronized, PDGF-stimulated human fibroblasts (FH109). After contact inhibition and serum depletion, more than 95% of FH109 cells were arrested in G0/G1-phase. PDGF-AB led to a 16-fold increase in proliferation compared with untreated cells. Cell cycle progression was studied by flow cytometric analysis, [3H]thymidine incorporation, and phosphorylation of the retinoblastoma gene product, pRB. Using Western blot analysis after subcellular fractionation, we revealed that after PDGF stimulation the phosphorylated (Thr 160), i.e., activated, form of cdk2 (33 kDa) first appeared in the nucleus at late G1-phase and persisted throughout until to…

CytoplasmFluorescent Antibody TechniqueProtein Serine-Threonine KinasesmedicineCDC2-CDC28 KinasesHumansCells CulturedCell NucleusPlatelet-Derived Growth FactorbiologyKinaseCyclin-dependent kinase 2Cyclin-Dependent Kinase 2G1 PhaseContact inhibitionBiological TransportCell BiologyCell cycleFibroblastsMolecular biologyCyclin-Dependent KinasesCell biologyCell CompartmentationCytosolmedicine.anatomical_structurebiology.proteinCell fractionationNucleusPlatelet-derived growth factor receptorCyclin-Dependent Kinase-Activating KinaseExperimental cell research
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Dynamic intracellular survivin in oral squamous cell carcinoma: underlying molecular mechanism and potential as an early prognostic marker

2007

Survivin functions as an apoptosis inhibitor and a regulator of cell division in many tumours. The intracellular localization of survivin in tumours has been suggested as a prognostic marker. However, current reports are inconsistent and the underlying molecular mechanisms are not understood. The present study has examined the localization and prognostic value of nuclear and cytoplasmic survivin in the pre-therapeutic biopsies from 71 oral and oropharyngeal squamous carcinoma (OSCC) patients. Statistical analysis indicated that preferential nuclear versus cytoplasmic survivin correlated with favourable versus unfavourable disease outcome. Uni- and multi-variate analysis showed that in contr…

CytoplasmProgrammed cell deathPathologymedicine.medical_specialtySurvivinReceptors Cytoplasmic and NuclearApoptosisKaplan-Meier EstimateCysteine Proteinase InhibitorsKaryopherinsInhibitor of Apoptosis ProteinsPathology and Forensic MedicineCell Line TumorSurvivinBiomarkers TumorCarcinomaHumansMedicineNuclear export signalneoplasmsCell NucleusNuclear Export SignalsPredictive markerbusiness.industryCell cyclePrognosismedicine.diseaseImmunohistochemistryNeoplasm ProteinsSquamous carcinomaOropharyngeal NeoplasmsHead and Neck NeoplasmsApoptosisCarcinoma Squamous CellCancer researchMouth NeoplasmsbusinessMicrotubule-Associated ProteinsThe Journal of Pathology
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Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G 1 phase cell cycle regulatory proteins

1999

The DNA-binding subunit of replication factor C (RFCp140) plays an important role in both DNA replication and DNA repair. The mechanisms regulating activation of RFCp140 thereby controlling replication and cellular proliferation are largely unknown. We analyzed protein expression of RFCp140 during cell cycle progression and investigated the association of RFCp140 with cell cycle regulatory proteins in cell lines of various tissue origin and in primary hematopoietic cells. Western and Northern blot analyses of RFCp140 from synchronized cells showed downregulation of RFCp140 when cells enter a G0-like quiescent state and upregulation of RFCp140 in cycling cells. Translocation from the cytopla…

CytoplasmSaccharomyces cerevisiae ProteinsT-LymphocytesCyclin ACell Cycle ProteinsEukaryotic DNA replicationCell LineMinor Histocompatibility AntigensDNA replication factor CDT1MiceReplication factor CControl of chromosome duplicationDrug DiscoveryAnimalsHumansReplication Protein CGenetics (clinical)Cell NucleusHomeodomain ProteinsbiologyG1 PhaseS-phase-promoting factor3T3 CellsCell cycleMolecular biologyUp-RegulationCell biologyDNA-Binding ProteinsRepressor ProteinsProto-Oncogene Proteins c-bcl-2biology.proteinMolecular MedicineOrigin recognition complexJournal of Molecular Medicine
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Molecular basis of the functional distinction between Cln1 and Cln2 cyclins

2012

Cln1 and Cln2 are very similar but not identical cyclins. In this work, we tried to describe the molecular basis of the functional distinction between Cln1 and Cln2. We constructed chimeric cyclins containing different fragments of Cln1 and Cln2 and performed several functional analysis that make it possible to distinguish between Cln1 or Cln2. We identified that region between amino acids 225 and 299 of Cln2 is not only necessary but also sufficient to confer Cln2 specific functionality compared with Cln1. We also studied Cln1 and Cln2 subcellular localization identifying additional differences between them. Both cyclins are distributed between the nucleus and the cytoplasm, but Cln1 shows…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticBlotting WesternGenes FungalGenetic VectorsGreen Fluorescent ProteinsActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyReportCyclinsGene Expression Regulation FungalmedicineAmino Acid SequenceNuclear export signalMolecular BiologyPeptide sequenceCyclinKaryopherinCell Nucleuschemistry.chemical_classificationCell Cycle CheckpointsCell BiologySubcellular localizationCell nucleusmedicine.anatomical_structureBiochemistrychemistryCytoplasmNuclear transportCDC28 Protein Kinase S cerevisiaePlasmidsDevelopmental BiologyCell Cycle
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Cell Cycle Activation of the Swi6p Transcription Factor Is Linked to Nucleocytoplasmic Shuttling

2003

The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in the regulation of cell division. In the present work, we have characterized the function of the karyopherin Msn5p in the control of the cell cycle of Saccharomyces cerevisiae. Phenotypic analysis of the msn5 mutant revealed an increase in cell size and a functional interaction between Msn5p and the cell cycle transcription factor SBF (composed of the Swi4p and Swi6p proteins), indicating that Msn5p is involved in Start control. In fact, we have shown that the level of Cln2p protein is drastically reduced in an msn5 mutant. The effect on CLN2 expression is mediated at a transcriptional …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticCell divisionChromosomal Proteins Non-HistoneActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyDNA-binding proteinCyclinsGene Expression Regulation FungalmedicineCell Growth and DevelopmentMolecular BiologyTranscription factorKaryopherinCell Nucleuschemistry.chemical_classificationCell CycleCell BiologyCell cycleSubcellular localizationCell biologyDNA-Binding ProteinsCell nucleusmedicine.anatomical_structurechemistryCytoplasmMutationCarrier ProteinsTranscription FactorsMolecular and Cellular Biology
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Cutting edge: priming of CTL by transcutaneous peptide immunization with imiquimod.

2005

Abstract CTL are important in combating cancer and viruses. Therefore, triggering the complete potential of CTL effector functions by new vaccination strategies will not only improve prophylaxis of tumor or virus-related diseases, but also open opportunities for effective therapeutic immunizations. Using transcutaneous immunization, we show that epicutaneous (e.c.)4 application of an ointment containing a CTL epitope and the TLR7 ligand imiquimod is highly effective in activating T cells in mice using TCR-transgenic CTL or in wild-type mice. Transcutaneous immunization-activated CTL mount a full-blown immune response against the target epitope characterized by proliferation, cytolytic activ…

Cytotoxicity ImmunologicAdoptive cell transferImmunologyReceptors Antigen T-CellPriming (immunology)Epitopes T-Lymphocytechemical and pharmacologic phenomenaImiquimodMice TransgenicAdministration CutaneousLymphocyte ActivationResting Phase Cell CycleEpitopeMiceImmune systemmedicineImmunology and AllergyAnimalsCells CulturedMice KnockoutImiquimodbusiness.industryTLR7VirologyAdoptive TransferVaccinationMice Inbred C57BLCTL*Protein TransportImmunologyVaccines SubunitAminoquinolinesLymph NodesbusinessSpleenmedicine.drugT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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Compromised repair of radiation-induced DNA double-strand breaks in Fanconi anemia fibroblasts in G2

2020

Fanconi anemia (FA) is a rare chromosomal instability syndrome with various clinical features and high cancer incidence. Despite being a DNA repair disorder syndrome and a frequently observed clinical hypersensitivity of FA patients towards ionizing radiation, the experimental evidence regarding the efficiency of radiation-induced DNA double-strand break (DSB) repair in FA is very controversial. Here, we performed a thorough analysis of the repair of radiation-induced DSBs in G1 and G2 in FA fibroblasts of complementation groups A, C, D1 (BRCA2), D2, E, F, G and P (SLX4) in comparison to normal human lung and skin fibroblasts. γH2AX, 53BP1, or RPA foci quantification after X-irradiation was…

DNA End-Joining RepairBiologyBiochemistryFanconi Anemia Complementation Group F ProteinHistonesRecombinases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineFanconi anemiaChromosome instabilitymedicineHumansDNA Breaks Double-StrandedFanconi Anemia Complementation Group G ProteinMolecular BiologyCells Cultured030304 developmental biologyBRCA2 ProteinChromosome Aberrations0303 health sciencesFanconi Anemia Complementation Group A ProteinFanconi Anemia Complementation Group D2 ProteinX-RaysCell CycleFanconi Anemia Complementation Group C ProteinRecombinational DNA RepairChromosomeDNACell BiologyFibroblastsCell cyclemedicine.diseaseFanconi Anemia Complementation Group E ProteinComplementationKineticsenzymes and coenzymes (carbohydrates)Fanconi Anemiachemistry030220 oncology & carcinogenesisPremature chromosome condensationMutationCancer researchChromatidTumor Suppressor p53-Binding Protein 1DNADNA Repair
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