Search results for "Mitosis."

showing 10 items of 146 documents

Inhibitory effect of resveratrol on the proliferation of human and rat hepatic derived cell lines.

2000

Resveratrol is a polyphenolic compound especially produced by grapevine and consequently found in wine. Based on epidemiological studies resveratrol may act as a cancer chemopreventive compound. The ability of resveratrol to inhibit cell proliferation was studied in rat hepatoma Fao cell line and human hepatoblastoma HepG2 cell line. The results show that resveratrol strongly inhibits cell proliferation at the micromolar range in a time- and dose-dependent manner. Concentrations higher than 50 microM become toxic. Fao cells are more sensitive than HepG2 cells. Interestingly, the presence of ethanol lowers the threshold of resveratrol effect. Resveratrol appears to prevent or to delay the en…

HepatoblastomaCancer Researchendocrine system diseasesCell SurvivalCellMitosisResveratrolBiologyPharmacologychemistry.chemical_compoundLiver Neoplasms ExperimentalStilbenesmedicineTumor Cells CulturedAnimalsHumansMitosisCell growthorganic chemicalsCell CycleLiver Neoplasmsfood and beveragesGeneral MedicineCell cycleAntineoplastic Agents PhytogenicCell biologyRatsmedicine.anatomical_structureOncologychemistryApoptosisCell cultureResveratrolHepatic stellate cellCell DivisionOncology reports
researchProduct

Sequence of lethal events in HeLa cells exposed to the G2 blocking cytolethal distending toxin

2000

The bacterial cytolethal distending toxin (CDT) was previously shown to block the cell cycle of several cell lines at stage G2 through inactivation of the cyclin-dependent kinase Cdkl and without induction of DNA strand breaks. In the present study, we have analyzed, using various methods of analytical cytometry, the progressive transformation and delayed lethal events in the tumor-derived HeLa cell line temporarily exposed to CDT. The cell proliferation arrest induced by CDT was irreversible but, starting about two days after exposure, the G2 block released partially, concomitantly with a decline in the level of Cdkl phosphorylation. This partial release resulted in endoreduplication, lead…

HistologyTime FactorsCytolethal distending toxinCell divisionAntimetabolitesCell Survival[SDV]Life Sciences [q-bio]Bacterial ToxinsMitosisApoptosisKINASE CYCLIQUE DEPENDANTEBiologyCyclin BPathology and Forensic MedicineCDC2 Protein KinaseEndoreduplicationHumansCyclin B1PhosphorylationMitosisCentrosomeCell DeathCell growthCell BiologyGeneral MedicineCell cycleFlow CytometryVirologyMolecular biologyImmunohistochemistry[SDV] Life Sciences [q-bio]BromodeoxyuridineMicroscopy FluorescenceCell cultureApoptosisCell DivisionHeLa Cells
researchProduct

In vivo detection of cytokeratin filament network breakdown in cells treated with the phosphatase inhibitor okadaic acid.

2001

We have previously described vulva carcinoma-derived A-431 subclone AK13-1, which stably expresses fluorescently labeled cytokeratin filaments (CKFs). Time-lapse fluorescence microscopy of these cells permits the continuous monitoring of the dynamics of the CKF cytoskeleton in vivo. To study mechanisms and principles of CKF disassembly as it occurs, e.g., during mitosis and liver disease, we have treated cells with the phosphatase inhibitor okadaic acid (OA), which induces complete CKF network breakdown within 3–5 h without significantly affecting the organization of the actin- and tubulin-based cytofilaments. In time-lapse movies, we find that the network breakdown starts at the cell perip…

HistologyTime FactorsRecombinant Fusion ProteinsGreen Fluorescent ProteinsPathology and Forensic Medicinechemistry.chemical_compoundCytokeratinAdenosine TriphosphateStress FibersOkadaic AcidFluorescence microscopeTumor Cells CulturedHumansEnzyme InhibitorsPhosphorylationCytoskeletonMitosisActinCytoskeletonbiologyVulvar NeoplasmsEpithelial CellsCell BiologyOkadaic acidCell biologyCytoskeletal ProteinsLuminescent ProteinsTubulinchemistryDesmoplakinsMicroscopy FluorescenceCytoplasmbiology.proteinKeratinsFemaleIndicators and ReagentsCell and tissue research
researchProduct

Transformation of the dermatophyte Trichophyton mentagrophytes to hygromycin B resistance.

1989

A transformation system for the ringworm-producing dermatophyte Trichophyton mentagrophytes has been developed. The system employs the plasmid pHIS, which contains a bacterial hygromycin B phosphotransferase gene linked to Cochliobolus heterostrophus regulatory sequences (B. G. Turgeon, R. C. Garber, and O. C. Yoder, Mol. Cell. Biol. 7:3297-3305, 1987). This plasmid confers hygromycin B resistance to T. mentagrophytes. The DNA was stably integrated into the fungal genome, and the number and sites of integrations varied among transformants. Transformant clones were capable of infecting guinea pigs. This system opens the way for the molecular genetic analysis of the interaction of T. mentagro…

ImmunologyGuinea PigsVirulenceMitosisCochliobolus heterostrophusmedicine.disease_causeMicrobiologyMicrobiologychemistry.chemical_compoundPlasmidTransformation GeneticTrichophytonmedicineAnimalsTrichophytonGenebiologyVirulenceDrug Resistance Microbialbiology.organism_classificationGrowth InhibitorsAnti-Bacterial AgentsTransformation (genetics)Blotting SouthernInfectious DiseaseschemistryDermatophyteParasitologyHygromycin BHygromycin BResearch ArticleInfection and immunity
researchProduct

Genome size and chromosomes in marine sponges [Suberites domuncula, Geodia cydonium]

1995

The genome size of the marine sponges Suberites domuncula and Geodia cydonium has been determined by flow cytofluorometric analysis using diamidino-phenylindole [DAPI]. Using human lymphocytes as reference the amount of DNA in cells from S. domuncula has been determined to be 3.7 pg and that of G. cydonium 3.3 pg. While no chromosomes could be identified in G. cydonium, the karyotype of the Suberites domuncula is 32 chromosomes in the diploid state. The size of the chromosomes was between 0.25 and 1.0 micron. No pronounced banding pattern was visible.

IndolesMitosisProphaseGenomeChromosomesMicrobiologychemistry.chemical_compoundProphaseAnimalsMitosisGenome sizeFluorescent DyesGenomebiologyKaryotypeDNACell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSuberites domunculachemistryKaryotypingPloidyDNACell Biology International
researchProduct

Synthesis and evaluation of microtubule assembly inhibition and cytotoxicity of prenylated derivatives of cyclo-l-Trp-l-Pro

2000

The synthesis of three isoprenylated derivatives of cyclo-L-Trp-L-Pro is described. These substances have been evaluated for cytotoxic activity in rat normal fibroblast 3Y1 cells and have also been evaluated in vitro for the inhibition of microtubule assembly.

IndolesStereochemistryClinical BiochemistryProtein PrenylationMitosisPharmaceutical ScienceMicrotubulesPeptides CyclicBiochemistryChemical synthesisPiperazinesIndole AlkaloidsMicrotubuleDrug DiscoverymedicineAnimalsFibroblastCytotoxicityMolecular BiologyCells Culturedchemistry.chemical_classificationMolecular StructureChemistryOrganic ChemistryBiological activityFibroblastsIn vitroCyclic peptideRatsmedicine.anatomical_structureBiochemistryCell cultureMolecular MedicineCattleMicrotubule-Associated ProteinsBioorganic & Medicinal Chemistry
researchProduct

p38 MAPK-dependent shaping of the keratin cytoskeleton in cultured cells

2007

Plasticity of the resilient keratin intermediate filament cytoskeleton is an important prerequisite for epithelial tissue homeostasis. Here, the contribution of stress-activated p38 MAPK to keratin network organization was examined in cultured cells. It was observed that phosphorylated p38 colocalized with keratin granules that were rapidly formed in response to orthovanadate. The same p38p recruitment was noted during mitosis, in various stress situations and in cells producing mutant keratins. In all these situations keratin 8 became phosphorylated on S73, a well-known p38 target site. To demonstrate that p38-dependent keratin phosphorylation determines keratin organization, p38 activity …

MAP Kinase Signaling SystemIntermediate filament cytoskeletonmacromolecular substancesBiologyp38 Mitogen-Activated Protein KinasesArticleKeratinHumansPhosphorylationCytoskeletonProtein Kinase InhibitorsMitosisResearch ArticlesCells CulturedCytoskeletonchemistry.chemical_classificationKeratin Filamentintegumentary systemCell BiologyCell biologyKeratin 5chemistryKeratin 8KeratinsPhosphorylationVanadatesJournal of Cell Biology
researchProduct

A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.

2011

http://linkinghub.elsevier.com/; International audience; Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. …

MESH : Molecular Sequence Data[SDV]Life Sciences [q-bio]CellMESH: Cell CycleMESH: Amino Acid SequenceAmino Acid Sequence; Cell Cycle; Cell Membrane/metabolism; Microtubule-Associated Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/metabolism; Schizosaccharomyces/cytology; Schizosaccharomyces/metabolism; Schizosaccharomyces pombe Proteins/metabolism; Sequence AlignmentMESH : Phosphorylation0302 clinical medicinePhosphorylation0303 health sciencesKinaseMESH : Amino Acid SequenceMESH : Sequence AlignmentCell CycleCortical gradientMESH : Schizosaccharomyces pombe ProteinsFission yeastCell biologymedicine.anatomical_structureMESH: SchizosaccharomycesPom1PhosphorylationMicrotubule-Associated ProteinsMESH : Cell MembraneMolecular Sequence DataMESH: Sequence AlignmentMESH : Protein KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyPom1Dephosphorylation03 medical and health sciencesMicrotubuleMESH : Cell CycleSchizosaccharomycesCell cortexmedicineAmino Acid SequenceMitosisMESH: Protein Kinases030304 developmental biologyMESH: Molecular Sequence Data[ SDV ] Life Sciences [q-bio]Phosphorylation cycleMESH: PhosphorylationBiochemistry Genetics and Molecular Biology(all)Cell MembraneMESH: Schizosaccharomyces pombe ProteinsMESH: Microtubule-Associated ProteinsMESH : SchizosaccharomycesMESH : Microtubule-Associated ProteinsSchizosaccharomyces pombe ProteinsDYRK family kinaseProtein KinasesSequence Alignment030217 neurology & neurosurgeryMESH: Cell Membrane
researchProduct

Keratinocyte-Derived Granulocyte-Macrophage Colony Stimulating Factor Accelerates Wound Healing: Stimulation of Keratinocyte Proliferation, Granulati…

2001

Chronic, nonhealing wounds represent a major clinical challenge to practically all disciplines in modern medicine including dermatology, oncology, surgery, and hematology. In skin wounds, granulocyte-macrophage colony stimulating factor (GM-CSF) is secreted by keratinocytes shortly after injury and mediates epidermal cell proliferation in an autocrine manner. Many other cells involved in wound healing including macrophages, lymphocytes, fibroblasts, endothelial cells, and dendritic cells synthesize GM-CSF and/or are targets of this cytokine. Therefore, GM-CSF is a pleiotropic cytokine evoking complex processes during wound repair. Despite this complexity and the scarcity of mechanistic unde…

Macrophage colony-stimulating factorKeratinocytesMalemedicine.medical_treatmentGene ExpressionMitosisNeovascularization PhysiologicMice TransgenicDermatologytransgenic miceBiologyBiochemistryProinflammatory cytokineTransforming Growth Factor beta1MiceTransforming Growth Factor betamedicineAnimalsRNA MessengerAutocrine signallingMolecular BiologySkinWound Healingintegumentary systemGranulation tissueGranulocyte-Macrophage Colony-Stimulating FactorGM-CSFCell BiologyUp-RegulationCytokinemedicine.anatomical_structureGranulocyte macrophage colony-stimulating factorImmunologyModels AnimalCancer researchCarcinogensGranulation TissueCytokinesTetradecanoylphorbol AcetateFemaleKeratinocyteWound healingmedicine.drugJournal of Investigative Dermatology
researchProduct

p14(ARF) Prevents Proliferation of Aneuploid Cells by Inducing p53-Dependent Apoptosis.

2014

Weakening the Spindle Assembly Checkpoint by reduced expression of its components induces chromosome instability and aneuploidy that are hallmarks of cancer cells. The tumor suppressor p14(ARF) is overexpressed in response to oncogenic stimuli to stabilize p53 halting cell progression. Previously, we found that lack or reduced expression of p14(ARF) is involved in the maintenance of aneuploid cells in primary human cells, suggesting that it could be part of a pathway controlling their proliferation. To investigate this aspect further, p14(ARF) was ectopically expressed in HCT116 cells after depletion of the Spindle Assembly Checkpoint MAD2 protein that was used as a trigger for aneuploidy. …

Mad2 ProteinApoptosis; M Phase Cell Cycle Checkpoints; Mad2 Proteins; RNA Interference; Tumor Suppressor Protein p14ARF; AneuploidyApoptosiMitosisApoptosisM Phase Cell Cycle CheckpointAneuploidyHCT116 CellsSettore BIO/18 - GeneticaGene Knockout TechniquesMad2 ProteinsTumor Suppressor Protein p14ARFHumansM Phase Cell Cycle CheckpointsRNA InterferenceTumor Suppressor Protein p53Cell ProliferationJournal of cellular physiology
researchProduct