Search results for "TERT"

showing 10 items of 1210 documents

Chromatin Domains and Regulation of Transcription

2007

Compartmentalization and compaction of DNA in the nucleus is the characteristic feature of eukaryotic cells. A fully extended DNA molecule has to be compacted 100,000 times to fit within the nucleus. At the same time it is critical that various DNA regions remain accessible for interaction with regulatory factors and transcription/replication factories. This puzzle is solved at the level of DNA packaging in chromatin that occurs in several steps: rolling of DNA onto nucleosomes, compaction of nucleosome fiber with formation of the so-called 30 nm fiber, and folding of the latter into the giant (50-200 kbp) loops, fixed onto the protein skeleton, the nuclear matrix. The general assumption is…

Cell NucleusGeneticsTranscriptionally active chromatinProtein FoldingTranscription GeneticDNABiologyChromatinChromatin remodelingNucleosomesProtein Structure TertiaryChromatinChIP-sequencingCell biologyHistonesGene Expression RegulationStructural BiologyAnimalsHumansHistone codeNucleosomeScaffold/matrix attachment regionMolecular BiologyChIA-PETJournal of Molecular Biology
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A novel moniliformin derivative as pan-inhibitor of histone deacetylases triggering apoptosis of leukemia cells

2021

New and potent agents that evade multidrug resistance (MDR) and inhibit epigenetic modifications are of great interest in cancer drug development. Here, we describe that a moniliformin derivative (IUPAC name: 3-(naphthalen-2-ylsulfanyl)-4-{[(2Z)-1,3,3-trimethyl-2,3-dihydro-1H-indol-2-ylidene]methyl}cyclobut-3-ene-1,2-dione; code: MCC1381) bypasses P-gp-mediated MDR. Using transcriptomics, we identified a large number of genes significantly regulated in response to MCC1381, which affected the cell cycle and disturbed cellular death and survival. The potential targets of MCC1381 might be histone deacetylases (HDACs) as predicted by SwissTargetPrediction. In silico studies confirmed that MCC13…

Cell SurvivalApoptosisBiochemistryHistone DeacetylasesProtein Structure SecondaryAnimalsHumansEpigeneticsZebrafishP-glycoproteinPharmacologyLeukemiaDose-Response Relationship DrugbiologyChemistryMycotoxinsCell cycleHDAC6HCT116 CellsXenograft Model Antitumor AssaysProtein Structure TertiaryCell biologyHistone Deacetylase InhibitorsMolecular Docking SimulationHEK293 CellsHistoneAcetylationApoptosisCancer cellbiology.proteinCyclobutanesBiochemical Pharmacology
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Identification of new P-glycoprotein inhibitors derived from cardiotonic steroids

2014

P-glycoprotein (ABCB1, MDR1) is capable of extruding chemotherapeutics outside the cell and its overexpression in certain cancer cells may cause failure of chemotherapy. Many attempts were carried out to identify potent inhibitors of this transporter and numerous compounds were shown to exert inhibitory effects in vitro, but so far none were able to make their way to the clinic due to serious complications. Natural compounds represent a great source of therapeutics, which are believed to be safe and effective. Therefore, we have screened a large library of naturally occurring cardiotonic steroids and their derivatives using high throughput flow cytometry. We were able to identify six compou…

Cell SurvivalHigh-throughput screeningIn silicoPharmacologyBiochemistryProtein Structure SecondaryCell LineFlow cytometryCardiac Glycosideschemistry.chemical_compoundmedicineHumansATP Binding Cassette Transporter Subfamily B Member 1P-glycoproteinPharmacologyDose-Response Relationship Drugbiologymedicine.diagnostic_testResazurinmedicine.diseaseIn vitroProtein Structure TertiaryLeukemiachemistryDoxorubicinCancer cellbiology.proteinBiochemical Pharmacology
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Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protei…

2008

Recent studies provide evidence that wild-type Cu/Zn-superoxide dismutase (SOD1(hWT)) might be an important factor in mutant SOD1-mediated amyotrophic lateral sclerosis (ALS). In order to investigate its functional role in the pathogenesis of ALS, we designed fusion proteins of two SOD1 monomers linked by a polypeptide. We demonstrated that wild-type-like mutants, but not SOD1(G85R) homodimers, as well as mutant heterodimers including SOD1(G85R)-SOD1(hWT) display dismutase activity. Mutant homodimers showed an increased aggregation compared with the corresponding heterodimers in cell cultures and transgenic Caenorhabditis elegans, although SOD1(G85R) heterodimers are more toxic in functiona…

Cell SurvivalRecombinant Fusion Proteinsanimal diseasesSOD1MutantProtein aggregationAnimals Genetically ModifiedProtein CarbonylationSuperoxide dismutaseMicechemistry.chemical_compoundSuperoxide Dismutase-1Cell Line TumorGeneticsAnimalsHumansAmino Acid SequenceCaenorhabditis elegansMolecular BiologyGenetics (clinical)Motor NeuronsbiologySuperoxide DismutaseSuperoxideAmyotrophic Lateral SclerosisWild typenutritional and metabolic diseasesHydrogen PeroxideGeneral MedicineFusion proteinProtein Structure Tertiarynervous system diseasesCell biologyAmino Acid Substitutionnervous systemchemistryBiochemistrybiology.proteinDismutaseDimerizationHuman Molecular Genetics
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Synthesis and biological evaluation of a D-ring-contracted analogue of lamellarin D

2017

A D-ring contracted analogue of the strongly cytotoxic marine pyrrole alkaloid lamellarin D was synthesized and investigated for its antiproliferative action towards a wild type and a multidrug resistant (MDR) cancer cell line. The compound was found to inhibit tumor cell growth at submicromolar concentrations and showed a lower relative resistance in the MDR cell line than the antitumor drug camptothecin to which lamellarin D shows cross resistance and with which lamellarin D shares the same binding site.

Cell SurvivalStereochemistryClinical BiochemistryPharmaceutical ScienceAntineoplastic Agents010402 general chemistryHeterocyclic Compounds 4 or More Rings01 natural sciencesBiochemistrychemistry.chemical_compoundCoumarinsCell Line TumorDrug DiscoverymedicineHumansCytotoxic T cellheterocyclic compoundsBinding siteMolecular BiologyBinding Sites010405 organic chemistryChemistryAlkaloidOrganic ChemistryWild typeIsoquinolinesProtein Structure Tertiary0104 chemical sciencesG2 Phase Cell Cycle CheckpointsMolecular Docking SimulationMultiple drug resistanceDNA Topoisomerases Type IDrug Resistance NeoplasmMutagenesisCell cultureLamellarin DM Phase Cell Cycle CheckpointsMolecular MedicineTopoisomerase I InhibitorsCamptothecinmedicine.drugBioorganic & Medicinal Chemistry
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Multiparametric evaluation of the cytoprotective effect of the Mangifera indica L. stem bark extract and mangiferin in HepG2 cells.

2012

Abstract Objective Mango (Mangifera indica L.) stem bark extract (MSBE) is a natural product with biological properties and mangiferin is the major component. This paper reported the evaluation of the protective effects of MSBE and mangiferin against the toxicity induced in HepG2 cells by tert-butyl hydroperoxide or amiodarone. Method Nuclear morphology, cell viability, intracellular calcium concentration and reactive oxygen species (ROS) production were measured by using a high-content screening multiparametric assay. Key findings MSBE and mangiferin produced no toxicity below 500 mg/ml doses. A marked recovery in cell viability, which was reduced by the toxicants, was observed in cells pr…

Cell SurvivalXanthonesPharmaceutical ScienceAmiodaronePharmacologychemistry.chemical_compoundtert-ButylhydroperoxidemedicineHumansMangiferaViability assayATP Binding Cassette Transporter Subfamily B Member 1MangiferinP-glycoproteinPharmacologychemistry.chemical_classificationReactive oxygen speciesMangiferabiologyDose-Response Relationship DrugPlant StemsPlant ExtractsHep G2 Cellsmedicine.diseaseCytoprotectionMitochondrial toxicityBiochemistrychemistryToxicitybiology.proteinPlant BarkCalciumReactive Oxygen SpeciesThe Journal of pharmacy and pharmacology
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PTHrP [67-86] regulates the expression of stress proteins in breast cancer cells inducing modifications in urokinase-plasminogen activator and MMP-1 …

2003

It was previously reported that a midregion domain of parathyroid hormone-related protein (PTHrP), that is, [67-86]-amide, is able to restrain growth and promote matrigel penetration by the 8701-BC cell line, derived from a biopsy fragment of a primary ductal infiltrating carcinoma of the human breast, and that cell invasion in vitro is drastically impaired by inactivation of urokinase-plasminogen activator (uPa). In this study we started a more detailed investigation of the possible effects on gene expression arising from the interaction between PTHrP [67-86]-amide and 8701-BC breast cancer cells by a combination of conventional-, differential display-and semi-quantitative multiplex-polyme…

CellBreast NeoplasmsBiologyHeat Shock Transcription FactorsDownregulation and upregulationCell Line TumorHeat shock proteinmedicineHumansNeoplasm InvasivenessHSP90 Heat-Shock ProteinsEnzyme InhibitorsHSF1Heat-Shock ProteinsMatrigelActivator (genetics)CarcinomaParathyroid Hormone-Related ProteinCell BiologyOligonucleotides AntisenseUrokinase-Type Plasminogen ActivatorMolecular biologyPeptide FragmentsProtein Structure TertiaryUp-RegulationDNA-Binding ProteinsGene Expression Regulation NeoplasticHeat shock factormedicine.anatomical_structureCell cultureCancer researchFemaleQuercetinMatrix Metalloproteinase 1Transcription FactorsJournal of Cell Science
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Comm Sorts Robo to Control Axon Guidance at the Drosophila Midline

2002

AbstractAxon growth across the Drosophila midline requires Comm to downregulate Robo, the receptor for the midline repellent Slit. We show here that comm is required in neurons, not in midline cells as previously thought, and that it is expressed specifically and transiently in commissural neurons. Comm acts as a sorting receptor for Robo, diverting it from the synthetic to the late endocytic pathway. A conserved cytoplasmic LPSY motif is required for endosomal sorting of Comm in vitro and for Comm to downregulate Robo and promote midline crossing in vivo. Axon traffic at the CNS midline is thus controlled by the intracellular trafficking of the Robo guidance receptor, which in turn depends…

Central Nervous SystemEmbryo NonmammalianEndosomeGrowth ConesMolecular Sequence DataEndocytic cycleDown-RegulationNerve Tissue ProteinsReceptors Cell SurfaceCell CommunicationEndosomesBiologyModels BiologicalFunctional LateralityGeneral Biochemistry Genetics and Molecular BiologySequence Homology Nucleic AcidEctodermmedicineAnimalsDrosophila ProteinsReceptors ImmunologicAxonTransport VesiclesReceptorSequence Homology Amino AcidBiochemistry Genetics and Molecular Biology(all)Stem CellsCell MembraneGraft SurvivalGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationAnatomyCommissureSlitProtein Structure TertiaryCell biologyProtein TransportDrosophila melanogastermedicine.anatomical_structureCOS CellsRoundaboutAxon guidanceStem Cell TransplantationCell
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The Process-inducing Activity of Transmembrane Agrin Requires Follistatin-like Domains

2009

Clustering or overexpression of the transmembrane form of the extracellular matrix proteoglycan agrin in neurons results in the formation of numerous highly motile filopodia-like processes extending from axons and dendrites. Here we show that similar processes can be induced by overexpression of transmembrane-agrin in several non-neuronal cell lines. Mapping of the process-inducing activity in neurons and non-neuronal cells demonstrates that the cytoplasmic part of transmembrane agrin is dispensable and that the extracellular region is necessary for process formation. Site-directed mutagenesis reveals an essential role for the loop between beta-sheets 3 and 4 within the Kazal subdomain of t…

Central Nervous SystemFollistatinanimal structuresBiologyCytoplasmic partPC12 CellsBiochemistryProtein Structure SecondaryNeuromuscular junctionCell membraneExtracellular matrixMolecular Basis of Cell and Developmental BiologyProtein structureChlorocebus aethiopsmedicineAnimalsHumansAgrinMolecular BiologyNeuronsAgrinCell MembraneCell BiologyTransmembrane proteinProtein Structure TertiaryRatsCell biologymedicine.anatomical_structurenervous systemProteoglycanBiochemistryCOS CellsMutagenesis Site-Directedbiology.proteinFemaleChickenshormones hormone substitutes and hormone antagonistsJournal of Biological Chemistry
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RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin

2005

The ORF15 isoform of RPGR (RPGR(ORF15)) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR(ORF15) and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR(ORF15) (ORF15(C2)) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mas…

CentrioleFluorescent Antibody TechniqueMicechemistry.chemical_compoundChlorocebus aethiopsGuanine Nucleotide Exchange FactorsProtein IsoformsBasal bodyConserved SequenceGenetics (clinical)CentriolesGlutathione Transferaseintegumentary systemNuclear ProteinsExonsGeneral MedicineRetinitis pigmentosa GTPase regulatorImmunohistochemistryNocodazoleCOS CellsNucleophosminCell NucleolusRecombinant Fusion ProteinsMolecular Sequence DataBiologyOpen Reading FramesMicrotubuleTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceEye ProteinsMolecular BiologyNucleophosminSequence Homology Amino AcidProteinsPrecipitin TestsMolecular biologyeye diseasesProtein Structure TertiaryMice Inbred C57BLCytoskeletal ProteinschemistryCentrosomeCytoplasmSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationMutationCattleHeLa CellsHuman Molecular Genetics
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