Search results for "Apoptosi"

showing 10 items of 1846 documents

Membrane-insertion fragments of Bcl-xL, Bax, and Bid.

2004

Apoptosis regulators of the Bcl-2 family associate with intracellular membranes from mitochondria and the endoplasmic reticulum, where they perform their function. The activity of these proteins is related to the release of apoptogenic factors, sequestered in the mitochondria, to the cytoplasm, probably through the formation of ion and/or protein transport channels. Most of these proteins contain a C-terminal putative transmembrane (TM) fragment and a pair of hydrophobic alpha helices (alpha5-alpha6) similar to the membrane insertion fragments of the ion-channel domain of diphtheria toxin and colicins. Here, we report on the membrane-insertion properties of different segments from antiapopt…

GlycosylationStereochemistryRecombinant Fusion ProteinsMolecular Sequence Databcl-X ProteinBcl-xLApoptosisBiochemistryProtein Structure SecondaryMembrane LipidsMiceProtein structureBcl-2-associated X proteinPredictive Value of TestsProto-Oncogene ProteinsProtein Interaction MappingAnimalsHumansAmino Acid SequencePeptide sequencebcl-2-Associated X ProteinbiologyIntracellular MembranesTransmembrane proteinPeptide FragmentsTransport proteinProtein TransportProto-Oncogene Proteins c-bcl-2Multigene FamilyHelixbiology.proteinBiophysicsCarrier ProteinsHydrophobic and Hydrophilic InteractionsAlpha helixBH3 Interacting Domain Death Agonist ProteinBiochemistry
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Increased expression of the potential proapoptotic molecule DD2 and increased synthesis of leukotriene B4 during allograft rejection in a marine spon…

2000

Sponges (Porifera) are a classical model to study the events during tissue transplantation. Applying the 'insertion technique' autografts from the marine sponge Geodia cydonium fuse within 5 days. In contrast, allografts are rejected and destroyed. Here we show that during allograft rejection the cells in the grafts undergo apoptosis; 5 days after transplantation 46% of the cells show signs of apoptosis. In a previous study it was shown that during this process a tumor necrosis factor-like molecule is induced in allo- and xenografts. Molecules grouped to the superfamily of tumor necrosis factor receptors and a series of associated adapter molecules contain the characteristic death domain. T…

Graft RejectionLeukotriene B4Molecular Sequence DataGene ExpressionApoptosisLeukotriene B4Transplantation Autologouschemistry.chemical_compoundDownregulation and upregulationGene expressionAnimalsHumansTransplantation HomologousAmino Acid SequenceCloning MolecularReceptorMolecular BiologyDeath domainSequence Homology Amino AcidChemistryCell BiologyMolecular biologyPoriferaTransplantationAlcohol Oxidoreductasessurgical procedures operativeApoptosisTumor necrosis factor alphaPeptidesCell Death & Differentiation
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Killing of p53-deficient hepatoma cells by parvovirus H-1 and chemotherapeutics requires promyelocytic leukemia protein

2008

To evaluate the synergistic targeting and killing of human hepatocellular carcinoma (HCC) cells lacking p53 by the oncolytic autonomous parvovirus (PV) H-1 and chemotherapeutic agents and its dependence on functional promyelocytic leukemia protein (PML).The role of p53 and PML in regulating cytotoxicity and gene transfer mediated by wild-type (wt) PV H-1 were explored in two pairs of isogenic human hepatoma cell lines with different p53 status. Furthermore, H-1 PV infection was combined with cytostatic drug treatment.While the HCC cells with different p53 status studied were all susceptible to H-1 PV-induced apoptosis, the cytotoxicity of H-1 PV was more pronounced in p53-negative than in p…

H-1 parvovirusLiver CancerH-1 parvovirusCarcinoma HepatocellularParvovirus H-1virusesAntineoplastic AgentsApoptosisPromyelocytic Leukemia ProteinPromyelocytic leukemia proteinDrug TherapyCell Line TumorHumansNuclear proteinCytotoxicityMembrane Potential MitochondrialbiologyParvovirusTumor Suppressor ProteinsLiver NeoplasmsGastroenterologyvirus diseasesNuclear ProteinsGeneral Medicinebiology.organism_classificationCombined Modality Therapydigestive system diseasesOncolytic virusApoptosisCancer researchbiology.proteinFluorouracilCisplatinTumor Suppressor Protein p53Transcription FactorsWorld Journal of Gastroenterology
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H89 enhances the sensitivity of cancer cells to glyceryl trinitrate through a purinergic receptor-dependent pathway

2014

// Marion Cortier 1, 2, 3 , Rahamata Boina-Ali 1, 2, 3 , Cindy Racoeur 1, 2, 3 , Catherine Paul 1, 2, 3 , Eric Solary 2, 4, 5 , Jean-Francois Jeannin 1, 2, 3 , Ali Bettaieb 1, 2, 3 1 EPHE, Tumor Immunology and Immunotherapy Laboratory, Dijon, F-21000, France 2 Inserm U866, Dijon, F-21000, France 3 EA7269, University of Burgundy, Dijon, F-21000, France 4 Inserm UMR1009, Gustave Roussy Institute, Villejuif F-94805, France 5 University Paris-Sud, Faculty of Medicine, Le Kremlin-Bicetre, F-94800, France Correspondence to: Ali Bettaieb, e-mail: ali.bettaieb@u-bourgogne.fr Keywords: H89, GTN, cancer, purinergic receptors, cGMP Received: October 08, 2014      Accepted: January 09, 2015      Publis…

H89SuraminApoptosisPharmacologyBiologyNitric OxideTransfectionNitric oxideMiceNitroglycerinReceptors Purinergic P2Y1chemistry.chemical_compoundAdenosine TriphosphateCell Line TumorNeoplasmspurinergic receptorsmedicineAnimalsHumanscancerCytotoxic T cellReceptorProtein Kinase InhibitorsMembrane Potential MitochondrialSulfonamidesReceptors Purinergic P2Gene Expression ProfilingPurinergic receptorReceptors PurinergicDrug SynergismOligonucleotides AntisenseIsoquinolinescGMPOncologychemistryApoptosisColonic NeoplasmsCancer cellcardiovascular systemSignal transductionReactive Oxygen SpeciesGTNReceptors Purinergic P2X3circulatory and respiratory physiologySignal TransductionResearch Papermedicine.drugOncotarget
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HISTONE DEACETYLASE INHIBITORS SENSITIZE HEPATOMA CELLS TO TRAIL_INDUCED APOPTOSIS

2008

HDACI HEPATOMA APOPTOSIS
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Synthesis and induction of G0–G1 phase arrest with apoptosis of 3,5-dimethyl-6-phenyl-8-(trifluoromethyl)-5,6-dihydropyrazolo[3,4-f][1,2,3,5]tetrazep…

2007

The multistep synthesis of 3,5-dimethyl-6-phenyl-8-(trifluoromethyl)-5,6-dihydropyrazolo[3,4-f][1,2,3,5]tetrazepin-4(3H)-one 15 has been carried out. The compound showed antiproliferative and apoptotic effects against K562, K562-R (imatinib mesilate resistant), HL60 and multidrug resistant (MDR) HL60 cell lines. Compound 15 showed a pro-apoptotic activity against HL60 and K562 resistant cell lines markedly higher than etoposide and busulfan, respectively. Flow cytometry studies carried out on K562 cells allowed to establish that 15 induces G0-G1 phase arrest followed by apoptosis.

HL60StereochemistryApoptosisHL-60 CellsAntiproliferative activityResting Phase Cell CycleChemical synthesisPyrazolo[34-f][1234]tetrazepinoneFlow cytometrychemistry.chemical_compoundhemic and lymphatic diseasesDrug DiscoverymedicineHumansCytotoxicityEtoposideG0-G1 arrestPharmacologyTrifluoromethylMolecular Structuremedicine.diagnostic_testOrganic ChemistryG1 PhaseApoptosiAzepinesGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaMolecular biologyMultiple drug resistancechemistryApoptosisDrug resistancePyrazoles1234-TetrazepinoneK562 Cellsmedicine.drugEuropean Journal of Medicinal Chemistry
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Hypoxia inducible factor-1 alpha expression is increased in infected positive HPV16 DNA oral squamous cell carcinoma and positively associated with H…

2011

Abstract Background There is increasing evidence for the role of High Risk (HR) Human PapillomaVirus (HPV) in the pathogenesis of Oral Squamous Cell Carcinoma (OSCC). The E6 and E7 oncogenes from HR HPVs are responsible for the deregulation of p53 and pRB proteins involved in cell cycle and apoptotic pathways. In cell lines experiments, the HPV E7 protein seems to be able to enhance Hypoxia Inducible Factor-1 alpha (HIF-1α) activity, normally involved in the response to hypoxia and able to enhance angiogenesis. Results We studied tumor specimens from 62 OSCC; a higher prevalence of tumors in TNM stage II and also in pT2 class between OSCC infected positive HPV16 DNA than non-infected ones w…

HPV16Cancer ResearchPathologymedicine.medical_specialtyHPVNecrosisAngiogenesisEpidemiologyAlpha (ethology)BiologyOral Squamous Cell Carcinomalcsh:RC254-282lcsh:Infectious and parasitic diseasesPathogenesisHypoxia-Inducible Factor 1-Alphachemistry.chemical_compoundmedicinelcsh:RC109-216E7Oral Squamous Cell Carcinoma Hif-1α HPV HPV16 E7virus diseasesHypoxia (medical)lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensfemale genital diseases and pregnancy complicationsstomatognathic diseasesInfectious DiseaseschemistryOncologyApoptosisCancer researchmedicine.symptomHif-1αDNAResearch ArticleInfectious agents and cancer
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Genetic manipulation of longevity-related genes as a tool to regulate yeast life span and metabolite production during winemaking

2013

Abstract Background Yeast viability and vitality are essential for different industrial processes where the yeast Saccharomyces cerevisiae is used as a biotechnological tool. Therefore, the decline of yeast biological functions during aging may compromise their successful biotechnological use. Life span is controlled by a variety of molecular mechanisms, many of which are connected to stress tolerance and genomic stability, although the metabolic status of a cell has proven a main factor affecting its longevity. Acetic acid and ethanol accumulation shorten chronological life span (CLS), while glycerol extends it. Results Different age-related gene classes have been modified by deletion or o…

HST3GlycerolSaccharomyces cerevisiae ProteinsTranscription Genetic<it>HST3</it>Saccharomyces cerevisiaeLongevitylcsh:QR1-502SOD2BioengineeringApoptosisWinePUB1Saccharomyces cerevisiaeStressApplied Microbiology and Biotechnologylcsh:MicrobiologyHistone DeacetylasesStress granuleSirtuin 2<it>PUB1</it>Gene expressionChronological agingSirtuinsNADH NADPH OxidoreductasesRNA MessengerEthanol metabolismSilent Information Regulator Proteins Saccharomyces cerevisiaeAcetic AcidbiologyEthanolSuperoxide DismutaseResearchRNA-Binding Proteinsbiology.organism_classificationYeastYeastBiochemistryCaspasesFermentationMutationFermentationHistone deacetylaseGene DeletionBiotechnologyMicrobial Cell Factories
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Activation of a caspase-3-independent mode of cell death associated with lysosomal destabilization in cultured human retinal pigment epithelial cells…

2008

International audience; Purpose: To characterize the possible cytotoxic effects of oxysterols (7-hydroxycholesterol (7-OH), 25-hydroxycholesterol (25-OH)) in human retinal pigment epithelial cells (ARPE-19) and to detail the relationships between some of these effects. Methods: ARPE-19 cells were treated with 7-OH and 25-OH. Cell viability was measured with the MTT assay. Membrane permeability, mitochondrial potential, and lysosomal integrity were measured by flow cytometry with propidium iodide, DiOC6(3), and acridine orange, respectively. Cell death was characterized by staining with Hoechst 33342, transmission electron microscopy, and analysis of the DNA fragmentation pattern. Caspase ac…

HUMAN BRUCHS MEMBRANECell Membrane PermeabilityMembrane PotentialsAGE-RELATED MACULOPATHYchemistry.chemical_compound0302 clinical medicineFluorescent Antibody Technique IndirectPigment Epithelium of EyeCaspaseCells CulturedElectrophoresis Agar Gel0303 health sciencesbiologyCell DeathCaspase 3CHOLESTEROLAcridine orangeApoptosis Inducing FactorCytochromes cDipeptidesKetonesFlow CytometrySensory SystemsCell biologyMitochondrial MembranesDNA fragmentationCOLORIMETRIC ASSAYMembrane permeabilityCell SurvivalBlotting WesternLOW-DENSITY-LIPOPROTEINCaspase 3DNA FragmentationCysteine Proteinase Inhibitors03 medical and health sciencesCellular and Molecular NeuroscienceBASAL DEPOSITSAPOPTOSIS-INDUCING FACTORHumansRPE CELLSViability assayPropidium iodide[SDV.MHEP.OS]Life Sciences [q-bio]/Human health and pathology/Sensory Organs030304 developmental biologyMACULAR DEGENERATIONMolecular biologyHydroxycholesterolsEnzyme ActivationOphthalmologychemistryApoptosis030221 ophthalmology & optometrybiology.proteinLysosomes7-KETOCHOLESTEROL-INDUCED APOPTOSIS[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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The aryl hydrocarbon receptor-dependent deregulation of cell cycle control induced by polycyclic aromatic hydrocarbons in rat liver epithelial cells

2006

Disruption of cell proliferation control by polycyclic aromatic hydrocarbons (PAHs) may contribute to their carcinogenicity. We investigated role of the aryl hydrocarbon receptor (AhR) in disruption of contact inhibition in rat liver epithelial WB-F344 'stem-like' cells, induced by the weakly mutagenic benz[a]anthracene (BaA), benzo[b]fluoranthene (BbF) and by the strongly mutagenic benzo[a]pyrene (BaP). There were significant differences between the effects of BaA and BbF, and those of the strongly genotoxic BaP. Both BaA and BbF increased percentage of cells entering S-phase and cell numbers, associated with an increased expression of Cyclin A and Cyclin A/cdk2 complex activity. Their eff…

Health Toxicology and MutagenesisCyclin AGene ExpressionApoptosisCell Cycle ProteinsCyclin ACell LineBenz(a)AnthracenesBenzo(a)pyreneCytochrome P-450 CYP1A1polycyclic compoundsGeneticsAnimalsRat liver ‘stem-like’ cellsRNA MessengerPolycyclic Aromatic HydrocarbonsRNA Small InterferingMolecular BiologyAryl hydrocarbon receptorCell proliferationCarcinogenCell ProliferationFluorenesBase SequencebiologyChemistryCell growthCell CycleCyclin-Dependent Kinase 2Contact inhibitionEpithelial CellsTransfectionAryl hydrocarbon receptorMolecular biologyPolycyclic aromatic hydrocarbonsPolycyclic Hydrocarbons AromaticRatsReceptors Aryl HydrocarbonBiochemistryApoptosisMultiprotein ComplexesContact inhibitionMutationHepatocytesbiology.proteinCDK inhibitorMutagensMutation Research/Fundamental and Molecular Mechanisms of Mutagenesis
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