Search results for "Molecular Cell Biology"

showing 10 items of 129 documents

3-Deazaneplanocin A (DZNep), an Inhibitor of the Histone Methyltransferase EZH2, Induces Apoptosis and Reduces Cell Migration in Chondrosarcoma Cells

2014

Objective Growing evidences indicate that the histone methyltransferase EZH2 (enhancer of zeste homolog 2) may be an appropriate therapeutic target in some tumors. Indeed, a high expression of EZH2 is correlated with poor prognosis and metastasis in many cancers. In addition, 3-Deazaneplanocin A (DZNep), an S-adenosyl-L homocysteine hydrolase inhibitor which induces EZH2 protein depletion, leads to cell death in several cancers and tumors. The aim of this study was to determine whether an epigenetic therapy targeting EZH2 with DZNep may be also efficient to treat chondrosarcomas. Methods EZH2 expression was determined by immunohistochemistry and western-blot. Chondrosarcoma cell line CH2879…

MESH: Cell DeathAdenosine[SDV]Life Sciences [q-bio]Cancer Treatmentlcsh:MedicineMESH: Flow CytometryApoptosischemistry.chemical_compoundSpectrum Analysis Techniques0302 clinical medicineCell MovementMolecular Cell BiologyMedicine and Health Sciences3-Deazaneplanocin AMESH: Epigenesis GeneticEnzyme Inhibitorslcsh:Science0303 health sciencesMultidisciplinaryCell DeathbiologyReverse Transcriptase Polymerase Chain ReactionEZH2Polycomb Repressive Complex 2DrugsCell migrationMESH: ChondrosarcomaFlow Cytometry3. Good healthHistone[SDV.MHEP.RSOA]Life Sciences [q-bio]/Human health and pathology/Rhumatology and musculoskeletal systemOncologyConnective TissueCell ProcessesSpectrophotometry030220 oncology & carcinogenesisHistone methyltransferaseHistone MethyltransferasesMESH: 3-deazaneplanocinCytophotometryAnatomyMESH: Polycomb Repressive Complex 2Epigenetic therapyMESH: Histone methyltransferaseResearch ArticleProgrammed cell deathHistologyChondrosarcoma[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular Biologymacromolecular substancesResearch and Analysis MethodsCell GrowthEpigenetic Therapy03 medical and health sciencesRheumatologyCell Line TumorMESH: Blotting WesternHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyEZH2Tumors030304 developmental biologyMESH: Apoptosislcsh:RMESH: Histone-Lysine N-MethyltransferaseBiology and Life SciencesMESH: ImmunohistochemistryHistone-Lysine N-MethyltransferaseCell BiologyBiological TissueCartilageHistone methyltransferasechemistryApoptosisbiology.proteinCancer researchMESH: EZH2 protein humanlcsh:QCytometry
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The Hsc/Hsp70 Co-Chaperone Network Controls Antigen Aggregation and Presentation during Maturation of Professional Antigen Presenting Cells

2011

The maturation of mouse macrophages and dendritic cells involves the transient deposition of ubiquitylated proteins in the form of dendritic cell aggresome-like induced structures (DALIS). Transient DALIS formation was used here as a paradigm to study how mammalian cells influence the formation and disassembly of protein aggregates through alterations of their proteostasis machinery. Co-chaperones that modulate the interplay of Hsc70 and Hsp70 with the ubiquitin-proteasome system (UPS) and the autophagosome-lysosome pathway emerged as key regulators of this process. The chaperone-associated ubiquitin ligase CHIP and the ubiquitin-domain protein BAG-1 are essential for DALIS formation in mou…

Macromolecular AssembliesImmune CellsCellular differentiationImmunologyAntigen presentationAntigen-Presenting Cellslcsh:MedicineAntigen Processing and RecognitionMajor histocompatibility complexBiochemistryMiceMolecular Cell BiologyMHC class IAutophagyAnimalsHSP70 Heat-Shock ProteinsAntigensProtein Interactionslcsh:ScienceAntigen-presenting cellBiologyImmune ResponseCellular Stress ResponsesAntigen PresentationMultidisciplinarybiologylcsh:RHSC70 Heat-Shock ProteinsImmunityProteinsCell DifferentiationDendritic cellChaperone ProteinsUbiquitin ligaseCell biologyProteostasisbiology.proteinlcsh:QProtein MultimerizationResearch ArticlePLoS ONE
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Aminopropyltransferases involved in polyamine biosynthesis localize preferentially in the nucleus of plant cells

2012

Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the…

Macromolecular AssembliesProteomicsS-AdenosylmethioninePlant anatomyImmunohistoquímicaArabidopsislcsh:MedicineSecondary MetabolismSpermineExpressionPlant ScienceSpermidine synthaseBiochemistrychemistry.chemical_compoundBimolecular fluorescence complementationCytosolMolecular Cell BiologyPolyaminesPlant Genomicslcsh:SciencePlant Growth and DevelopmentMultidisciplinarybiologyPlant BiochemistryArabidopsis-ThalianaGenomicsImmunohistochemistryMetabolismeFunctional GenomicsBiochemistrySpermine synthasePlant proteinPlant PhysiologyMechanismResearch ArticleHistologyAcyltransferasePlant Cell BiologyActive Transport Cell NucleusSpermidine SynthaseBimolecular fluorescence complementationProtein InteractionsBiologyCell NucleusCrystal-Structurelcsh:RHistologiaBotanyProtein interactionsSubcellular localizationAnatomia vegetalExpressió gènicaMolecular WeightSpermidineMetabolismchemistryDecarboxylasebiology.proteinPutrescineBotànicalcsh:QGene expressionSpermidine synthase
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Inhibition of Xanthine Oxidase by Allopurinol Prevents Skeletal Muscle Atrophy: Role of p38 MAPKinase and E3 Ubiquitin Ligases

2012

International audience; Abstract Top Alterations in muscle play an important role in common diseases and conditions. Reactive oxygen species (ROS) are generated during hindlimb unloading due, at least in part, to the activation of xanthine oxidase (XO). The major aim of this study was to determine the mechanism by which XO activation causes unloading-induced muscle atrophy in ratsand its possible prevention by allopurinol, a well-known inhibitor of this enzyme. For this purpose we studied one of the main redox sensitive signalling cascades involved in skeletal muscle atrophy i.e. p38 MAPKinaseand the expression of two well known muscle specific E3 ubiquitin ligases involved in proteolysis, …

MaleAgingAnatomy and Physiology[SDV]Life Sciences [q-bio]lcsh:MedicineMuscle ProteinsGene ExpressionHindlimbSignal transductionmedicine.disease_causep38 Mitogen-Activated Protein KinasesTripartite Motif Proteinschemistry.chemical_compound0302 clinical medicineMolecular cell biologySignaling in Cellular Processeslcsh:ScienceMusculoskeletal System0303 health sciencesMultidisciplinarySignaling cascadesMuscle BiochemistryAnimal ModelsMuscle atrophy3. Good healthMuscular Atrophymedicine.anatomical_structureBiochemistryHindlimb SuspensionMuscleMedicinemedicine.symptomCellular Typesmedicine.drugResearch Articlemedicine.medical_specialtyXanthine OxidaseMAPK signaling cascadesAllopurinolUbiquitin-Protein LigasesAllopurinolBiology03 medical and health sciencesAtrophyModel OrganismsInternal medicinemedicineAnimalsRats WistarXanthine oxidaseMuscle SkeletalBiology030304 developmental biologySoleus muscleMuscle CellsSKP Cullin F-Box Protein LigasesSuperoxide Dismutaselcsh:RSkeletal musclemedicine.diseaseRatsEnzyme ActivationOxidative StressEndocrinologychemistryRatlcsh:QPhysiological Processes030217 neurology & neurosurgeryOxidative stress
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Differential expression of PGC-1α and metabolic sensors suggest age-dependent induction of mitochondrial biogenesis in Friedreich ataxia fibroblasts.

2011

11 pages, 6 figures. PMID:21687738[PubMed] PMCID: PMC3110204

MaleAgingMitochondrial DiseasesMitochondrial MyopathyUbiquinoneCardiomyopathylcsh:MedicineMitochondrionAMP-Activated Protein Kinasesp38 Mitogen-Activated Protein KinasesAntioxidantsAdenosine TriphosphateAMP-activated protein kinaseTrinucleotide RepeatsFibrosisMolecular Cell BiologyChildlcsh:ScienceHeat-Shock ProteinsRegulation of gene expressionMultidisciplinaryMovement DisordersbiologyNeuromuscular DiseasesMiddle AgedCatalasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCell biologyMitochondriaDNA-Binding ProteinsNeurologyDisease ProgressionMedicineFemalemedicine.symptomSignal TransductionResearch ArticleAdultcongenital hereditary and neonatal diseases and abnormalitiesAtaxiaAdolescentMitochondrial ProteinsmedicineGeneticsHumansBiologyAllelesGlutathione PeroxidaseSuperoxide Dismutaselcsh:RHuman GeneticsFibroblastsmedicine.diseaseMolecular biologyOxidative StressMitochondrial biogenesisGene Expression RegulationFriedreich Ataxiabiology.proteinFrataxinlcsh:QEnergy MetabolismReactive Oxygen SpeciesTranscription FactorsPLoS ONE
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Therapeutic effects of hMAPC and hMSC transplantation after stroke in mice.

2012

Stroke represents an attractive target for stem cell therapy. Although different types of cells have been employed in animal models, a direct comparison between cell sources has not been performed. The aim of our study was to assess the effect of human multipotent adult progenitor cells (hMAPCs) and human mesenchymal stem cells (hMSCs) on endogenous neurogenesis, angiogenesis and inflammation following stroke. BALB/Ca-RAG 2(-/-) γC(-/-) mice subjected to FeCl(3) thrombosis mediated stroke were intracranially injected with 2 × 10(5) hMAPCs or hMSCs 2 days after stroke and followed for up to 28 days. We could not detect long-term engraftment of either cell population. However, in comparison w…

MaleAnatomy and PhysiologyMousemedicine.medical_treatmentCell therapyMiceCell MovementMolecular Cell BiologyNeurobiology of Disease and RegenerationMedicineMultidisciplinaryNeuronal MorphologyNeurogenesisQRBrainInfarction Middle Cerebral ArteryAnimal ModelsStem-cell therapyStrokeAdult Stem Cellsmedicine.anatomical_structureNeurologyMedicineResearch ArticleAdult stem cellCell PhysiologyHistologyCell SurvivalCerebrovascular DiseasesScienceTherapeutic effectsNeurophysiologyNeovascularization PhysiologicSubventricular zoneMesenchymal Stem Cell TransplantationNeurological SystemModel OrganismsAnimalsHumansProgenitor cellBiologyTransplantationbusiness.industryMultipotent Stem CellsMesenchymal stem cellMultipotent Stem CellCellular NeuroscienceImmunologyCancer researchMolecular NeurosciencebusinesshMAPC and hMSCNeurosciencePLoS ONE
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Obese Rats Exhibit High Levels of Fat Necrosis and Isoprostanes in Taurocholate-Induced Acute Pancreatitis

2012

BACKGROUND: Obesity is a prognostic factor for severity in acute pancreatitis in humans. Our aim was to assess the role of oxidative stress and abdominal fat in the increased severity of acute pancreatitis in obese rats. METHODOLOGY: Taurocholate-induced acute pancreatitis was performed in lean and obese Zucker rats. Levels of reduced glutathione, oxidized glutathione, L-cysteine, cystine, and S-adenosylmethionine were measured in pancreas as well as the activities of serine/threonine protein phosphatases PP1 and PP2A and tyrosin phosphatases. Isoprostane, malondialdehyde, triglyceride, and free fatty acid levels and lipase activity were measured in plasma and ascites. Lipase activity was m…

MaleAnatomy and PhysiologyNecrosislcsh:MedicineAdipose tissueIsoprostanesmedicine.disease_causeBiochemistrychemistry.chemical_compoundMalondialdehydeMolecular Cell Biologylcsh:ScienceMultidisciplinaryPancreatitis Acute Necrotizingmusculoskeletal neural and ocular physiologyAnimal ModelsMalondialdehydeGlutathioneLipidsEnzymesBlood ChemistryMedicineAcute pancreatitismedicine.symptomResearch ArticleTaurocholic AcidCell Physiologymedicine.medical_specialtyBlotting WesternImmunologyGastroenterology and Hepatologymacromolecular substancesModel OrganismsInternal medicineChemical BiologymedicineAnimalsFat necrosisObesityPancreasBiologyTriglyceridesbusiness.industrylcsh:Rmedicine.diseaseObesityRatsRats ZuckerOxidative StressMetabolismEndocrinologyPancreatitisnervous systemchemistrySmall MoleculesRatPancreatitislcsh:QbusinessOxidative stressPLoS ONE
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Functional evidence of multidrug resistance transporters (MDR) in rodent olfactory epithelium.

2012

WOS: 000305340700029; International audience; BACKGROUND: P-glycoprotein (Pgp) and multidrug resistance-associated protein (MRP1) are membrane transporter proteins which function as efflux pumps at cell membranes and are considered to exert a protective function against the entry of xenobiotics. While evidence for Pgp and MRP transporter activity is reported for olfactory tissue, their possible interaction and participation in the olfactory response has not been investigated. PRINCIPAL FINDINGS: Functional activity of putative MDR transporters was assessed by means of the fluorometric calcein acetoxymethyl ester (calcein-AM) accumulation assay on acute rat and mouse olfactory tissue slices.…

MaleAnatomy and Physiology[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionGene Expressionlcsh:MedicineATP-binding cassette transporterPharmacologyMicechemistry.chemical_compoundMolecular Cell Biologypolycyclic compoundslcsh:ScienceMice Inbred BALB CMultidisciplinaryNeuromodulationProbenecidReverse Transcriptase Polymerase Chain ReactionNeurochemistryFluoresceinsSensory SystemsCell biologyElectrophysiologymedicine.anatomical_structureAlimentation et NutritionCyclosporineQuinolinesMedicineFemaleEffluxCellular TypesMultidrug Resistance-Associated Proteinsproduct p-glycoprotein;blood-brain-barrier;receptor neurons;cyclic-nucleotides;tumor-cells;expression;localization;protein;gene;tissuesMultidrug Resistance-Associated ProteinsResearch ArticleATP Binding Cassette Transporter Subfamily BNeurophysiologyBiologyOlfactory Receptor NeuronsOlfactory mucosaPsychologie (Sciences cognitives)Olfactory MucosaPeripheral Nervous SystemmedicineAnimalsFood and NutritionRats WistarBiologyOlfactory SystemOlfactory receptorlcsh:RNeurosciencesEpithelial CellsBiological TransportTransporterRatsCalceinMicroscopy FluorescenceVerapamilchemistryNeurons and Cognitionlcsh:QPropionates[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOlfactory epitheliumNeuroscience
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Enhanced Activity of Meprin-α, a Pro-Migratory and Pro-Angiogenic Protease, in Colorectal Cancer

2011

Meprin-α is a metalloprotease overexpressed in cancer cells, leading to the accumulation of this protease in a subset of colorectal tumors. The impact of increased meprin-α levels on tumor progression is not known. We investigated the effect of this protease on cell migration and angiogenesis in vitro and studied the expression of meprin-α mRNA, protein and proteolytic activity in primary tumors at progressive stages and in liver metastases of patients with colorectal cancer, as well as inhibitory activity towards meprin-α in sera of cancer patient as compared to healthy controls. We found that the hepatocyte growth factor (HGF)- induced migratory response of meprin-transfected epithelial c…

MaleAngiogenesisColorectal cancerCancer TreatmentGene Expressionlcsh:MedicineBiochemistry0302 clinical medicineCell MovementMolecular Cell BiologyGastrointestinal CancersMorphogenesisPathologylcsh:ScienceAged 80 and over0303 health sciencesMetalloproteinaseMultidisciplinaryHepatocyte Growth FactorLiver NeoplasmsMetalloendopeptidasesMiddle AgedImmunohistochemistryRecombinant ProteinsEnzymes3. Good healthOncology030220 oncology & carcinogenesisMedicineFemaleHepatocyte growth factorAntiangiogenesis TherapyColorectal NeoplasmsResearch Articlemedicine.drugAdultmedicine.medical_specialtyImmunoblottingHistopathologyNeovascularization PhysiologicCell MigrationGastroenterology and HepatologyIn Vitro TechniquesBiologyMannose-Binding LectinCell LineRectal CancerYoung Adult03 medical and health sciencesDogsDiagnostic MedicineInternal medicineGastrointestinal TumorsmedicineAnimalsHumansImmunoprecipitationBiologyAged030304 developmental biologylcsh:RCancers and NeoplasmsCancerPlasminogenBlotting Northernmedicine.diseaseRatsEndocrinologyAnatomical PathologyTumor progressionZymogen activationCancer cellCancer researchlcsh:QDevelopmental BiologyPLoS ONE
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Role of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coli

2011

Ileal lesions in Crohn's disease (CD) patients are colonized by pathogenic adherent-invasive Escherichia coli (AIEC) able to adhere to and invade intestinal epithelial cells (IEC), and to survive within macrophages. The interaction of AIEC with IEC depends on bacterial factors mainly type 1 pili, flagella, and outer membrane proteins. In humans, proteases can act as host defence mechanisms to counteract bacterial colonization. The protease meprin, composed of multimeric complexes of the two subunits alpha and beta, is abundantly expressed in IECs. Decreased levels of this protease correlate with the severity of the inflammation in patients with inflammatory bowel disease. The aim of the pre…

MaleBacterial Diseasesmedicine.medical_treatmentACTIVATION MECHANISMBiochemistryBacterial AdhesionPilusMice0302 clinical medicineCrohn DiseaseIntestinal mucosaMolecular Cell BiologyGastrointestinal InfectionsIntestinal MucosaAged 80 and over0303 health sciencesMultidisciplinaryQRMetalloendopeptidasesMiddle AgedEnzymesBacterial Pathogens3. Good healthHost-Pathogen InteractionInfectious DiseasesCytokineESCHERICHIA-COLI030220 oncology & carcinogenesisAlimentation et NutritionMedicineFemaleINFLAMMATORY-BOWEL-DISEASE;INTESTINAL EPITHELIAL-CELLS;URINARY-TRACT-INFECTIONS;ESCHERICHIA-COLI;ALPHA-SUBUNIT;STRAIN LF82;METALLOPROTEASE MEPRIN;ACTIVATION MECHANISM;BETA-SUBUNIT;TYPE-1 PILICellular Typesmedicine.symptomBacterial outer membraneALPHA-SUBUNITResearch ArticleAdultProteasesScienceMédecine humaine et pathologieInflammationGastroenterology and HepatologyBiologyMETALLOPROTEASE MEPRINMicrobiologyMicrobiologyURINARY-TRACT-INFECTIONS03 medical and health sciencesTYPE-1 PILIEscherichia colimedicineAnimalsHumansFood and NutritionSecretionInterleukin 8BETA-SUBUNITBiologyAged030304 developmental biologySTRAIN LF82Interleukin-8Inflammatory Bowel DiseaseEpithelial Cellsdigestive system diseasesMice Inbred C57BLHuman health and pathologyINTESTINAL EPITHELIAL-CELLS[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyINFLAMMATORY-BOWEL-DISEASE
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