Search results for "Protein transport"

showing 10 items of 197 documents

Geldanamycin-induced osteosarcoma cell death is associated with hyperacetylation and loss of mitochondrial pool of heat shock protein 60 (hsp60)

2013

Osteosarcoma is one of the most malignant tumors of childhood and adolescence that is often resistant to standard chemo- and radio-therapy. Geldanamycin and geldanamycin analogs have been recently studied as potential anticancer agents for osteosarcoma treatment. Here, for the first time, we have presented novel anticancer mechanisms of geldanamycin biological activity. Moreover, we demonstrated an association between the effects of geldanamycin on the major heat shock proteins (HSPs) and the overall survival of highly metastatic human osteosarcoma 143B cells. We demonstrated that the treatment of 143B cells with geldanamycin caused a subsequent upregulation of cytoplasmic Hsp90 and Hsp70 w…

Cell SurvivalLactams Macrocycliclcsh:MedicineApoptosisBone NeoplasmsBiologyMitochondrionMitochondrial Proteinschemistry.chemical_compoundGeldanamycin Hsp60 Osteosarcoma cellHeat shock proteinCell Line Tumorpolycyclic compoundsBenzoquinonesHumansHeat shocklcsh:ScienceCell ProliferationOsteosarcomaMultidisciplinaryAntibiotics Antineoplasticlcsh:RAcetylationChaperonin 60GeldanamycinHsp90Molecular biologyMitochondriaProtein TransportchemistryCancer cellCancer researchbiology.proteinApoptotic signaling pathwayHSP60lcsh:QDrug Screening Assays AntitumorProtein Processing Post-TranslationalResearch ArticleSignal Transduction
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Human Hsp10 and Early Pregnancy Factor (EPF) and their relationship and involvement in cancer and immunity: current knowledge and perspectives.

2009

This article is about Hsp10 and its intracellular and extracellular forms focusing on the relationship of the latter with Early Pregnancy Factor and on their roles in cancer and immunity. Cellular physiology and survival are finely regulated and depend on the correct functioning of the entire set of proteins. Misfolded or unfolded proteins can cause deleterious effects and even cell death. The chaperonins Hsp10 and Hsp60 act together inside the mitochondria to assist protein folding. Recent studies demonstrated that these proteins have other roles inside and outside the cell, either together or independently of each other. For example, Hsp10 was found increased in the cytosol of different t…

Cell physiologyHsp10 tumor immunity chaperonins early pregnancy factor developmentProgrammed cell deathProtein Foldingmedicine.medical_treatmentBiologyPregnancy ProteinsGeneral Biochemistry Genetics and Molecular BiologyAutoimmune DiseasesImmune systemImmunityNeoplasmsExtracellularmedicineChaperonin 10Suppressor Factors ImmunologicHumansGeneral Pharmacology Toxicology and PharmaceuticsSettore BIO/16 - Anatomia UmanaGrowth factorGeneral MedicineCell biologyMitochondriaProtein TransportHSP60IntracellularLife sciences
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The translocation of signaling molecules in dark adapting mammalian rod photoreceptor cells is dependent on the cytoskeleton.

2008

In vertebrate rod photoreceptor cells, arrestin and the visual G-protein transducin move between the inner segment and outer segment in response to changes in light. This stimulus dependent translocation of signalling molecules is assumed to participate in long term light adaptation of photoreceptors. So far the cellular basis for the transport mechanisms underlying these intracellular movements remains largely elusive. Here we investigated the dependency of these movements on actin filaments and the microtubule cytoskeleton of photoreceptor cells. Co-cultures of mouse retina and retinal pigment epithelium were incubated with drugs stabilizing and destabilizing the cytoskeleton. The actin a…

Cell signalingCytochalasin Dgenetic structuresLightPaclitaxelPhalloidineDark AdaptationBiologyHeterocyclic Compounds 4 or More RingsMicrotubulesRetinaMiceStructural BiologyMicrotubuleRetinal Rod Photoreceptor CellsCytoskeletal drugsThiabendazolemedicineArrestinAnimalsTransducinCytoskeletonMicroscopy ImmunoelectronActinCytoskeletonVision OcularMice KnockoutRetinal pigment epitheliumArrestinHomozygoteCell BiologyDarknessRod Cell Outer Segmenteye diseasesActinsCell biologyMice Inbred C57BLActin CytoskeletonProtein Transportmedicine.anatomical_structureMicroscopy Fluorescencesense organsTransducinCell Migration AssaysSignal TransductionCell motility and the cytoskeleton
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High expression of QSOX1 reduces tumorogenesis, and is associated with a better outcome for breast cancer patients.

2012

International audience; ABSTRACT: INTRODUCTION: The gene quiescin/sulfhydryl oxidase 1, QSOX1, encodes an enzyme directed to the secretory pathway and excreted into the extracellular space. QSOX1 participates in the folding and stability of proteins and thus could regulate the biological activity of its substrates in the secretory pathway and/or outside the cell. The involvement of QSOX1 in oncogenesis has been studied primarily in terms of its differential expression in systemic studies. QSOX1 is overexpressed in prostate cancers and in pancreatic adenocarcinoma. In contrast, QSOX1 gene expression is repressed in endothelial tumors. In the present study, we investigated the role of QSOX1 i…

CellGene ExpressionBreast Neoplasms[SDV.CAN]Life Sciences [q-bio]/CancerBiologymedicine.disease_causeMetastasis[ SDV.CAN ] Life Sciences [q-bio]/CancerMice03 medical and health sciences0302 clinical medicineBreast cancer[SDV.CAN] Life Sciences [q-bio]/CancerCell MovementCell Line TumormedicineExtracellularAnimalsHumansOxidoreductases Acting on Sulfur Group DonorsRNA MessengerNeoplasm MetastasisCell ProliferationRetrospective Studies030304 developmental biologyMedicine(all)0303 health sciencesCell growthCancermedicine.diseaseExtracellular MatrixTumor Burden3. Good healthPatient Outcome AssessmentDisease Models AnimalProtein TransportCell Transformation Neoplasticmedicine.anatomical_structure030220 oncology & carcinogenesisCancer researchHeterograftsAdenocarcinomaFemaleNeoplasm GradingCarcinogenesisResearch Article
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Role of cAMP in mediating AHR signaling.

2009

Regulation of the nuclear import of many transcription factors represents a step in gene regulation which is crucial for a number of cellular processes. The aryl hydrocarbon receptor (AHR), a basic helix-loop-helix protein of the PAS (PER-ARNT-SIM) family of transcriptional regulators is a cytosol-associated and ligand-activated receptor. The environmental toxin dioxin binds with high affinity to AHR rendering it nuclear and leading to the activation of AHR sensitive genes. However, the fact, that the AHR mediates a large variety of physiological events without the involvement of any known exogenous ligand, including liver and vascular system development, maturation of the immune system, re…

Cellular differentiationNuclear translocationSignal transductionDioxinsLigandsBiochemistryCell LineProtein kinase ACyclic AMPCytochrome P-450 CYP1A1AnimalsHumansPhosphorylationReceptorProtein kinase ATranscription factorAryl hydrocarbon receptorPharmacologyRegulation of gene expressionbiologyAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesProtein TransportBiochemistryReceptors Aryl HydrocarbonSecond messenger systembiology.proteinEnvironmental PollutantsSignal transductionDioxin toxicitySignal TransductionBiochemical pharmacology
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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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Characterization of the transporterB0AT3 (Slc6a17) in the rodent central nervous system.

2013

Abstract Background The vesicular B0AT3 transporter (SLC6A17), one of the members of the SLC6 family, is a transporter for neutral amino acids and is exclusively expressed in brain. Here we provide a comprehensive expression profile of B0AT3 in mouse brain using in situ hybridization and immunohistochemistry. Results We confirmed previous expression data from rat brain and used a novel custom made antibody to obtain detailed co-labelling with several cell type specific markers. B0AT3 was highly expressed in both inhibitory and excitatory neurons. The B0AT3 expression was highly overlapping with those of vesicular glutamate transporter 2 (VGLUT2) and vesicular glutamate transporter 1 (VGLUT1…

Central Nervous SystemMaleSerotonin reuptake inhibitorVesicular glutamate transporter 1Central nervous systemVesicular Transport ProteinsNerve Tissue ProteinsIn situ hybridizationPharmacology and ToxicologyPharmacologyBiologyPlasma Membrane Neurotransmitter Transport ProteinsRats Sprague-DawleyCellular and Molecular NeuroscienceGlutamatergicMiceDopaminePregnancyMonoaminergicmedicineAnimalsRats WistarCells CulturedNeuronsGeneral NeuroscienceNeurosciencesTransporterFarmakologi och toxikologiEmbryo MammalianAntidepressive AgentsRatsMice Inbred C57BLProtein Transportmedicine.anatomical_structureGene Expression Regulationbiology.proteinFemaleFood DeprivationNeurovetenskapermedicine.drugResearch ArticleBMC neuroscience
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Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes

2009

Oligodendrocytes form the central nervous system myelin sheath by spiral wrapping of their plasma membrane around axons, necessitating a high rate of exocytic membrane addition to the growing myelin membrane. Membrane fusion is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins (SNAREs), which act by specific pairing of vesicle (R)- and target (Q)-SNAREs. To characterize oligodendroglial SNAREs and their trafficking pathways, we performed a detailed expression analysis of SNAREs in differentiating cultured oligodendrocytes and myelin and determined their subcellular localization. Expression of the plasma membrane Q-SNAREs syntaxin 3, syntaxin 4, SNAP2…

Central Nervous SystemMaleVesicle-Associated Membrane Protein 3SynaptobrevinGolgi ApparatusBiologyMembrane FusionR-SNARE ProteinsMiceCellular and Molecular NeuroscienceSNAP23AnimalsSyntaxinQc-SNARE ProteinsTransport VesiclesCells CulturedMyelin SheathR-SNARE ProteinsQa-SNARE ProteinsVesicleCell MembraneLipid bilayer fusionQb-SNARE ProteinsSyntaxin 3Cell CompartmentationTransport proteinCell biologyOligodendrogliaProtein Transportnervous systemFemalebiological phenomena cell phenomena and immunitySNARE ProteinsDimerizationJournal of Neuroscience Research
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Neuronal Activity Drives Localized Blood-Brain-Barrier Transport of Serum Insulin-like Growth Factor-I into the CNS

2010

Upon entry into the central nervous system (CNS), serum insulin-like growth factor-1 (IGF-I) modulates neuronal growth, survival, and excitability. Yet mechanisms that trigger IGF-I entry across the blood-brain barrier remain unclear. We show that neuronal activity elicited by electrical, sensory, or behavioral stimulation increases IGF-I input in activated regions. Entrance of serum IGF-I is triggered by diffusible messengers (i.e., ATP, arachidonic acid derivatives) released during neurovascular coupling. These messengers stimulate matrix metalloproteinase-9, leading to cleavage of the IGF binding protein-3 (IGFBP-3). Cleavage of IGFBP-3 allows the passage of serum IGF-I into the CNS thro…

Central Nervous SystemTime FactorsMicrodialysismedicine.medical_treatmentAction PotentialsStimulationFunctional LateralityBody TemperatureReceptor IGF Type 1chemistry.chemical_compoundNeural PathwaysPremovement neuronal activityDrug InteractionsInsulin-Like Growth Factor IMicroscopy ImmunoelectronReceptorCells CulturedNeuronsGeneral NeuroscienceSysneuro//purl.org/becyt/ford/3.1 [https]Protein TransportMedicina Básicamedicine.anatomical_structureMatrix Metalloproteinase 9Blood-Brain BarrierSIGNALING//purl.org/becyt/ford/3 [https]Arachidonic acidNeurogliaLow Density Lipoprotein Receptor-Related Protein-1CIENCIAS MÉDICAS Y DE LA SALUDNeuroscience(all)Central nervous systemNeurocienciasBiophysicsGlutamic AcidEnzyme-Linked Immunosorbent AssayNerve Tissue ProteinsBiologyBlood–brain barrierMOLNEUROmedicineAnimalsHumansImmunoprecipitationRats WistarAnalysis of VarianceGrowth factorEndothelial CellsTransporterCoculture TechniquesElectric StimulationSignalingRatsMolneurochemistryRegional Blood FlowVibrissaeSYSNEURODigoxigeninExcitatory Amino Acid AntagonistsNeuroscience
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In vitro P-glycoprotein efflux inhibition by atypical antipsychotics is in vivo nicely reflected by pharmacodynamic but less by pharmacokinetic chang…

2011

Abstract Background P-glycoprotein (P-gp), an efflux transporter of the blood–brain barrier, limits the access of multiple xenobiotics to the central nervous system (CNS). Thus drug-dependent inhibition, induction or genetic variation of P-gp impacts drug therapy. Methods We investigated atypical antipsychotics and their interaction with P-gp. Amisulpride, clozapine, N-desmethylclozapine, olanzapine, and quetiapine were assessed in vitro on their inhibitory potential and in vivo on their disposition in mouse serum and brain, and behaviourally on the RotaRod test. In vivo wildtype (WT) and mdr1a/1b double knockout mice (mdr1a/1b (−/−, −/−); KO) were investigated. Results In rhodamine 123 eff…

Clinical BiochemistryIn Vitro TechniquesPharmacologyToxicologyBlood–brain barrierBiochemistryRhodamine 123Rotarod performance testMiceBehavioral Neurosciencechemistry.chemical_compoundPharmacokineticsIn vivoCell Line TumormedicineAnimalsRhodamine 123ATP Binding Cassette Transporter Subfamily B Member 1Biological PsychiatryClozapineP-glycoproteinMice KnockoutPharmacologybiologyReceptors Dopamine D2Protein Transportmedicine.anatomical_structurechemistryRotarod Performance Testbiology.proteinDopamine AntagonistsEffluxAntipsychotic Agentsmedicine.drugPharmacology Biochemistry and Behavior
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