Search results for "Golgi"

showing 10 items of 97 documents

Role of two sequence motifs of mesencephalic astrocyte-derived neurotrophic factor in its survival-promoting activity

2015

AbstractMesencephalic astrocyte-derived neurotrophic factor (MANF) is a prosurvival protein that protects the cells when applied intracellularly in vitro or extracellularly in vivo. Its protective mechanisms are poorly known. Here we studied the role of two short sequence motifs within the carboxy-(C) terminal domain of MANF in its neuroprotective activity: the CKGC sequence (a CXXC motif) that could be involved in redox reactions, and the C-terminal RTDL sequence, an endoplasmic reticulum (ER) retention signal. We mutated these motifs and analyzed the antiapoptotic effect and intracellular localization of these mutants of MANF when overexpressed in cultured sympathetic or sensory neurons. …

Cancer ResearchCell SurvivalImmunologyMutantAmino Acid MotifsIntracellular SpaceGolgi ApparatusSuperior Cervical GanglionBiologyRats Sprague-DawleyCellular and Molecular Neurosciencesymbols.namesakeMiceStructure-Activity RelationshipMutant proteinNeurotrophic factorsGanglia SpinalExtracellularAnimalsCysteineNerve Growth FactorsEtoposideSequence DeletionEndoplasmic reticulumprosurvival proteinsta1182Cell BiologyGolgi apparatusMolecular biologyRecombinant ProteinsStrokeDisease Models AnimalProtein Transportmesencephalic astrocyte-derived neurotrophic factorNeuroprotective AgentsMutationsymbolsOriginal ArticleSequence motifIntracellularCell Death and Disease
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Study of surface carbohydrates on isolated Golgi subfractions by fluorescent-lectin binding and flow cytometry

1995

The Golgi complex is a functionally heterogeneous subcellular structure that plays a key role in the synthesis, maturation, and sorting of newly synthesized glycoproteins. Fluorescent lectins have been used extensively to analyze surface glycoproteins by flow cytometry in whole cells and more recently in isolated subcellular organelles, such as mitochondria and chloroplasts. We report here the use of several fluorescein-isothiocyanate-conjugated lectins to detect and quantify specific surface sugars by flow cytometry on isolated elements from purified cis and trans-Golgi fractions from rat liver. Our results show that this approach may be useful to study Golgi composition and function, sinc…

CarbohydratesBiophysicsGolgi ApparatusPathology and Forensic MedicineFlow cytometrysymbols.namesakeEndocrinologyIsothiocyanatesLectinsOrganellemedicineAnimalsRats WistarFluorescent Dyeschemistry.chemical_classificationMembrane Glycoproteinsbiologymedicine.diagnostic_testIntracellular MembranesCell BiologyHematologyGolgi apparatusFlow CytometryWheat germ agglutininRatsChloroplastLiverBiochemistrychemistryConcanavalin Asymbolsbiology.proteinGlycoproteinFunction (biology)Protein BindingCytometry
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Sites of sulfatation in the chondrocytes of the articular cartilage of the rabbit

1977

35S sulfate uptake by the articular cartilage chondrocytes, from biopsies of rabbit, have been studied by high resolution autoradiography. The Golgi apparatus, rough endoplasmic reticulum, cytosol, cytoplasmic membrane and extracellular space were considered as cell compartments in the quantitative analysis of the autoradiograms. The results obtained show: 1) a high activity of radiosotope incorporation in the Golgi apparatus; 2) a fast rhythm of transfer of the substances labelled in the Golgi apparatus to the cell membrane; 3) significant labelling of the rough endoplasmic reticulum, throughout the experiment. It is concluded: 1) The grains observed in the rough endoplasmic reticulum show…

Cartilage ArticularSulfatesChemistryEndoplasmic reticulumCell MembraneCellGolgi ApparatusGolgi apparatusEndoplasmic ReticulumPathology and Forensic MedicineCell biologyCell membraneMicroscopy Electronsymbols.namesakeCytosolCytosolmedicine.anatomical_structureCytoplasmmedicinesymbolsExtracellularAnimalsAutoradiographyRabbitsQuantitative analysis (chemistry)Virchows Archiv B Cell Pathology
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Reversible stress-induced lipid body formation in fast twitch rat myofibers

2012

We analyzed the existence of lipid bodies (LBs) in the fast twitch rat flexor digitorum brevis (FDB) myofibers and found that these structures were scarce. However, isolation procedure of the myofibers, heath shock, viral infection or the glycosylation inhibitor tunicamycin induced formation of the LBs, which were stationary structures flanking Z lines. We next infected FDB myofibers with recombinant Semliki Forest virus expressing caveolin 3-yellow fluorescent protein (cav3-YFP) since this chimeric protein was targeted to the LBs facilitating their further analysis. Photobleaching experiments showed that the LBs recovered cav 3-YFP extremely slowly, indicating that they were not continuous…

Caveolin 3Blotting WesternGolgi ApparatusBiologyEndoplasmic ReticulumSemliki Forest virusRats Sprague-Dawleychemistry.chemical_compoundSarcolemmaBacterial ProteinsAnimalsCells CulturedSarcolemmaLipogenesisEndoplasmic reticulumCell BiologyTunicamycinBrefeldin AEndoplasmic Reticulum StressLipid Metabolismmusculoskeletal systembiology.organism_classificationFusion proteinRatsCell biologyCaveolin 3Luminescent ProteinsProtein TransportSarcoplasmic ReticulumCholesterolBiochemistrychemistryMuscle Fibers Fast-TwitchVirusesUnfolded protein responseFemaleExperimental Cell Research
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Interaction of Neuronal Calcium Sensor-1 (NCS-1) with Phosphatidylinositol 4-Kinase β Stimulates Lipid Kinase Activity and Affects Membrane Trafficki…

2001

Phosphatidylinositol 4-kinases (PI4K) catalyze the first step in the synthesis of phosphatidylinositol 4,5-bisphosphate, an important lipid regulator of several cellular functions. Here we show that the Ca(2+)-binding protein, neuronal calcium sensor-1 (NCS-1), can physically associate with the type III PI4Kbeta with functional consequences affecting the kinase. Recombinant PI4Kbeta, but not its glutathione S-transferase-fused form, showed enhanced PI kinase activity when incubated with recombinant NCS-1, but only if the latter was myristoylated. Similarly, in vitro translated NCS-1, but not its myristoylation-defective mutant, was found associated with recombinant- or in vitro translated P…

Cell Membrane PermeabilityLipoproteinsNeuronal Calcium-Sensor ProteinsLipid kinase activityBiologyPhosphatidylinositolsbehavioral disciplines and activitiesBiochemistrychemistry.chemical_compoundsymbols.namesakePhosphatidylinositol PhosphatesChlorocebus aethiopsmental disordersAnimalsCalcium SignalingPhosphatidylinositol1-Phosphatidylinositol 4-KinaseMolecular BiologyCellular compartmentMyristoylationKinaseCalcium-Binding ProteinsCell MembraneNeuropeptidesBiological TransportCell BiologyTransfectionGolgi apparatusCell CompartmentationRatsCell biologychemistryBiochemistryNeuronal calcium sensor-1COS Cellssymbolsbiology.proteinCattleMyristic AcidsProtein Processing Post-TranslationalProtein BindingJournal of Biological Chemistry
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SPHINGOLIPID TRANSPORT FROM THE TRANSGOLGI NETWORK TO THE APICAL SURFACE IN PERMEABILIZED MDCK CELLS

1992

AbstractWe have measured the transport of de novo synthesized fluorescent analogs of sphingomyelin and glucosylceramide from the trans-Golgi network (TGN) to the apical membrane in basolaterally permeabilized Madin-Darby canine kidney (MDCK) cells. Sphingolipid transport was temperature, ATP and cytosol dependent. Introduction of bovine serum albumin (BSA), which binds fluorescent sphingolipid monomer, into the permeabilized cells, did not affect lipid transport to the apical membrane. Both fluorescent sphingomyelin and glucosylceramide analogs were localized to the lumenal bilayer leaflet of isolated TGN-derived vesicles. These results strongly suggest that both sphingolipids are transport…

Cell Membrane PermeabilityTrans Golgi networkBiophysicsGolgi ApparatusBiologyGlucosylceramidesKidneyBiochemistryCell Linesymbols.namesakeMembrane LipidsDogsStructural BiologyApical membraneGeneticsAnimalsBovine serum albuminStreptolysin OMolecular BiologyLipid TransportSphingolipidsVesicleBiological TransportSerum Albumin BovineCell BiologyGolgi apparatusApical membraneSphingolipid transportSphingolipidSphingomyelinscarbohydrates (lipids)CytosolPermeabilized cellBiochemistryFluorescent lipid analogsymbolsBiophysicsbiology.proteinlipids (amino acids peptides and proteins)SphingomyelinMDCK cell
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The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Mod…

2012

BACKGROUND: In a previous work we showed for the first time that human tumor cells secrete Hsp60 via exosomes, which are considered immunologically active microvesicles involved in tumor progression. This finding raised questions concerning the route followed by Hsp60 to reach the exosomes, its location in them, and whether Hsp60 can be secreted also via other mechanisms, e.g., by the Golgi. We addressed these issues in the work presented here. PRINCIPAL FINDINGS: We found that Hsp60 localizes in the tumor cell plasma membrane, is associated with lipid rafts, and ends up in the exosomal membrane. We also found evidence that Hsp60 localizes in the Golgi apparatus and its secretion is prevent…

Cell Physiologyanimal structuresAnatomy and PhysiologyHistologylcsh:MedicineGolgi ApparatusBiologyExosomesBiochemistrysymbols.namesakeCytosolMembrane MicrodomainsDiagnostic MedicineCell Line TumorOrganelleMolecular Cell BiologyPathologyHumansSecretionlcsh:ScienceLipid raftBiologyhsp60 exosomeOrganellesMultidisciplinarylcsh:RfungiChaperonin 60Golgi apparatusMicrovesiclesCellular StructuresTransport proteinCell biologyProtein TransportMembrane proteinSubcellular OrganellesTumor progressionsymbolsCytochemistryMedicinelcsh:QMembranes and SortingExtracellular SpaceBiomarkersResearch ArticleGeneral PathologyPLoS ONE
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The ARF GAPs ELMOD1 and ELMOD3 act at the Golgi and cilia to regulate ciliogenesis and ciliary protein traffic

2022

ELMODs are a family of three mammalian paralogs that display GTPase activating protein (GAP) activity towards a uniquely broad array of ADP-ribosylation factor (ARF) family GTPases that includes ARF-like (ARL) proteins. ELMODs are ubiquitously expressed in mammalian tissues, highly conserved across eukaryotes, and ancient in origin, being present in the last eukaryotic common ancestor. We described functions of ELMOD2 in immortalized mouse embryonic fibroblasts (MEFs) in the regulation of cell division, microtubules, ciliogenesis, and mitochondrial fusion. Here, using similar strategies with the paralogs ELMOD1 and ELMOD3, we identify novel functions and locations of these cell regulators a…

Cell divisionGTPase-activating proteinGolgi ApparatusGTPaseBiologyMicrotubulesMitochondrial Dynamicssymbols.namesakeMiceMicrotubuleCiliogenesisAnimalsCiliaMolecular BiologyADP-Ribosylation FactorsCiliumGTPase-Activating ProteinsCorrectionCell BiologyGolgi apparatusFibroblastsCell biologyCytoskeletal Proteinsmitochondrial fusionsymbolsSignal Transduction
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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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Efectos de la exposición crónica al etanol sobre el tráfico intracelular y citoesqueleto como factores implicados en la migración neuronal

2013

El consumo de etanol durante la gestación puede inducir una serie de alteraciones graves en el desarrollo del feto, la manifestación más extrema da lugar al Síndrome Alcohólico Fetal (SAF). La exposición prenatal al alcohol es la causa conocida y, además evitable, más importante de retraso mental en el mundo occidental. Además de déficits cognitivos, los niños con SAF presentan múltiples anomalías estructurales en el sistema nervioso central, como reducción de la masa cerebral, y a nivel celular, daños en la migración neuronal, en el proceso de formación de espinas dendríticas y establecimiento de sinapsis. En la actualidad, los mecanismos moleculares implicados en la teratogénesis inducida…

Central Nervous Systemaparato de Golgietanolespinas dendríticasneuronasneurons:CIENCIAS DE LA VIDA::Neurociencias [UNESCO]migración neuronalMAP2Fetal Alcoholic SyndromeRho GTPasasactinaRho GTPasesendocitosis:CIENCIAS MÉDICAS::Toxicología [UNESCO]endocytosismicrotúbuloneuronal migrationUNESCO::CIENCIAS MÉDICAS::Toxicologíatráfico intracelularUNESCO::CIENCIAS DE LA VIDA::Biología celular::Cultivo celularcytoskeletondendritic spinesSAFSíndrome Alcohólico Fetalcitoesqueleto:CIENCIAS DE LA VIDA::Biología celular::Cultivo celular [UNESCO]Golgi apparatusUNESCO::CIENCIAS DE LA VIDA::Neurocienciasethanolintracellular trafficactinSistema Nervioso Centralmicrotubule
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