Search results for "Vesicular Transport Protein"

showing 10 items of 40 documents

High Lymph Vessel Density and Expression of Lymphatic Growth Factors in Peritoneal Endometriosis

2012

To investigate the occurrence of lymph vessels and lymphangiogenic growth factors in peritoneal lesions, we performed immunohistochemical staining of peritoneal lesions of 37 patients with antibodies against podoplanin (D2-40), lymphatic vessel endothelial hyaluronan receptor 1 (LYVE-1), prospero homeobox protein 1 (Prox-1), vascular epithelial growth factor (VEGF)-C/VEGF-D. Overall, 10 lesions were double stained against D2-40 and von Willebrand factor. The lymph vessel density in peritoneal lesion was significantly higher in comparison with healthy peritoneum. All lymph vessel makers could be detected, whereby the lymph vessel density of LYVE-1- and Prox-1-positive lymph vessels was signi…

Pathologychronic inflammatory proceMacrophageVascular Endothelial Growth Factor CVascular Endothelial Growth Factor DVesicular Transport ProteinsFluorescent Antibody TechniquePeritoneal DiseasesAntibodies Monoclonal Murine-Derivedlymphatic disseminationIntercellular Signaling Peptides and ProteinEndometriosiEndothelial CellObstetrics and GynecologyHomeodomain ProteinMiddle AgedImmunohistochemistryLymphangiogenesisLymphatic systemmedicine.anatomical_structureVascular endothelial growth factor CIntercellular Signaling Peptides and ProteinsFemaleLymphEndothelium LymphaticHumanAdultmedicine.medical_specialtyEndometriosisendometriosis; lymphatic dissemination; chronic inflammatory processlymphangiogenesiperitoneal endometriosiLymphatic VesselVesicular Transport ProteinPeritoneummedicineLymphatic vesselLymph node stromal cellHumansLymph sacsLymphatic VesselsHomeodomain ProteinsTumor Suppressor Proteinbusiness.industryMacrophagesTumor Suppressor ProteinsEndothelial CellsBiomarkerchronic inflammatory processPeritoneal DiseasebusinessBiomarkersReproductive Sciences
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An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.

2016

Cellular organelles provide opportunities to relate biological mechanisms to disease. Here we use affinity proteomics, genetics and cell biology to interrogate cilia: poorly understood organelles, where defects cause genetic diseases. Two hundred and seventeen tagged human ciliary proteins create a final landscape of 1,319 proteins, 4,905 interactions and 52 complexes. Reverse tagging, repetition of purifications and statistical analyses, produce a high-resolution network that reveals organelle-specific interactions and complexes not apparent in larger studies, and links vesicle transport, the cytoskeleton, signalling and ubiquitination to ciliary signalling and proteostasis. We observe sub…

Proteomics0301 basic medicineSystems AnalysisDNA Mutational Analysislnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4]General Physics and AstronomyDatasets as Topicmethods [Chromatography Affinity]ProteomicsSensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Chromatography AffinityMass SpectrometryProtein Interaction Mappingtherapy [Ciliopathies]genetics [Ciliopathies]methods [Molecular Targeted Therapy]Molecular Targeted TherapyProtein Interaction MapsMultidisciplinaryCiliumChemistry (all)Qabnormalities [Spine]pathology [Ciliopathies]genetics [Muscle Hypotonia]therapy [Muscle Hypotonia]Metabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]metabolism [Proteins]isolation & purification [Proteins]physiology [Biological Transport]3. Good healthCell biologyVesicular transport proteinpathology [Dwarfism]metabolism [Cilia]Muscle Hypotoniaddc:500pathology [Muscle Hypotonia]pathology [Spine]genetics [Dwarfism]Rare cancers Radboud Institute for Health Sciences [Radboudumc 9]ScienceDwarfismExocystBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyPhysics and Astronomy (all)03 medical and health sciencesIntraflagellar transportCiliogenesisOrganelleHumansCiliaBiochemistry Genetics and Molecular Biology (all)ProteinsBiological TransportGeneral Chemistrytherapy [Dwarfism]Fibroblastsgenetics [Proteins]CiliopathiesSpinemethods [Protein Interaction Mapping]Renal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]030104 developmental biologyProteostasisHEK293 Cellsmethods [Proteomics]
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Reconstitution of vesicular transport to Rab11-positive recycling endosomes in vitro.

2003

Rab GTPases are key regulators of vesicular protein transport in both the endocytic and exocytic pathways. In endocytosis and recycling, Rab11 plays a role in receptor recycling to plasma membrane via the pericentriolar recycling compartment. However, little is known about the molecular requirements and partners that promote transport through Rab11-positive recycling endosomes. Here, we report a novel approach to reconstitute transport to immunoabsorbed recycling endosomes in vitro. We show that transport is temperature-, energy-, and time-dependent and requires the presence of Rab proteins, as it is inhibited by the Rab-interacting protein Rab GDP-dissociation inhibitor that removes Rab pr…

Receptor recyclingCytochalasin DEndosomeEndocytic cycleBiophysicsVesicular Transport ProteinsCHO CellsEndosomesEndocytosisBiochemistryCricetulusCricetinaeReceptors TransferrinAnimalsVesicular Protein TransportTransport VesiclesMolecular BiologyGuanine Nucleotide Dissociation InhibitorsChemistryCell BiologyActin cytoskeletonAdaptation PhysiologicalCell biologyVesicular transport proteinProtein Transportrab GTP-Binding ProteinsRabBiochemical and biophysical research communications
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Vesicle transport and photoreceptor death: fishing for molecular links.

2013

Intracellular vesicle transport defects can induce retinal degeneration and photoreceptor cell death, but the molecular connections between these processes remains poorly understood. Reporting in Developmental Cell, Nishiwaki et al. (2013) suggest that a vesicle fusion cis-SNARE complex component translates vesicular transport defects into photoreceptor cell apoptosis.

Retinal degenerationVesicle fusionLipid bilayer fusionIntracellular vesicleApoptosisCell BiologyBiologymedicine.diseaseMembrane FusionGeneral Biochemistry Genetics and Molecular BiologyPhotoreceptor cellCell biologyVesicular transport proteinSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteinsmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2ApoptosismedicineRetinal Cone Photoreceptor CellsAnimalsMolecular BiologyDevelopmental BiologyDevelopmental cell
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Regulation of the hDlg/hScrib/Hugl-1 tumour suppressor complex.

2008

The proper function of the Scribble tumour suppressor complex is dependent upon the correct localisation of its components. Previously we observed dynamic relocalisation of the hDlg component under conditions of osmotic stress. We now show that the other two components of the complex, hScrib and Hugl-1 display similar patterns of expression. We demonstrate, by shRNA ablation of hScrib expression, that hDlg and Hugl-1 are in part dependent upon hScrib for their correct localization. However under conditions of osmotic stress this apparent dependency no longer exists: hDlg and Hugl-1 localise to cell membranes independently of hScrib. We also demonstrate an interaction between the three compo…

SCRIBBlotting WesternBiologylaw.inventionCell LineSmall hairpin RNADiscs Large Homolog 1 ProteinlawSyntaxinAnimalsHumansSorbitolTransport VesiclesAdaptor Proteins Signal TransducingRegulation of gene expressionQa-SNARE ProteinsTumor Suppressor ProteinsOsmolar ConcentrationSignal transducing adaptor proteinMembrane ProteinsCell BiologyTransport proteinCell biologyVesicular transport proteinCytoskeletal ProteinsProtein TransportGene Expression RegulationMultiprotein ComplexesSuppressorRNA InterferenceSignal TransductionExperimental cell research
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Direct binding of Magi2 to the USH1G protein SANS links the periciliary USH protein network to endocytosis

2012

The human Usher syndrome (USH) is the most common form of combined deaf-blindness. The encoded molecules are integrated into protein networks by scaffolds including the USH1G protein SANS (scaffold protein containing ankyrin repeats and SAM domain). Previous studies indicated SANS´ participation in vesicle transport and cargo handover at the periciliary region of photoreceptor cells. To decipher the precise cellular role of SANS, we searched for interacting partners. Therefore we adopted a yeast-2-hybrid screen of a retinal cDNA library using SANS´ C-terminus as bait. Amongst others we identified the MAGUK protein Magi2 (membrane-associated guanylate kinase inverted-2) as putative binding p…

Scaffold proteinImmunoelectron microscopyCell BiologyBiologyEndocytosisInteractomePhotoreceptor cellCell biologyVesicular transport proteinmedicine.anatomical_structureCiliary pocketPoster PresentationmedicineAnkyrin repeatCilia
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The Synapse-Like Interaction between Chloroplast, dictyosome, and Other Cell Compartments during Increased Ethylene Production in Leaves of Rye (Seca…

2000

Rye (Secale cereale L.) plants were treated with an ethylene releaser ethephon (2-chloroethylphosphonic acid) in concentration of 4×10−2 M. We studied electron microscopically, if and how chloroplasts interact with well-documented sites of ethylene production/binding, i.e., with endoplasmic reticulum, dictyosomes, mitochondria, plasma membrane, and tonoplast. During the sharp increase of ethylene synthesis in mesophyll cells of rye leaves, the direct local continguity of chloroplast envelope or envelope protrusions with the above mentioned cell compartments was typical. Moreover, a large number and diversity of versatile chloroplast-dictyosome associations were conspicuous, in which both th…

SecalePhysiologyEndoplasmic reticulumfood and beveragesPlant ScienceVacuoleGolgi apparatusBiologybiology.organism_classificationChloroplast membraneApoplastChloroplastVesicular transport proteinsymbols.namesakeBiochemistryBiophysicssymbolsPhotosynthetica
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Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

2013

AbstractExit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER.

Vesicular Transport ProteinsBiophysicsEndoplasmic ReticulumBiochemistryCell LineVesicular Transport ProteinGeneticStructural BiologyERESGeneticsVesicular Transport ProteinsHumansCOPIIEndoplasmic Reticulum StreMolecular BiologyCOPIIChemistryVesicleEndoplasmic reticulumSec23Cell BiologyCOP-Coated VesiclesSEC23AEndoplasmic Reticulum StressCell biologyBiophysicUnfolded protein responseER streProtein foldingCOP-Coated VesiclesER stressCOP-Coated VesicleHumanProtein BindingFEBS Letters
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Immunoelectron Microscopy of Vesicle Transport to the Primary Cilium of Photoreceptor Cells

2009

Cilia are organelles of high structural complexity. Since the biosynthetic machinery is absent from cilia all their molecular components must be synthesized in organelles of the cytoplasm and subsequently transported to the cilium. Ciliary cargos are thought to be translocated in the membrane of transport vesicles or association with these vesicles to the base of the cilium where the vesicles fuse with the periciliary target membrane for further delivery of their cargo into the ciliary compartment by the intraflagellar transport (IFT). Here we describe a modified preembedding labeling method as an alternative technique to conventional postembedding methods eligible for analyses of ciliary c…

Vesicular transport proteinImmunolabelingCytoplasmIntraflagellar transportCiliumVesicleImmunoelectron microscopyOrganellesense organsBiologyCell biology
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Huntingtin controls neurotrophic support and survival of neurons by enhancing BDNF vesicular transport along microtubules.

2004

AbstractPolyglutamine expansion (polyQ) in the protein huntingtin is pathogenic and responsible for the neuronal toxicity associated with Huntington's disease (HD). Although wild-type huntingtin possesses antiapoptotic properties, the relationship between the neuroprotective functions of huntingtin and pathogenesis of HD remains unclear. Here, we show that huntingtin specifically enhances vesicular transport of brain-derived neurotrophic factor (BDNF) along microtubules. Huntingtin-mediated transport involves huntingtin-associated protein-1 (HAP1) and the p150Glued subunit of dynactin, an essential component of molecular motors. BDNF transport is attenuated both in the disease context and b…

congenital hereditary and neonatal diseases and abnormalitiesHuntingtinCell SurvivalContext (language use)Nerve Tissue ProteinsMicrotubulesModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyMiceNeurotrophic factorsmental disordersHuntingtin ProteinAnimalsCells CulturedNeuronsHuntingtin ProteinbiologyBiochemistry Genetics and Molecular Biology(all)Huntingtin-associated protein 1Brain-Derived Neurotrophic FactorCytoplasmic VesiclesBrainNuclear ProteinsBiological TransportDynactin ComplexCell biologynervous system diseasesVesicular transport proteinDNA-Binding ProteinsBiochemistrynervous systembiology.proteinDynactinMicrotubule-Associated ProteinsNeurotrophinCell
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