Search results for "Secretor"

showing 10 items of 159 documents

Intestinal drug efflux: formulation and food effects

2001

The intestine, primarily regarded as an absorptive organ, is also prepared for the elimination of certain organic acids, bases and neutral compounds depending on their affinity to intestinal carrier systems. Several of the transport systems known to mediate efflux in the major clearing organs--liver and kidney--are also expressed in the intestine. Examples of secretory transporters in the intestine are P-glycoprotein, members of the multidrug resistance associated protein family, breast cancer resistance protein, organic cation transporters and members of the organic anion polypeptide family. In this communication, the P-glycoprotein mediated intestinal secretion of talinolol, a model compo…

Drug CarriersIntestinal permeabilityOrganic cation transport proteinsbiologyPharmaceutical ScienceIleummedicine.diseaseRatsJejunumFood-Drug Interactionsmedicine.anatomical_structureSecretory proteinIntestinal AbsorptionPharmaceutical PreparationsBiochemistrybiology.proteinmedicineAnimalsHumansEffluxIntestinal MucosaDrug metabolismP-glycoproteinAdvanced Drug Delivery Reviews
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Biosynthesis of ecdysones in isolated prothoracic glands and oenocytes of Tenebrio molitor in vitro.

1974

Abstract Isolated prothoracic glands from Tenebrio larvae synthesize in vitro α-ecdysone, but not β-ecdysone from 4-14C-cholesterol. Isolated abdominal oenocytes from the larvae synthesize mainly β-ecdysone, but only little α-ecdysone. When prothoracic glands and oenocytes are cultured together, the α-ecdysone derived from the prothoracic glands is oxidized by the oenocytes to β-ecdysone. The newly synthesized hormones are not stored in the cells, but are secreted into the medium if sufficient amounts of non-labelled hormones are present. If no unlabelled hormones are added to the culture medium, the newly formed hormones are converted to a large extent into polar conjugates.

EcdysonePhysiologyBiologyProthoracic glandNeurosecretory SystemsIn vitrochemistry.chemical_compoundBiochemistryBiosynthesischemistryInsect ScienceCulture TechniquesLarvaAbdomenAnimalsTenebrioHormoneJournal of insect physiology
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3D-Ultrastructure, Functions and Stress Responses of Gastropod (Biomphalaria glabrata) Rhogocytes

2014

Rhogocytes are pore cells scattered among the connective tissue of different body parts of gastropods and other molluscs, with great variation in their number, shape and size. They are enveloped by a lamina of extracellular matrix. Their most characteristic feature is the "slit apparatus", local invaginations of the plasma membrane bridged by cytoplasmic bars, forming slits of ca. 20 nm width. A slit diaphragm creates a molecular sieve with permeation holes of 20×20 nm. In blue-blooded gastropods, rhogocytes synthesize and secrete the respiratory protein hemocyanin, and it has been proposed-though not proven-that in the rare red-blooded snail species they might synthesize and secrete the he…

Electron Microscope TomographyRespiratory SystemCell PoresProtein SynthesisBiochemistryNucleic AcidsTissue DistributionHemoproteinsSecretory PathwayMultidisciplinaryBiomphalariabiologyQRImmunogold labellingAnatomyEndoplasmic ReticulaEndocytosisBody FluidsExtracellular MatrixCell biologyRespiratory proteinProtein TransportConnective TissueCell ProcessesSlit diaphragmMedicineAnatomyCellular Structures and OrganellesCellular TypesResearch ArticleCadmiumProtein StructureHistologyScienceMolecular Sequence DataBiosynthesisProtein ChemistryExocytosisNephrinImaging Three-DimensionalStress PhysiologicalAnimalsBiomphalaria glabrataAmino Acid SequenceEvolutionary BiologyCell MembraneBiology and Life SciencesProteinsMembrane ProteinsGlobulinsCell Biologybiology.organism_classificationCytoskeletal ProteinsBiological TissueMembrane proteinCytoplasmUltrastructurebiology.proteinExtracellular SpaceRibosomesZoologyPLoS ONE
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Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles.

1999

Here, to study lipid-protein interactions that contribute to the biogenesis of regulated secretory vesicles, we have developed new approaches by which to label proteins in vivo, using photoactivatable cholesterol and glycerophospholipids. We identify synaptophysin as a major specifically cholesterol-binding protein in PC12 cells and brain synaptic vesicles. Limited cholesterol depletion, which has little effect on total endocytic activity, blocks the biogenesis of synaptic-like microvesicles (SLMVs) from the plasma membrane. We propose that specific interactions between cholesterol and SLMV membrane proteins, such as synaptophysin, contribute to both the segregation of SLMV membrane constit…

Endocytic cycleSynaptophysinKidneyTritiumSynaptic vesiclePC12 CellsExocytosisR-SNARE ProteinsAnimalsHumansNeuronsVAMP2biologyCell MembraneMembrane ProteinsCell BiologySecretory VesicleMicrovesiclesEndocytosisCell biologyRatsCholesterolMembrane proteinSynaptophysinbiology.proteinPhosphatidylcholinesSynaptic VesiclesBiogenesisSynaptosomesNature cell biology
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Sorting of a secretory protein (gp80) to the apical surface of Caco-2 cells

1994

We have investigated the synthesis and polarized secretion of the exogenous gp80 glycoprotein complex in the human epithelial adenocarcinoma cell line, Caco-2. gp80 is secreted at the apical surface of Madin-Darby canine kidney (MDCK) cells and should, therefore, display the signal(s) required for sorting into the apical exocytic pathway. In Caco-2 cells, no bona fide secretory protein released preferentially at the apical surface has been described so far. To address the question of whether Caco-2 cells possess a machinery capable of delivery of secretory proteins at the apical surface, we stably transfected the cells with a recombinant gene coding for the gp80 glycoprotein complex. Pulse-…

Gene ExpressionBiologyTransfectionCell LineDogsGlycoprotein complexCell polarityTumor Cells CulturedAnimalsHumansSecretionchemistry.chemical_classificationMembrane GlycoproteinsCell MembraneCell PolarityCell BiologyTransfectionApical membraneReceptors Interleukin-6Molecular biologyCell biologyPhenotypeSecretory proteinchemistryCell cultureGlycoproteinJournal of Cell Science
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LRP1 modulates APP trafficking along early compartments of the secretory pathway

2008

The amyloid beta peptide (A beta) is a central player in Alzheimer's disease (AD) pathology. A beta liberation depends on APP cleavage by beta- and gamma-secretases. The low density lipoprotein receptor related protein 1 (LRP1) was shown to mediate APP processing at multiple steps. Newly synthesized LRP1 can interact with APP, implying an interaction between these two proteins early in the secretory pathway. We wanted to investigate whether LRP1 mediates APP trafficking along the secretory pathway, and, if so, whether it affects APP processing. Indeed, the early trafficking of APP within the secretory pathway is strongly influenced by its interaction with the C-terminal domain of LRP1. The …

GlycosylationAmyloid betaAmino Acid MotifsPlaque AmyloidCHO CellsSecretory pathwayTrafficinglcsh:RC321-571Amyloid beta-Protein PrecursorCricetulusAlzheimer DiseaseCricetinaemental disordersAmyloid precursor proteinAnimalsHumansReceptorlcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySecretory pathwayNeuronsAmyloid beta-PeptidesbiologyLow density lipoprotein receptor related proteinBrainLRP1Cell CompartmentationProtein Structure TertiaryCell biologyProtein TransportNeurologyBiochemistryAlpha secretaseRetentionAmyloid precursor proteinLDL receptorbiology.proteinLiberationProtein Processing Post-TranslationalLow Density Lipoprotein Receptor-Related Protein-1Signal TransductionNeurobiology of Disease
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A role for the immunoglobulin-like domain of the human IL-6 receptor. Intracellular protein transport and shedding.

1999

Interleukin (IL)-6, IL-11 and cililary neurotrophic factor (CNTF) belong to the same family of hematopoietic and neurotrophic cytokines. Their receptor complexes contain a cytokine-binding alpha receptor and the common glycoprotein (gp)130 subunit for signal transduction. The extracellular parts of the alpha-receptor subunits consist of a membrane-proximal cytokine-binding domain and an N-terminal immunoglobulin (Ig)-like domain with unknown function. We examined the role of the Ig-like domain of IL-6R by constructing deletion mutants lacking the Ig domain (IL-6RDeltaIg and soluble IL-6RDeltaIg). IL-6RDeltaIg was shed as effectively as wild-type IL-6R from transfected COS-7 cells upon 4beta…

GlycosylationTime FactorsImmunoglobulin domainBiologyTransfectionBiochemistryModels BiologicalCell LineMiceAnimalsHumansSecretionSecretory pathwayMembrane GlycoproteinsDose-Response Relationship DrugInterleukin-6Lysosome-Associated Membrane GlycoproteinsTransfectionGlycoprotein 130Flow CytometryMolecular biologyReceptors Interleukin-6Transmembrane proteinRecombinant ProteinsCell biologyInterleukin-6 receptorCOS CellsTetradecanoylphorbol AcetateSignal transductionSignal TransductionEuropean journal of biochemistry
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Retention mechanisms for ER and Golgi membrane proteins

2014

Unless there are mechanisms to selectively retain membrane proteins in the endoplasmic reticulum (ER) or in the Golgi apparatus, they automatically proceed downstream to the plasma or vacuole membranes. Two types of coat protein complex I (COPI)-interacting motifs in the cytosolic tails of membrane proteins seem to facilitate membrane retention in the early secretory pathway of plants: a dilysine (KKXX) motif (which is typical of p24 proteins) for the ER and a KXE/D motif (which occurs in the Arabidopsis endomembrane protein EMP12) for the Golgi apparatus. The KXE/D motif is highly conserved in all eukaryotic EMPs and is additionally present in hundreds of other proteins of unknown subcellu…

Golgi membraneSecretory PathwayKKXXMolecular Sequence DataGolgi ApparatusMembrane ProteinsGolgi TargetingPlant ScienceCOPIGolgi apparatusBiologyEndoplasmic ReticulumCoat Protein Complex ICell biologysymbols.namesakeMembrane proteinPlant CellssymbolsAmino Acid SequenceIntegral membrane proteinSecretory pathwayTrends in Plant Science
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Deletions in the hepatitis B virus small envelope protein: effect on assembly and secretion of surface antigen particles

1992

The small envelope S protein of hepatitis B virus carrying the surface antigen has the unique property of mobilizing cellular lipids into empty envelope particles which are secreted from mammalian cells. We studied the biogenesis of such particles using site-directed mutagenesis. In this study, we describe the effect of deletions in the N-terminal hydrophobic and hydrophilic domains of the S protein. Whereas short overlapping deletions of hydrophilic sequences flanking the first hydrophobic domain were tolerated, larger deletions of the same sequences were not. Conversely, the hydrophilic region preceding the second hydrophobic domain was not permissive for even short deletions. Deletion of…

Hepatitis B virusMolecular Sequence DataImmunologyMutantMutagenesis (molecular biology technique)Biologymedicine.disease_causeMicrobiologyViral Envelope ProteinsViral envelopeVirologymedicineInterleukin 9SecretionCloning MolecularCells CulturedSecretory pathwayMutationHepatitis B Surface AntigensBase SequenceTunicamycinEndoplasmic reticulumPrecipitin TestsMolecular biologyInsect ScienceMutagenesis Site-DirectedChromosome DeletionPlasmidsResearch ArticleJournal of Virology
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Protein delivery by subviral particles of human cytomegalovirus

2003

Direct protein delivery is an emerging technology in vaccine development and gene therapy. We could previously show that subviral dense bodies (DB) of human cytomegalovirus (HCMV), a beta-herpesvirus, transport viral proteins into target cells by membrane fusion. Thus these non-infectious particles provide a candidate delivery system for the prophylactic and therapeutic application of proteins. Here we provide proof of principle that DB can be modified genetically. A 55 kDa fusion protein consisting of the green fluorescent protein and the neomycin phosphotransferase could be packed in and delivered into cells by recombinant DB in a functional fashion. Furthermore, transfer of protein into …

Human cytomegalovirusRecombinant Fusion ProteinsGenetic enhancementGenetic VectorsGreen Fluorescent ProteinsCongenital cytomegalovirus infectionCytomegalovirusGene ExpressionBiologylaw.inventionGreen fluorescent proteinlawVaccines DNAGeneticsmedicineHumansMolecular BiologyKanamycin KinaseSecretory VesiclesLipid bilayer fusionDendritic CellsGenetic TherapyFibroblastsmedicine.diseaseFusion proteinVirologyCell biologyLuminescent ProteinsFluorescent Antibody Technique DirectRecombinant DNAMolecular MedicineDelivery systemGenetic EngineeringGene Therapy
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