Search results for "secret"

showing 10 items of 1132 documents

PSD3 downregulation confers protection against fatty liver disease

2022

Fatty liver disease (FLD) is a growing health issue with burdening unmet clinical needs. FLD has a genetic component but, despite the common variants already identified, there is still a missing heritability component. Using a candidate gene approach, we identify a locus (rs71519934) at the Pleckstrin and Sec7 domain-containing 3 (PSD3) gene resulting in a leucine to threonine substitution at position 186 of the protein (L186T) that reduces susceptibility to the entire spectrum of FLD in individuals at risk. PSD3 downregulation by short interfering RNA reduces intracellular lipid content in primary human hepatocytes cultured in two and three dimensions, and in human and rodent hepatoma cell…

GenotypeEndocrinology Diabetes and MetabolismVARIANTSUSCEPTIBILITYPolymorphism Single NucleotideArticleCell LineMiceRibonucleasesPhysiology (medical)Internal MedicineAnimalsGuanine Nucleotide Exchange FactorsHumansRNA-SeqAllelesNon-alcoholic steatohepatitisNONALCOHOLIC STEATOHEPATITISHERITABILITYGene Expression ProfilingfungiNASHGenetic VariationCell BiologyMetabolic syndromeFatty LiverMetabolismGene Expression RegulationLiverEXOME-WIDE ASSOCIATION3121 General medicine internal medicine and other clinical medicineACIDHepatocytesSECRETIONDisease SusceptibilityVLDLBiomarkersTRIGLYCERIDESNon-alcoholic fatty liver disease
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Secretin—cerulein test and fecal chymotrypsin concentration in children with intestinal giardiasis

1993

We studied six patients with giardiasis (five males, one female), median age 3.5 yr (range 1-11) and 12 healthy control subjects (10 males, 2 females), median age 3.5 yr (range 1-10). Intestinal biopsy and a contemporaneous secretin-cerulein test were performed in all patients, and fecal chymotrypsin was also assayed. Intestinal biopsy was normal in five of the six patients with giardiasis, whereas one of the six presented a partial atrophy of the intestinal villi. The secretin-cerulein test (1 CU/kg of secretin + 75 ng/kg of cerulein) did not show any significant difference between values in the outputs of chymotrypsin, lipase, phospholipase, and bicarbonate obtained in patients and in con…

GiardiasisMalemedicine.medical_specialtyBicarbonatemedicine.disease_causeGastroenterologySecretinFeceschemistry.chemical_compoundEndocrinologyPancreatic JuiceSecretinInternal medicinemedicineChymotrypsinHumansGiardia lambliaLipaseChildPancreasFecesFecal chymotrypsinChymotrypsinbiologyGastroenterologyInfantMetronidazoleEndocrinologyOncologychemistryChild Preschoolbiology.proteinFemaleCeruletidemedicine.drugInternational journal of pancreatology
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Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
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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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Expression and Secretion of Barley Cysteine Endopeptidase B and Cellobiohydrolase I in Trichoderma reesei.

2006

Localization of expression and secretion of a heterologous barley cysteine endopeptidase (EPB) and the homologous main cellobiohydrolase I (CBHI) in a Trichoderma reesei transformant expressing both proteins were studied. The transformant was grown on solid medium with Avicel cellulose and lactose to induce the cbh1 promoter for the synthesis of the native CBHI and the recombinant barley protein linked to a cbh1 expression cassette. Differences in localization of expression between the two proteins were clearly indicated by in situ hybridization, indirect immunofluorescence, and immunoelectron microscopy. In young hyphae, native-size recombinant epb mRNA was localized to apical compartments…

GlycosylationEcologybiologyEndoplasmic reticulumImmunoelectron microscopyfungibiology.organism_classificationApplied Microbiology and BiotechnologyMolecular biologylaw.inventionchemistry.chemical_compoundchemistrylawGene expressionRecombinant DNASecretionHordeum vulgareTrichoderma reeseiFood ScienceBiotechnologyResearch ArticleApplied and environmental microbiology
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Killer toxin of Hanseniaspora uvarum

1990

The yeast Hanseniaspora uvarum liberates a killer toxin lethal to sensitive strains of the species Saccharomyces cerevisiae. Secretion of this killer toxin was inhibited by tunicamycin, an inhibitor of N-glycosylation, although the mature killer protein did not show any detectable carbohydrate structures. Culture supernatants of the killer strain were concentrated by ultrafiltration and the extracellular killer toxin was precipitated with ethanol and purified by ion exchange chromatography. SDS-PAGE of the electrophoretically homogenous killer protein indicated an apparent molecular mass of 18,000. Additional investigations of the primary toxin binding sites within the cell wall of sensitiv…

GlycosylationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaechemical and pharmacologic phenomenaSaccharomyces cerevisiaemedicine.disease_causeHanseniasporaBiochemistryMicrobiologyMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallGeneticsmedicineExtracellularSecretionIsoelectric PointGlucansMolecular BiologyBinding SitesbiologyMolecular massToxinGeneral MedicineTunicamycinMycotoxinsChromatography Ion Exchangebiology.organism_classificationKiller Factors YeastYeastBiochemistrychemistrySaccharomycetalesElectrophoresis Polyacrylamide GelArchives of Microbiology
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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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A comparative study of the incorporation of a 1,6-beta-glucan and an O-glycosylated protein epitope into the cell wall of Candida albicans.

1996

The topological distribution of two epitopes in the cell wall of Candida albicans, the kinetics of their incorporation into the regenerating protoplast wall, and the effect of different antibiotics upon their incorporation and localization have been studied. To do so, two monoclonal antibodies that react against an O-glycosylated mannoprotein (1B12) and against a 1,6-beta-glucan epitope (JRR1) were used. The results show that the JRR1 epitope is localized in an internal layer of the cell wall, in contrast to the 1B12 epitope, which is superficial, and that the incorporation of the JRR1 epitope into walls of regenerating protoplasts precedes that of the 1B12 epitope. The JRR1 epitope is norm…

Glycosylationbeta-Glucansmedicine.drug_classEnzyme-Linked Immunosorbent AssayBiologyMonoclonal antibodyMicrobiologyEpitopeCell wallchemistry.chemical_compoundEpitopesCell WallCandida albicansmedicineSecretionCandida albicansFluorescent Antibody Technique IndirectGlucansMembrane GlycoproteinsLinear epitopeProtoplastsAntibodies MonoclonalTunicamycinbiology.organism_classificationMolecular biologycarbohydrates (lipids)KineticsBiochemistrychemistrybiology.proteinAntibodyMicrobiology (Reading, England)
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Maturation of barley cysteine endopeptidase expressed in Trichoderma reesei is distorted by incomplete processing

2002

Maturation of barley cysteine endopeptidase B (EPB) in Trichoderma reesei was studied with metabolic inhibitors, Western blotting, and immuno microscopy. The inactive 42-kDa recombinant EPB proprotein, first detected in apical cells, was sequentially processed in a time-dependent manner to a secreted polypeptide of 38.5 kDa, and thereafter, to polypeptides of 37.5, 35.5, and 32 kDa exhibiting enzyme activity both in the hyphae and culture medium. The sizes of the different forms of recombinant EPB were in accordance with molecular masses calculated from the deduced amino acid sequence, assuming cleavage at four putative Kex2p sites present in the 42-kDa proprotein. Both the liquid and the z…

GlycosylationglycosylationStereochemistryBlotting WesternMolecular Sequence DataImmunologyApplied Microbiology and BiotechnologyMicrobiologylaw.inventioncysteine proteinasemodified Golgi-like bodychemistry.chemical_compoundlawGeneticsAmino Acid SequenceProproteinMolecular BiologyPeptide sequenceTrichoderma reeseiGlycoproteinsTrichodermachemistry.chemical_classificationbiologyTunicamycinHordeumGeneral MedicineBrefeldin Abiology.organism_classificationKex2pRecombinant ProteinsEnzyme assayEnzyme ActivationMolecular WeightsecretionCysteine EndopeptidasesEnzymechemistryBiochemistryRecombinant DNAbiology.proteinProtein Processing Post-Translational
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Biological protective substances in Marthasterias glacialis (Asteroidea) epidermal secretion

1990

Marthasterias glacialis secretes a watery mucous liquid consisting of 14% carbohydrate and 86% protein. The mucous secretion possesses different biological active molecules responsible for lysozyme-like, protease and haemolytic activities. These substances could constitute a molecular barrier playing a protective role against the penetration by bacteria, fungi and parasites. The secretory apparatus consists of two unicellular glands, a large goblet cell and a granular cell, which open directly into the epidermis.

Goblet cellProteasebiologymedicine.medical_treatmentCarbohydratebiology.organism_classificationMicrobiologymedicine.anatomical_structureGranular cellBiochemistryMucous secretionmedicineAnimal Science and ZoologyMarthasteriasSecretionEcology Evolution Behavior and SystematicsBacteriaJournal of Zoology
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