Search results for "Endopeptidase"

showing 10 items of 361 documents

Alternatively spliced transcripts of the thymus-specific protease PRSS16 are differentially expressed in human thymus.

2004

The putative serine protease PRSS16 is abundantly expressed in the thymic cortex and the gene is encoded within the HLA I complex. Although its function is not yet defined, the very restricted expression points to a role in T-cell development in the thymus. In this study, we show that the PRSS16 mRNA is alternatively spliced to generate at least five transcripts. Apart from the full-length sequence, we found two other isoforms with all putative active site residues of the serine protease, suggesting that those variants may also be functional. Semi-quantitative analysis of the splice variants in different tissue samples revealed a strong correlation between the specific formation of alternat…

Gene isoformAdultMaleThymomamedicine.medical_treatmentImmunologyMolecular Sequence DataMorphogenesisThymus GlandGene Expression Regulation EnzymologicMyasthenia GravisGeneticsmedicineMorphogenesisHumansGeneGenetics (clinical)Serine proteaseMessenger RNAProteasebiologyBase SequenceSerine EndopeptidasesMiddle Agedmedicine.diseaseMolecular biologyMyasthenia gravisIsoenzymesAlternative Splicingbiology.proteinFemaleGenes and immunity
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Endothelin receptor B in trabecular meshwork

2007

Abstract Endothelin-1 (ET-1), the most potent vasoconstrictor known to date, seems to be involved in the pathogenesis of primary open angle glaucoma. ET-1 was found in different tissues of the eye and in high concentrations in the aqueous humour. The effects of ET-1 are mediated by two receptors, ET-A receptor (ET-AR) and ET-B receptor (ET-BR), which are both expressed in bovine trabecular meshwork (TM). ET-1 induced contraction of TM predominantly by activation of ET-AR. This study analyzes the role of ET-BR in TM function and investigates the synthesis of ET-1 by human TM (HTM) cells. The effect of IRL-1620, a specific ET-BR agonist, on contractility of bovine TM (BTM) was investigated wi…

Gene isoformAgonistmedicine.medical_specialtyCarbacholmedicine.drug_classBlotting WesternEndothelin-Converting EnzymesBiologyPolymerase Chain ReactionCellular and Molecular NeuroscienceWestern blotTrabecular MeshworkInternal medicinemedicineAnimalsAspartic Acid EndopeptidasesHumansReceptorCells CulturedEndothelin-1medicine.diagnostic_testReceptors EndothelinAqueous humourEndothelinsMetalloendopeptidasesReceptor Endothelin BMolecular biologyPeptide FragmentsSensory SystemsOphthalmologyEndocrinologymedicine.anatomical_structureCalciumCattlesense organsTrabecular meshworkEndothelin receptormedicine.drugExperimental Eye Research
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A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model

2004

Alzheimer disease (AD) is characterized by excessive deposition of amyloid beta-peptides (A beta peptides) in the brain. In the nonamyloidogenic pathway, the amyloid precursor protein (APP) is cleaved by the alpha-secretase within the A beta peptide sequence. Proteinases of the ADAM family (adisintegrin and metalloproteinase) are the main candidates as physiologically relevant alpha-secretases, but early lethality of knockout animals prevented a detailed analysis in neuronal cells. To overcome this restriction, we have generated transgenic mice that overexpress either ADAM10 or a catalytically inactive ADAM10 mutant. In this report we show that a moderate neuronal overexpression of ADAM10 i…

Genetically modified mousePathologymedicine.medical_specialtyAmyloidAmyloidADAM10BACE1-ASGene ExpressionMice TransgenicHippocampusArticleAmyloid beta-Protein PrecursorMiceAlzheimer DiseaseEndopeptidasesAmyloid precursor proteinmedicineAnimalsAspartic Acid EndopeptidasesHumansbiologybusiness.industryP3 peptideAmyloidosisGeneral Medicinemedicine.diseaseCell biologyEnzyme ActivationDisease Models AnimalCommentarybiology.proteinErratumAlzheimer's diseaseAmyloid Precursor Protein SecretasesbusinessAmyloid precursor protein secretaseJournal of Clinical Investigation
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TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections.

2012

Abstract Proteolytic enzymes are involved in almost all biological processes reflecting their importance in health and disease. The human genome contains nearly 600 protease-encoding genes forming more than 2% of the total human proteome. The serine proteases, with about 180 members, built the oldest and second largest family of human proteases. Ten years ago, a novel serine protease family named the type II transmembrane family (TTSP) was identified. This minireview summarizes the up-to-date knowledge about the still growing TTSPs, particularly focusing on the pathophysiological functions of the family member type II transmembrane serine protease (TMPRSS) 4. Recent studies provided importa…

GeneticsSerine proteaseTMPRSS6ProteasesClinical BiochemistrySerine EndopeptidasesProteolytic enzymesMembrane ProteinsBiologyBiochemistryTransmembrane proteinSerineBiochemistryVirus DiseasesNeoplasmsbiology.proteinHuman proteome projectAnimalsHumansMolecular BiologyMASP1Biological chemistry
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Acanthamoeba isolates belonging to T1, T2, T3, T4 and T7 genotypes from environmental freshwater samples in the Nile Delta region, Egypt.

2006

The free-living amoebae of the genus Acanthamoeba include non-pathogenic and pathogenic species and has been recently classified into 15 different genotypes, T1–T15. In this study, a survey was conducted in order to determine the presence and pathogenic potential of free-living amoebae of Acanthamoeba genus in freshwater sources associated with human activities in the Nile Delta region, Egypt. Identification of Acanthamoeba was based on the morphology of cyst and trophozoite forms and PCR amplification with a genus specific primer pair. The pathogenic potential of Acanthamoeba isolates was characterized using temperature and osmotolerance assays and PCR reactions with two primer pairs speci…

GenotypeVeterinary (miscellaneous)Molecular Sequence DataAcanthamoebaFresh WaterLoboseaPolymerase Chain ReactionMicrobiologylaw.inventionlawPhylogeneticsWater Supplyparasitic diseasesGenotypeAnimalsHumansPathogenRibosomal DNAPolymerase chain reactionPhylogenybiologyOsmolar ConcentrationSerine EndopeptidasesTemperatureSequence Analysis DNAbiology.organism_classificationAcanthamoebaInfectious DiseasesInsect ScienceProtozoaParasitologyEgyptPublic HealthActa tropica
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Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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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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Interplay among Gcn5, Sch9 and mitochondria during chronological aging of wine yeast is dependent on growth conditions.

2015

Saccharomyces cerevisiae chronological life span (CLS) is determined by a wide variety of environmental and genetic factors. Nutrient limitation without malnutrition, i.e. dietary restriction, expands CLS through the control of nutrient signaling pathways, of which TOR/Sch9 has proven to be the most relevant, particularly under nitrogen deprivation. The use of prototrophic wine yeast allows a better understanding of the role of nitrogen in longevity in natural and more demanding environments, such as grape juice fermentation. We previously showed that acetyltransferase Gcn5, a member of the SAGA complex, has opposite effects on CLS under laboratory and winemaking conditions, and is detrimen…

GrapesSaccharomyces cerevisiae ProteinsNitrogenmedia_common.quotation_subjectSaccharomyces cerevisiaeLongevitylcsh:MedicineWineSaccharomyces cerevisiaeMitochondrionYeastsEndopeptidasesAutophagylcsh:ScienceWinemakingmedia_commonHistone AcetyltransferasesCell NucleusMultidisciplinarybiologyEthanollcsh:RLongevityIntracellular Signaling Peptides and ProteinsNutrientsbiology.organism_classificationYeastMitochondriaSAGA complexYeast in winemakingAutophagic cell deathPhenotypeBiochemistryFermentationFermentationlcsh:QProtein KinasesSignal TransductionTranscription FactorsResearch ArticlePLoS ONE
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Single-cell RNA sequencing of SARS-CoV-2 cell entry factors in the preconceptional human endometrium.

2021

Abstract STUDY QUESTION Are SARS-CoV-2 canonical cell entry machinery, consisting of ACE2, TMPRSS2, NRP1 and LY6E, or alternative potential cell entry machinery, consisting of BSG, ANPEP, CD209, CLEC4G, TMPRSS4, TMPRSS11A, FURIN, CTSB, CTSL and IFITM1, expressed in the human endometrium across the menstrual cycle? SUMMARY ANSWER Analysis of cell entry factors for SARS-CoV-2 by single-cell RNA-sequencing (scRNAseq) in the preconceptional human endometrium reveals low risk of infection. WHAT IS KNOWN ALREADY Gene expression datasets from bulk endometrial tissue show no significant expression of the SARS-CoV-2 receptor ACE2 and TMPRSS2. This is in contrast to reported expression of ACE2 at the…

HUTER ProjectCell typeStromal cellvirusesACE2BiologyEndometriumTranscriptomeAndrologyEndometriumPregnancyGene expressionmedicinemedia_common.cataloged_instanceHumansNRP1European unionGeneTMPRSS2media_commonSARS-CoV-2Sequence Analysis RNARehabilitationDeciduaSerine EndopeptidasesObstetrics and Gynecologyvirus diseasesCOVID-19Membrane ProteinsscRNAseqVirus InternalizationAcademicSubjects/MED00905NRPImedicine.anatomical_structureReproductive MedicineFemaleOriginal ArticleHuman reproduction (Oxford, England)
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Inhibition of ubiquitin-dependent proteolysis by a synthetic glycine-alanine repeat peptide that mimics an inhibitory viral sequence.

2002

AbstractThe glycine–alanine repeat (GAr) of the Epstein–Barr virus nuclear antigen-1 is a cis-acting transferable element that inhibits ubiquitin/proteasome-dependent proteolysis in vitro and in vivo. We have here examined the effect of a synthetic 20-mer GAr oligopeptide on the degradation of iodinated or biotin labeled lysozyme in a rabbit reticulocyte lysates in vitro assay. Micromolar concentrations of the GA-20 peptide inhibited the hydrolysis of lysozyme without significant effect on ubiquitination. Addition of the peptide did not inhibit the hydrolysis of fluorogenic substrate by purified proteasomes and did not affect the ubiquitination of lysozyme. An excess of the peptide failed t…

Herpesvirus 4 HumanProteasome Endopeptidase ComplexGly–Ala repeatPolymersProteolysisMolecular Sequence DataBiophysicsGlycineBiotinPeptideBiochemistryIodine Radioisotopeschemistry.chemical_compoundS5aUbiquitinStructural BiologyMultienzyme ComplexesGeneticsmedicineAnimalsAmino Acid SequenceEnzyme InhibitorsMolecular BiologyPeptide sequenceUbiquitinsEpstein–Barr virus nuclear antigen-1Alaninechemistry.chemical_classificationOligopeptideAlaninebiologymedicine.diagnostic_testProteasomeMolecular MimicryUbiquitinationCell BiologyCysteine EndopeptidasesBiochemistryProteasomechemistryEpstein-Barr Virus Nuclear AntigensIsotope Labelingbiology.proteinMuramidaseRabbitsLysozymeCarrier ProteinsPeptidesOligopeptidesFEBS letters
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