Search results for "PROTEASES"

showing 10 items of 196 documents

SAR of novel benzothiazoles targeting an allosteric pocket of DENV and ZIKV NS2B/NS3 proteases

2021

In recent years, dengue virus (DENV) and Zika virus (ZIKV), both mosquito-borne members of the Flaviviridae family, have emerged as intercontinental health issues since their vectors have spread from their tropical origins to temperate climate zones due to climate change and increasing globalization. DENV and ZIKV are positive-sense, single-stranded RNA viruses, whose genomes consist of three structural (capsid, membrane precursor, envelope) and seven non-structural (NS) proteins, all of which are initially expressed as a single precursor polyprotein. For virus maturation, the polyprotein processing is accomplished by host proteases and the viral NS2B/NS3 protease complex, whose inhibitors …

Proteasesvirusesmedicine.medical_treatmentClinical BiochemistryAllosteric regulationPharmaceutical ScienceViral Nonstructural ProteinsDengue virusmedicine.disease_causeBiochemistryStructure-Activity RelationshipViral ProteinsFlaviviridaeAllosteric RegulationDrug DiscoveryVirus maturationmedicineHumansProtease InhibitorsBenzothiazolesMolecular BiologyNS3ProteaseDose-Response Relationship DrugMolecular StructurebiologyChemistrySerine EndopeptidasesOrganic Chemistrybiochemical phenomena metabolism and nutritionbiology.organism_classificationVirologyCapsidMolecular MedicineBioorganic & Medicinal Chemistry
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The production of 85 kDa N-terminal fragment of apolipoprotein B in mutant HepG2 cells generated by targeted modification of apoB gene occurs by ALLN…

2010

Abstract To study the mechanism of low levels of full length and truncated apoB in individuals heterozygous for apoB truncation, a non-sense mutation was introduced in one of the three alleles of apob gene of HepG2 cells by homologous recombination. Despite very low levels of apoB-82 (1–2%) in the media, a prominent N-terminal apoB protein of 85 kDa (apoB-15) was secreted that fractionated at d > 1.065 in density gradient ultracentrifugation. The mechanism of production of this short protein was studied by 35S-methionine pulse–chase experiment. Oleate prevented presecretory degradation of apoB-100 in the cell and resulted in increased secretion of newly synthesized apoB-100 with decreases i…

Protein FoldingHepG2Apolipoprotein BLeupeptinsmedicine.medical_treatmentMutantBiophysicsBiologyCysteine Proteinase Inhibitorsdigestive systemBiochemistry85 kDa N-terminalCysteine ProteasesapoBmedicineHumansSecretionMolecular BiologyApolipoproteins BProteasenutritional and metabolic diseasesCell BiologyHep G2 CellsCysteine proteaseMolecular biologyTransmembrane proteinProtein TransportCodon NonsenseHypobetalipoproteinemia Familial Apolipoprotein Bbiology.proteinlipids (amino acids peptides and proteins)Density gradient ultracentrifugationIntracellular
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Sialotranscriptomics of the argasid tick ornithodoros moubata along the trophogonic cycle

2021

32 páginas, 8 tablas, 6 figuras

Proteomics0301 basic medicineSwinePhysiologyRC955-962Gene ExpressionDisease VectorsProteomicsBiochemistryTranscriptomeMedical Conditions0302 clinical medicineTicksArctic medicine. Tropical medicineGene expressionMedicine and Health SciencesHuman relapsing feverGeneticsbiologyEukaryotaGenomicsProteasesBody FluidsEnzymesBloodInfectious DiseasesFemaleMetabolic PathwaysAnatomyPublic aspects of medicineRA1-1270Transcriptome analysisVitellogeninsMetabolic Networks and PathwaysResearch ArticleIxodidaeArthropoda030231 tropical medicineTickSalivary glandsArthropod Proteins03 medical and health sciencesExocrine GlandsOrnithodoros moubataArachnidaGeneticsAnimalsXenobiotic MetabolismTick ControlOrnithodorosSalivaIllumina dye sequencingIxodesAsfarviridaeImmunityOrganismsPublic Health Environmental and Occupational HealthBiology and Life SciencesComputational BiologyProteinsGenome Analysisbiology.organism_classificationInvertebratesOrnithodoros moubataPhospholipases A2Species InteractionsMetabolism030104 developmental biologyAfricaEnzymologyMetalloproteasesAfrican swine feverTranscriptomeDigestive SystemZoology
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Identification of Rothia Bacteria as Gluten-Degrading Natural Colonizers of the Upper Gastro-Intestinal Tract

2011

Background Gluten proteins, prominent constituents of barley, wheat and rye, cause celiac disease in genetically predisposed subjects. Gluten is notoriously difficult to digest by mammalian proteolytic enzymes and the protease-resistant domains contain multiple immunogenic epitopes. The aim of this study was to identify novel sources of gluten-digesting microbial enzymes from the upper gastro-intestinal tract with the potential to neutralize gluten epitopes. Methodology/Principal Findings Oral microorganisms with gluten-degrading capacity were obtained by a selective plating strategy using gluten agar. Microbial speciations were carried out by 16S rDNA gene sequencing. Enzyme activities wer…

ProteomicsApplied Microbiologylcsh:MedicineBiochemistryGliadinEpitopeSubstrate SpecificityUpper Gastrointestinal Tractlcsh:ScienceBifidobacterium2. Zero hungerchemistry.chemical_classification0303 health sciencesAniline CompoundsMultidisciplinarymedicine.diagnostic_testbiologyHydrolysisProteolytic enzymesfood and beveragesHydrogen-Ion ConcentrationEnzymes3. Good healthSolutionsBiochemistryMedical MicrobiologyMedicineSmall IntestineResearch ArticleProteasesGlutensProteolysisMolecular Sequence DataDental PlaqueGastroenterology and HepatologyMicrobiologydigestive systemMicrobiology03 medical and health sciencesAntigenmedicineHumansAmino Acid SequenceSalivaBiology030304 developmental biologyBinding Sites030306 microbiologylcsh:Rnutritional and metabolic diseasesbiology.organism_classificationGlutenPeptide Fragmentsdigestive system diseasesMolecular WeightCeliac DiseasechemistryProteolysisbiology.proteinlcsh:QGliadinMicrococcaceaePLoS ONE
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Bioassays to monitor taspase1 function for the identification of pharmacogenetic inhibitors

2011

Background Threonine Aspartase 1 (Taspase1) mediates cleavage of the mixed lineage leukemia (MLL) protein and leukemia provoking MLL-fusions. In contrast to other proteases, the understanding of Taspase1's (patho)biological relevance and function is limited, since neither small molecule inhibitors nor cell based functional assays for Taspase1 are currently available. Methodology/Findings Efficient cell-based assays to probe Taspase1 function in vivo are presented here. These are composed of glutathione S-transferase, autofluorescent protein variants, Taspase1 cleavage sites and rational combinations of nuclear import and export signals. The biosensors localize predominantly to the cytoplasm…

ProteomicsCytoplasmHydrolasesmedicine.medical_treatmentThreonine Aspartase 1Drug Evaluation Preclinicallcsh:MedicineBiosensing TechniquesBiochemistryMiceMolecular Cell BiologyBasic Cancer Researchlcsh:ScienceMultidisciplinaryEnzyme ClassesProteomic Databases3T3 CellsSmall moleculeCellular StructuresEnzymesBiochemistryOncologyMedicineBiological AssayBiologieResearch ArticleProteasesCell SurvivalIn silicoBiologyCleavage (embryo)In vivoGenetic Mutationddc:570EndopeptidasesChemical BiologyConsensus sequencemedicineGeneticsAnimalsHumansProtease InhibitorsBiologyCell NucleusProteaselcsh:RProteinsPharmacogeneticsSmall MoleculesMutagenesislcsh:Q
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The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
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LC–MS Based Cleavage Site Profiling of the Proteases ADAM10 and ADAM17 Using Proteome-Derived Peptide Libraries

2014

A Disintegrin and Metalloproteinase 10 (ADAM10) and ADAM17 catalyze ectodomain shedding of a number of cell surface proteins important for embryonic development and tissue homeostasis. Changes in the expression levels or dysregulated proteolytic activity of ADAM10 and ADAM17 have been shown to play important roles in multiple diseases such as inflammation, cancer, and neurodegenerative disorders. Despite the well documented substrate repertoire of ADAM10 and ADAM17, little is known about their cleavage site specificity. We optimized Q-PICS (Quantitative Proteomics for the Identification of Cleavage Sites) to elucidate the cleavage site specificity of recombinant murine ADAM10 and ADAM17. Tw…

ProteomicsProteasesProteomeQuantitative proteomicsADAM17 ProteinBiologyCleavage (embryo)BiochemistryMass SpectrometryADAM10 ProteinMicePeptide LibraryAnimalsHumansADAM17 ProteinPeptide libraryTissue homeostasisMembrane ProteinsGeneral ChemistryPeptide FragmentsADAM ProteinsBiochemistryEctodomainProteomeAmyloid Precursor Protein SecretasesChromatography LiquidJournal of Proteome Research
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The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10

2012

The in vivo roles of meprin metalloproteases in pathophysiological conditions remain elusive. Substrates define protease roles. Therefore, to identify natural substrates for human meprin α and β we employed TAILS (terminal amine isotopic labeling of substrates), a proteomics approach that enriches for N-terminal peptides of proteins and cleavage fragments. Of the 151 new extracellular substrates we identified, it was notable that ADAM10 (a disintegrin and metalloprotease domain-containing protein 10)—the constitutive α-secretase—is activated by meprin β through cleavage of the propeptide. To validate this cleavage event, we expressed recombinant proADAM10 and after preincubation with meprin…

Proteomicsalpha-2-HS-Glycoproteinmedicine.medical_treatmentADAM10ADAM10 ProteinMice0302 clinical medicine610 Medicine & healthMice KnockoutExtracellular Matrix Proteins0303 health sciencesMetalloproteinaseDegradomeMetalloendopeptidasesMeprinADAM10Terminal amine isotopic labeling of substratesADAM ProteinsElafinBiochemistryTAILSCytokinesMolecular MedicineElafinResearch Article610 Medicine & healthBiologyCell Line03 medical and health sciencesCellular and Molecular NeurosciencemedicineDisintegrinAnimalsHumansAmino Acid SequenceCystatin CMolecular Biology030304 developmental biologyPharmacologyProteaseMeprin; ADAM10; Metalloproteases; Proteomics; TAILS; DegradomeMembrane ProteinsCell BiologyADAM ProteinsHEK293 CellsMembrane proteinbiology.proteinMetalloproteases570 Life sciences; biologyAmyloid Precursor Protein SecretasesCaco-2 Cells030217 neurology & neurosurgery
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Cardioprotective effects of the serine protease inhibitor aprotinin after regional ischemia and reperfusion on the beating heart.

2002

AbstractObjective: Early coronary reperfusion of the ischemic myocardium is a desired therapeutic goal to preserve myocardium. However, reperfusion itself contributes to an additional myocardial injury (ie, reperfusion injury), which has been attributed to neutrophil infiltration with subsequent release of proteases and oxygen-derived radicals. We studied the effects of the serine protease inhibitor aprotinin (Trasylol) on myocardial ischemia and reperfusion in a rat model. Methods: The effects of aprotinin (5000 and 20,000 U/kg) were examined in vivo in a rat model of regional myocardial ischemia (20 minutes) and long-term reperfusion (24 hours). Cardioprotecive effects were determined by …

Pulmonary and Respiratory MedicineMaleProteasesCardiotonic AgentsSerine Proteinase InhibitorsNeutrophilsHeart VentriclesIschemiaMyocardial IschemiaApoptosisMyocardial ReperfusionMyocardial Reperfusion InjuryPharmacologyRats Sprague-DawleyLeukocyte CountAprotininIn vivoMedicineAnimalsAprotininCreatine KinasePeroxidaseCardioprotectionbiologyDose-Response Relationship Drugbusiness.industryMyocardiumModels Cardiovascularmedicine.diseaseCombined Modality TherapyRatsDisease Models AnimalTreatment OutcomeEnzyme inhibitorAnesthesiabiology.proteinSurgeryCreatine kinaseCardiology and Cardiovascular MedicinebusinessReperfusion injuryBiomarkersmedicine.drugThe Journal of thoracic and cardiovascular surgery
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