Search results for "Protease"

showing 10 items of 463 documents

Identification of Plakortide E from the Caribbean Sponge Plakortis halichondroides as a Trypanocidal Protease Inhibitor using Bioactivity-Guided Frac…

2014

In this paper, we report new protease inhibitory activity of plakortide E towards cathepsins and cathepsin-like parasitic proteases. We further report on its anti-parasitic activity against Trypanosoma brucei with an IC50 value of 5 mu M and without cytotoxic effects against J774.1 macrophages at 100 mu M concentration. Plakortide E was isolated from the sponge Plakortis halichondroides using enzyme assay-guided fractionation and identified by NMR spectroscopy and mass spectrometry. Furthermore, enzyme kinetic studies confirmed plakortide E as a non-competitive, slowly-binding, reversible inhibitor of rhodesain.

ProteasesStereochemistrymedicine.medical_treatmentTrypanosoma brucei bruceiPlakortis halichondroidesPharmaceutical ScienceTrypanosoma brucei01 natural sciences570 Life sciencesDioxanesprotease inhibitor03 medical and health sciencesddc:593Drug DiscoverymedicineAnimalsHumansProtease Inhibitorscathepsinlcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)IC50030304 developmental biologyTrypanocidal agentrhodesainchemistry.chemical_classification0303 health sciencesProteaseAntiparasitic Agentsbiology010405 organic chemistryCommunicationplakortide Ebiology.organism_classificationCathepsinsTrypanocidal AgentsAntiparasitic agentProtease inhibitor (biology)Porifera0104 chemical sciencesCysteine Endopeptidasesslowly-binding reversible inhibitorEnzymelcsh:Biology (General)BiochemistrychemistryDrug Screening Assays Antitumor570 Biowissenschaftenmedicine.drug
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Resistance toBacillus thuringiensis Cry1Ac toxin in three strains ofHeliothis virescens: Proteolytic and SEM study of the larval midgut

1999

In a previous study, we demonstrated that resistance to Bacillus thuringiensis toxins in Heliothis virescens might be related to differences in the composition of the proteolytic extracts from insect midgut. There, we found specific proteolytic bands present in the gut extracts of the resistant strain and absent from the susceptible one. Here we report related facts using a new resistant strain (KCB) and a cross between the two strains used in our previous study. As would be expected, no quantitative differences in total proteolytic activity were found between the strains, although qualitative differences related to the presence or absence of specific proteolytic activity bands using SDS-PA…

ProteasesStrain (chemistry)Heliothis virescensbiologyPhysiologyToxinmedia_common.quotation_subjectfungiMidgutGeneral MedicineInsectmedicine.disease_causebiology.organism_classificationBiochemistryMicrobiologyCry1AcInsect ScienceBacillus thuringiensismedicinemedia_commonArchives of Insect Biochemistry and Physiology
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Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.

2014

Increased expression of metalloprotease meprin β is associated with fibrotic syndromes and Alzheimer's disease (AD). Hence, regulation of meprin activity might be a suitable strategy for the treatment of these conditions. Meprin β is a type 1 transmembrane protein, but can be released from the cell surface by ectodomain shedding. The protease is expressed as an inactive zymogen and requires proteolytic maturation by tryptic serine proteases. In the present study, we demonstrate, for the first time, the differences in the activation of soluble and membrane bound meprin β and suggest transmembrane serine protease 6 [TMPRSS6 or matriptase-2 (MT2)] as a new potent activator, cleaving off the pr…

ProteasesTMPRSS6Swinemedicine.medical_treatmentMolecular Sequence DataBiologyBiochemistryProtein Structure SecondaryAmyloid beta-Protein PrecursorChlorocebus aethiopsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologySerine proteaseProteaseCell MembraneSerine EndopeptidasesMetalloendopeptidasesCell BiologySheddaseTrypsinTransmembrane proteinHEK293 CellsBiochemistryEctodomainCOS Cellsbiology.proteinmedicine.drugThe Biochemical journal
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Controlling the semi-permeability of protein nanocapsules influences the cellular response to macromolecular payloads.

2021

Nanocapsules are an excellent platform for the delivery of macromolecular payloads such as proteins, nucleic acids or polyprodrugs, since they can both protect the sensitive cargo and target its delivery to the desired site of action. However, the release of macromolecules from nanocapsules remains a challenge due to their restricted diffusion through the nanoshell compared to small molecule cargo. Here, we designed degradable protein nanocapsules with varying crosslinking densities of the nanoshell to control the release of model macromolecules. While the crosslinking did not influence the degradability of the capsules by natural proteases, it significantly affected the release profiles. F…

ProteasesVaccinesChemistryMacromolecular SubstancesBiomedical EngineeringProteinsGeneral ChemistryGeneral MedicineSmall moleculeNanocapsulesNanoshellPermeabilityFluorescamineDrug LiberationDrug Delivery SystemsNanocapsulesPermeability (electromagnetism)Restricted DiffusionBiophysicsGeneral Materials ScienceEndopeptidase KSite of actionMacromoleculeJournal of materials chemistry. B
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Specific processing of tenascin-C by the metalloprotease meprinβ neutralizes its inhibition of cell spreading

2009

The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-terminal pep…

Proteasesanimal structuresColonRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataTenascinCleavage (embryo)Cell LineCrohn DiseaseCell AdhesionAnimalsHumansProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologyAlternative splicingTenascin CMetalloendopeptidasesTenascinMolecular biologyPeptide FragmentsExtracellular MatrixFibronectinsFibronectinAlternative SplicingProtein Subunitsembryonic structuresbiology.proteinProtein MultimerizationChickensMatrix Biology
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Analysis of serine proteases from marine sponges by 2-D zymography.

2007

Proteolytic activities isolated from the marine demosponges Geodia cydonium and Suberites domuncula were analyzed by 2-D zymography, a technique that combines IEF and zymography. After purification, a 200 kDa proteolytically active protein band was obtained from G. cydonium when analyzed in gelatin copolymerized 1-D zymograms. The enzymatic activity was quantified using alpha-N-benzoyl-D-arginine p-nitroanilide (BAPNA) as a substrate and corresponded to a serine protease. The protease activity was resistant to urea and SDS. DTT and 2-mercaptoethanol (2-ME) did not significantly change the protease activity, but induced a shift in molecular mass of the proteolytic band to lower M(r) values a…

Proteasesmedicine.medical_treatmentClinical BiochemistryBiologyBenzoylarginine NitroanilideBiochemistryAnalytical ChemistrySubstrate SpecificitySerinemedicineAnimalsUreaZymographyElectrophoresis Gel Two-DimensionalMercaptoethanolSerine proteasechemistry.chemical_classificationProteaseMolecular massSerine EndopeptidasesSodium Dodecyl Sulfatebiology.organism_classificationMolecular biologyPoriferaSuberites domunculaEnzyme ActivationMolecular WeightDithiothreitolEnzymeBiochemistrychemistrybiology.proteinElectrophoresis
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Potent Inhibitor of Human Trypsins from the Aeruginosin Family of Natural Products

2021

Funding Information: We would like to thank A. Löfhjelm and L. Saari for excellent technical assistance. This work was supported by a Sigrid Jusélius Foundation grant to H.K. and the Academy of Finland funding (321809) to T.S. We would also like to thank the Erkko Foundation and Nordforsk Nordic center of Excellency NordAqua (project number #82845) and University of Helsinki’s Doctoral Programme in Microbiology and Biotechnology funding to M.N.A. D.O.A. was supported by a postdoctoral research fellowship from the São Paulo Research Foundation (FAPESP #2018/01563-2). We thank Biocenter Kuopio for the use of their facilities for molecular modeling and MD simulations. We thank the DNA Sequenci…

Proteasesserine proteases116 Chemical sciencesproteaasiluonnontuotteet01 natural sciencesBiochemistryGenomeproteomiikkaSerine03 medical and health sciencesCell Line TumorGene clusterinhibitorsHumansIC50Genetrypsiinit030304 developmental biologyCell ProliferationinhibiittoritSerine protease0303 health sciencesBiological Productsbiologybiokemia010405 organic chemistryCell growthChemistrybioinformatiikkaGeneral MedicineArticlesseriiniproteaasi0104 chemical sciences3. Good healthsyöpäsolutBiochemistryGenes Bacterialbiology.proteinMolecular MedicineproteasessyöpätauditproteiinitTrypsin InhibitorsAzabicyclo CompoundsNodulariaAeruginosins
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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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Relative contribution of different l-arginine sources to the substrate supply of endothelial nitric oxide synthase

2011

In certain cases of endothelial dysfunction l-arginine becomes rate-limiting for NO synthesis in spite of sufficiently high plasma concentrations of the amino acid. To better understand this phenomenon, we investigated routes of substrate supply to endothelial nitric oxide synthase (eNOS). Our previous data with human umbilical vein (HUVEC) and EA.hy.926 endothelial cells demonstrated that eNOS can obtain its substrate from the conversion of l-citrulline to l-arginine and from protein breakdown. In the present study, we determined the quantitative contribution of proteasomal and lysosomal protein degradation and investigated to what extent extracellular peptides and l-citrulline can provide…

Proteasome Endopeptidase ComplexNitric Oxide Synthase Type IIIArginineEndotheliumLeupeptinsPeptideArginineNitric OxideUmbilical veinCell LineGenes ReporterEnosLysosomeHuman Umbilical Vein Endothelial CellsmedicineExtracellularHumansHistidineProtease InhibitorsMolecular BiologyChromatography High Pressure LiquidHistidinechemistry.chemical_classificationbiologyMembrane Transport ProteinsBiological TransportChloroquineDipeptidesAtherosclerosisbiology.organism_classificationmedicine.anatomical_structureBiochemistrychemistryProteolysisCitrullineEndothelium VascularLysosomesCardiology and Cardiovascular MedicineOligopeptidesJournal of Molecular and Cellular Cardiology
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SUMOylation of Blimp-1 promotes its proteasomal degradation

2011

Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its …

Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1IntracellularFEBS Letters
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