Search results for "DASES"

showing 10 items of 485 documents

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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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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Cryo-negative staining

1998

Abstract A procedure is presented for the preparation of thin layers of vitrified biological suspensions in the presence of ammonium molybdate, which we termcryo-negative staining. The direct blotting of sample plus stain solution on holey carbon supports produces thin aqueous films across the holes, which are routinely thiner than the aqueous film produced by conventional negative staining on a continuous carbon layer. Because of this, a higher than usual concentration of negative stain (ca. 16% rather than 2%) is required for cryo-negative staining in order to produce an optimal image contrast. The maintenance of the hydrated state, the absence of adsorption to a carbon film and associate…

Proteasome Endopeptidase ComplexAnalytical chemistryGeneral Physics and AstronomyNegative Staininglaw.inventionMultienzyme ComplexesStructural BiologylawImage Processing Computer-AssistedTobacco mosaic virusAnimalsGeneral Materials ScienceColoring AgentsMolybdenumAmmonium molybdateTurnip yellow mosaic virusbiologyChemistryChaperonin 60Cell BiologyCatalasebiology.organism_classificationNegative stainStainingCysteine EndopeptidasesMicroscopy ElectronCrystallographyFreeze DryingElectron diffractionHemocyaninsVirusesCattleElectron microscopeTomato bushy stunt virusMicron
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Analysis of the MHC Class I Antigen Presentation Machinery in Human Embryonal Carcinomas: Evidence for Deficiencies in TAP, LMP and MHC Class I Expre…

1998

The expression of the major histocompatibility complex (MHC) class I antigens is suppressed in early post-implantation embryonic cells as well as in embryonal carcinoma (EC) cells, but could be upregulated by treatment with interferon (IFN)-gamma or retinoic acid. In a number of human and murine tumours, defects in the expression of the different components of the MHC class I antigen processing machinery, such as the proteasomal subunits LMP-2 and LMP-7 and the peptide transporters TAP-1 and TAP-2, account for impaired MHC class I surface expression. Here, we analysed the constitutive and IFN-gamma regulated mRNA and protein expression of the LMP, TAP and MHC class I molecules in the human …

Proteasome Endopeptidase ComplexCD74HIV AntigensImmunologyCD1CytomegalovirusInterferon-gammaATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesCarcinoma EmbryonalMHC class ITumor Cells CulturedHumansATP Binding Cassette Transporter Subfamily B Member 2Antigens ViralAntigen PresentationbiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class ITemperatureGeneral MedicineTransporter associated with antigen processingMHC restrictionMolecular biologyUp-RegulationCysteine EndopeptidasesProtein Biosynthesisbiology.proteinATP-Binding Cassette TransportersPeptidesCD8Scandinavian Journal of Immunology
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Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation

2001

Dendritic cells (DC) are professional antigen-presenting cells (APC) which proceed from immature to a mature stage during their final differentiation. Immature DC are highly effective in terms of antigen uptake and processing, whereas mature DC become potent immunostimulatory cells. Until now, the expression profiles of the major components of the MHC class I antigen-processing machinery (APM) during DC development have not been well characterized. In this study, the mRNA and protein expression levels of the IFN-gamma inducible proteasome subunits, of the proteasome activators PA28, and of key components required for peptide transport and MHC class I-peptide complex assembly have been evalu…

Proteasome Endopeptidase ComplexCD74ImmunologyAntigen presentationLipopolysaccharide ReceptorsDown-RegulationImmunoglobulinsMuscle ProteinsAntiportersMonocytesMultienzyme ComplexesMHC class IHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationMHC class IIbiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class IMembrane Transport ProteinsProteinsCell DifferentiationDendritic CellsGeneral MedicineTransporter associated with antigen processingMHC restrictionMolecular biologyUp-RegulationCell biologyCysteine EndopeptidasesProtein TransportProtein Biosynthesisbiology.proteinATP-Binding Cassette TransportersPeptidesInternational Immunology
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Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1

2001

Glucocorticoids inhibit the proinflammatory activities of transcription factors such as AP-1 and NF-kappa B as well as that of diverse cellular signaling molecules. One of these signaling molecules is the extracellular signal-regulated kinase (Erk-1/2) that controls the release of allergic mediators and the induction of proinflammatory cytokine gene expression in mast cells. The mechanism of inhibition of Erk-1/2 activity by glucocorticoids is unknown. Here we report a novel dual action of glucocorticoids for this inhibition. Glucocorticoids increase the expression of the MAP kinase phosphatase-1 (MKP-1) gene at the promoter level, and attenuate proteasomal degradation of MKP-1, which we re…

Proteasome Endopeptidase ComplexCell signalingMitogen-Activated Protein Kinase 3Cell Cycle ProteinsBiologyDexamethasoneGene Expression Regulation EnzymologicArticleGeneral Biochemistry Genetics and Molecular BiologyCell LineImmediate-Early ProteinsProinflammatory cytokineMiceGlucocorticoid receptorMultienzyme ComplexesProtein Phosphatase 1Phosphoprotein PhosphatasesAnimalsEnzyme InhibitorsPhosphorylationMolecular BiologyTranscription factorDNA PrimersMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3Base SequenceGeneral Immunology and MicrobiologyKinaseHydrolysisGeneral NeuroscienceDual Specificity Phosphatase 1Cell biologyMice Inbred C57BLCysteine EndopeptidasesMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesThe EMBO Journal
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Cloning of Sponge (Geodia cydonium) and Tunicate (Botryllus schlosseri) Proteasome Subunit Epsilon (PRCE): Implications about the Vertebrate MHC-Enco…

1996

Proteasomes are large protein complexes that play a major role in selective degradation of intracellular proteins. Eukaryotes feature seven different alpha and beta subunits. Two of the vertebrate housekeeping beta-subunits have MHC-encoded homologues that can substitute for the housekeeping counterparts upon interferon-gamma induction. In the present study we report the cloning of invertebrate beta-subunit proteasome epsilon (PRCE), from the marine sponge Geodia cydonium and from the colonial tunicate Botryllus schlosseri. Sequence comparisons revealed that the sponge and tunicate proteins are strikingly similar to vertebrate and yeast PRCEs and their MHC-linked counterparts the PRCCs (als…

Proteasome Endopeptidase ComplexDNA ComplementaryProtein subunitMolecular Sequence DataBiophysicsSaccharomyces cerevisiaeBotryllus schlosseriPolymerase Chain ReactionBiochemistryMiceMultienzyme ComplexesConsensus SequenceBotanyAnimalsHumansAmino Acid SequenceUrochordataCloning MolecularProtein precursorMolecular BiologyPhylogenyDNA Primerschemistry.chemical_classificationCloningBase SequenceSequence Homology Amino AcidbiologyProteinsCell Biologybiology.organism_classificationYeastPoriferaRatsAmino acidTunicateCell biologyCysteine EndopeptidaseschemistryProteasomeVertebratesChickensBiochemical and Biophysical Research Communications
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Functional deficiencies of components of the MHC class I antigen pathway in human tumors of epithelial origin

2000

An association between oncogenic transformation and repression of different components of the MHC class I antigen processing machinery (APM) have been described in murine model systems. In order to discover whether a similar correlation exists, human tumor cell lines of distinct histology with altered ras protein were analyzed for the expression of APM components utilizing RT-PCR and Western blot analyses. A heterogeneous expression pattern of MHC class I antigens, TAP peptide transporter, proteasome subunits, proteasome activator PA28 and the chaperones calnexin, calreticulin as well as tapasin was displayed by these tumor cell lines. Single or combined deficiencies in the expression and/o…

Proteasome Endopeptidase ComplexGene ExpressionInterferon-gammaMiceTapasinATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesCalnexinGene expressionMHC class ITumor Cells CulturedAnimalsHumansNeoplasms Glandular and EpithelialATP Binding Cassette Transporter Subfamily B Member 2DNA PrimersAntigen PresentationTransplantationBase SequencebiologyAntigen processingMHC class I antigenHistocompatibility Antigens Class IProteinsHematologyTransporter associated with antigen processingRecombinant ProteinsCell biologyCysteine EndopeptidasesGenes rasMutationCancer researchbiology.proteinATP-Binding Cassette TransportersCalreticulinBone Marrow Transplantation
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Characterizing the N-terminal processing motif of MHC class I ligands.

2008

Abstract Most peptide ligands presented by MHC class I molecules are the product of an intracellular pathway comprising protein breakdown in the cytosol, transport into the endoplasmic reticulum, and successive N-terminal trimming events. The efficiency of each of these processes depends on the amino acid sequence of the presented ligand and its precursors. Thus, relating the amino acid composition N-terminal of presented ligands to the sequence specificity of processes in the pathway gives insight into the usage of ligand precursors in vivo. Examining the amino acid composition upstream the true N terminus of MHC class I ligands, we demonstrate the existence of a distinct N-terminal proces…

Proteasome Endopeptidase ComplexImmunologyAmino Acid MotifsEndoplasmic ReticulumLigandsAminopeptidaseAminopeptidasesCell LineMiceCytosolCell Line TumorMHC class IImmunology and AllergyAnimalsHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Peptide sequenceAntigen PresentationbiologyLigandEndoplasmic reticulumHistocompatibility Antigens Class ITransporter associated with antigen processingPeptide FragmentsN-terminusBiochemistryProteasomebiology.proteinATP-Binding Cassette TransportersPeptidesHeLa CellsProtein BindingJournal of immunology (Baltimore, Md. : 1950)
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Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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