Search results for "Endopeptidases"

showing 10 items of 285 documents

Mast cells promote homeostasis by limiting endothelin-1-induced toxicity

2004

Endothelin-1 (ET-1) is a 21-amino-acid peptide, derived from vascular endothelial cells, with potent vasoconstrictor activity. ET-1 has been implicated in diverse physiological or pathological processes, including the vascular changes associated with sepsis. However, the factors that regulate ET-1-associated toxicity during bacterial infections, or in other settings, are not fully understood. Both the pathology associated with certain allergic and autoimmune disorders, and optimal host defence against bacterial and parasitic infections are mediated by mast cells. In vitro, mast cells can produce ET-1 (ref. 11), undergo ET-1-dependent and endothelin-A receptor (ET(A))-dependent activation, a…

DiarrheaProteasesDrug-Related Side Effects and Adverse ReactionsCell SurvivalPeritonitisBiologyPeptides CyclicCell DegranulationBody TemperatureMiceChymasesIn vivomedicineAnimalsHomeostasisMast CellsReceptorEgtazic AcidMice KnockoutMultidisciplinaryEndothelin-1Stem CellsBody WeightSerine EndopeptidasesEndogenous mediatorMast cellEndothelin 1In vitroCell biologyMice Inbred C57BLSurvival RateProto-Oncogene Proteins c-kitmedicine.anatomical_structureMutationImmunologyFemaleOligopeptidesInjections IntraperitonealHomeostasisNature
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Mode of action of Bacillus thuringiensis PS86Q3 strain in hymenopteran forest pests

2001

The mode of action of Cry toxins has been described principally in lepidopteran insects as a multistep process. In this work we describe the mode of action of a Cry toxin active in the common pine sawfly Diprion pini (Hymenoptera, Diprionidae), considered a major forest pest in Europe. Strain PS86Q3 contains a long bipyramidal crystal composed of five major proteins. The N-terminal sequence shows that the 155 kDa protein corresponds to Cry5B toxin and the other proteins belong to the Cry5A subgroup. PCR analysis indicates the presence of cry5Ac and cry5Ba genes, suggesting that Cry5A protein should be Cry5Ac. Activation of protoxins with trypsin or with midgut content from D. pini and Cepha…

DiprionidaeBacterial ToxinsBacillus thuringiensisBiotinmedicine.disease_causeBiochemistryMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsMode of actionMolecular BiologyBacillus thuringiensis ToxinsbiologyToxinfungiMidgutTrypsinbiology.organism_classificationHymenopteraEndotoxinsEnzyme ActivationSawflyLarvaInsect ScienceDiprion pinimedicine.drugInsect Biochemistry and Molecular Biology
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A peptide inhibiting the collagen binding function of integrin alpha2I domain.

1999

Integrin alpha2 subunit forms in the complex with the beta1 subunit a cell surface receptor binding extracellular matrix molecules, such as collagens and laminin-1. It is a receptor for echovirus-1, as well. Ligands are recognized by the special "inserted" domain (I domain) in the integrin alpha2 subunit. Venom from a pit viper, Bothrops jararaca, has been shown to inhibit the interaction of platelet alpha2beta1 integrin with collagen because of the action of a disintegrin/metalloproteinase named jararhagin. The finding that crude B. jararaca venom could prevent the binding of human recombinant ralpha2I domain to type I collagen led us to study jararhagin further. Synthetic peptides represe…

EGF-like domainIntegrinIntegrin alpha2PeptideBiologyBiochemistryPeptides CyclicEuropiumAntigens CDCrotalid VenomsDisintegrinHumansAmino Acid SequenceMolecular BiologyRGD motifDNA Primerschemistry.chemical_classificationBase SequenceCell MembraneMetalloendopeptidasesCell BiologyCyclic peptideRecombinant ProteinsBiochemistrychemistryJararhaginbiology.proteinCollagenBinding domainThe Journal of biological chemistry
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Antibodies to proteinase 3 increase adhesion of neutrophils to human endothelial cells

1993

SUMMARY The detection of anti-neutrophil cytoplasmic antibodies (ANCA), especially those with specificity for proteinase 3, is important in the diagnosis and in monitoring disease activity of Wegener's granulomatosis and related vasculitides. An ubiquitous feature of all ANCA-associated acute vascular injury is lytic necrosis. Adhesion of neutrophils to endothelium is a fundamental early step of the inflammatory response. Recently we were able to show that ANCA recognize their target antigen (proteinase 3) translocated into the membrane of human endothelial cells. The aim of this study was to investigate the effect of ANCA on the adhesion of neutrophils to human endothelial cells. Incubatio…

EndotheliumNeutrophilsMyeloblastinImmunologyFluorescent Antibody TechniqueEnzyme-Linked Immunosorbent AssayAntibodies Antineutrophil CytoplasmicAutoimmune DiseasesFlow cytometryProteinase 3E-selectinCell AdhesionmedicineHumansImmunology and AllergyCell adhesionCells CulturedAutoantibodiesMixed Connective Tissue Diseasebiologymedicine.diagnostic_testSerine EndopeptidasesGranulomatosis with PolyangiitisAdhesionFlow CytometryEndothelial stem cellmedicine.anatomical_structureImmunoglobulin GImmunologybiology.proteinEndothelium VascularAntibodyE-SelectinCell Adhesion MoleculesResearch ArticleClinical and Experimental Immunology
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Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production

2004

Increased Abeta42 production has been linked to the development of Alzheimer disease. We now identify a number of compounds that raise Abeta42. Among the more potent Abeta42-raising agents identified are fenofibrate, an antilipidemic agent, and celecoxib, a COX-2-selective NSAID. Many COX-2-selective NSAIDs tested raised Abeta42, including multiple COX-2-selective derivatives of two Abeta42-lowering NSAIDs. Compounds devoid of COX activity and the endogenous isoprenoids FPP and GGPP also raised Abeta42. These compounds seem to target the gamma-secretase complex, increasing gamma-secretase-catalyzed production of Abeta42 in vitro. Short-term in vivo studies show that two Abeta42-raising comp…

Enzyme-Linked Immunosorbent AssayEndogenyProtein Serine-Threonine KinasesPharmacologyTransfectionMass SpectrometryGeneral Biochemistry Genetics and Molecular BiologyPresenilinCell LineFenofibrateAlzheimer DiseaseIn vivoEndopeptidasesmedicineAspartic Acid EndopeptidasesHumansImmunoprecipitationCyclooxygenase InhibitorsProtein precursorHypolipidemic AgentsSulfonamidesrho-Associated KinasesAmyloid beta-PeptidesFenofibratebusiness.industryAnti-Inflammatory Agents Non-SteroidalIntracellular Signaling Peptides and ProteinsBrainGeneral Medicinemedicine.diseaseIn vitroEnzyme ActivationBiochemistryCelecoxibPyrazolesFemaleAmyloid Precursor Protein SecretasesAlzheimer's diseaserhoA GTP-Binding ProteinbusinessAntilipidemic Agentmedicine.drugNature Medicine
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Photobacterium damselae subsp. damselae Major Virulence Factors Dly, Plasmid-Encoded HlyA, and Chromosome-Encoded HlyA Are Secreted via the Type II S…

2015

ABSTRACT Photobacterium damselae subsp. damselae is a marine bacterium that causes septicemia in marine animals and in humans. Previously, we had determined a major role of pPHDD1 plasmid-encoded Dly (damselysin) and HlyA (HlyA pl ) and the chromosome-encoded HlyA (HlyA ch ) hemolysins in virulence. However, the mechanisms by which these toxins are secreted remain unknown. In this study, we found that a mini-Tn 10 transposon mutant in a plasmidless strain showing an impaired hemolytic phenotype contained an insertion in epsL , a component of a type II secretion system (T2SS). Reconstruction of the mutant by allelic exchange confirmed the specific involvement of epsL in HlyA ch secretion. In…

ErythrocytesTranscription GeneticVirulence FactorsImmunologyMutantVirulenceTransposasesBiologyGene MutantHemolysin ProteinsMicrobiologyHemolysisMicrobiologyHemolysin ProteinsMiceBacterial ProteinsEndopeptidasesAnimalsSecretionBacterial Secretion SystemsMice Inbred BALB CType II secretion systemBase SequencePhotobacteriumHemolysinBacterial InfectionsSequence Analysis DNAInfectious DiseasesPhotobacterium damselaeMutationParasitologyPlasmids
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Mass spectral identification of the blocked N-terminal tryptic peptide of the ATPase inhibitor from beef heart mitochondria

1984

AbstractThe presence of a formyl blocking group at the N-terminus of the ATPase inhibitor has been identified and the partial sequence of the N-terminal peptide has been determined by fast atom bombardment and field desorption coupled to mass spectrometry. Minor discrepancies in amino acid sequence of the inhibitor between the present and published data [(1981) Proc. Natl. Acad. Sci. USA 78, 7403-7407] are reported and its relationships with other inhbitors are briefly discussed.

Fast atom bombardmentATPaseBiophysicsPeptideN-formyi blocking groupSaccharomyces cerevisiaeMass spectrometryBiochemistryMass SpectrometryMitochondria HeartSpecies SpecificityStructural BiologyEndopeptidasesGeneticsAnimalsTrypsinAmino Acid SequenceMolecular BiologyPeptide sequencechemistry.chemical_classificationBeef heart mitochondriabiologyChemistryTryptic peptideProteinsCell BiologyFast atom bombardmentField desorption Amino acid sequenceATPase inhibitorPeptide FragmentsMitochondriaProton-Translocating ATPasesBiochemistrybiology.proteinCattleFEBS Letters
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Apoptosis induced in hepatoblastoma HepG2 cells by the proteasome inhibitor MG132 is associated with hydrogen peroxide production, expression of Bcl-…

2002

This report is focused on the apoptotic effect induced by MG132, an inhibitor of 26S proteasome, in human hepatoma HepG2 cells. The results were compared with those obtained with non-transformed human Chang liver cells. MG132 reduced the viability of HepG2 cells in a time- and dose-dependent manner. The effect was in tight connection with the induction of apoptosis, as indicated by fluorescence microscopy and cytometric analysis, and was accompanied by a remarkable increase in the production of H2O2 and a reduction in mitochondrial transmembrane potential (Deltapsim). In addition cell death was prevented by antioxidants such as GSH, N-acetylcysteine or catalase. Western blot analysis showed…

G2 PhaseHepatoblastomaCancer ResearchProgrammed cell deathProteasome Endopeptidase ComplexMG132Time FactorsCell SurvivalLeupeptinsPoly ADP ribose polymeraseBlotting Westernbcl-X ProteinMitosisCaspase 3Antineoplastic AgentsApoptosismacromolecular substancesMembrane Potentialschemistry.chemical_compoundCytosolMultienzyme ComplexesMG132medicineTumor Cells CulturedHumansCaspasebiologyCaspase 3Cytochrome cCell CycleLiver NeoplasmsHydrogen PeroxideFlow CytometryMolecular biologyMitochondriaEnzyme ActivationCysteine EndopeptidasesOxidative StressOncologyBiochemistrychemistryProto-Oncogene Proteins c-bcl-2ApoptosisCaspasesbiology.proteinProteasome inhibitormedicine.drug
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Urokinase Plasminogen Activator and Gelatinases Are Associated with Membrane Vesicles Shed by Human HT1080 Fibrosarcoma Cells

1997

Membrane vesicles are shed by tumor cells both in vivo and in vitro. Although their functions are not well understood, it has been proposed that they may play multiple roles in tumor progression. We characterized membrane vesicles from human HT1080 fibrosarcoma cell cultures for the presence of proteinases involved in tumor invasion. By gelatin zymography and Western blotting, these vesicles showed major bands corresponding to the zymogen and active forms of gelatinase B (MMP-9) and gelatinase A (MMP-2) and to the MMP-9. tissue inhibitor of metalloproteinase 1 complex. Both gelatinases appeared to be associated with the vesicle membrane. HT1080 cell vesicles also showed a strong, plasminoge…

GelatinasesMacromolecular SubstancesFibrosarcomaBlotting WesternCellGelatinase ABiologyBiochemistryTumor Cells CulturedmedicineHumansCollagenasesFibrinolysinMolecular BiologyGlycoproteinsUrokinaseEnzyme PrecursorsVesicleMetalloendopeptidasesTissue Inhibitor of MetalloproteinasesCell BiologyTissue inhibitor of metalloproteinaseUrokinase-Type Plasminogen ActivatorMolecular biologyExtracellular MatrixUrokinase receptorBloodmedicine.anatomical_structureMatrix Metalloproteinase 9GelatinasesMatrix Metalloproteinase 2HT1080medicine.drugJournal of Biological Chemistry
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Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage

2015

The SOS response in Eubacteria is a global response to DNA damage and its activation is increasingly associated with the movement of mobile genetic elements. The temperate phage GIL01 is induced into lytic growth using the host's SOS response to genomic stress. LexA, the SOS transcription factor, represses bacteriophage transcription by binding to a set of SOS boxes in the lysogenic promoter P1. However, LexA is unable to efficiently repress GIL01 transcription unless the small phage-encoded protein gp7 is also present. We found that gp7 forms a stable complex with LexA that enhances LexA binding to phage and cellular SOS sites and interferes with RecA-mediated auto-cleavage of LexA, the ke…

Gene Expression Regulation ViralSOS responsebacteriophagesTranscription GeneticvirusesRepressorBacillus PhagesBiologybakteriofagitBacteriophage03 medical and health sciencesSOS Response (Genetics)Viral ProteinsBacterial ProteinsLysogenic cycleGeneticsSOS responsePromoter Regions GeneticSOS Response GeneticsTranscription factor030304 developmental biologyGenetics0303 health sciences030306 microbiologyLexA repressorGene regulation Chromatin and EpigeneticsSerine Endopeptidasesta1182DNAbiochemical phenomena metabolism and nutritionbiology.organism_classification3. Good healthCell biologyRepressor Proteinsenzymes and coenzymes (carbohydrates)Rec A RecombinasesLytic cyclebacteriaRepressor lexAProtein BindingNucleic Acids Research
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