Search results for "Endopeptidase"

showing 10 items of 361 documents

Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins.

2001

The L1 adhesion molecule plays an important role in axon guidance and cell migration in the nervous system. L1 is also expressed by many human carcinomas. In addition to cell surface expression, the L1 ectodomain can be released by a metalloproteinase, but the biological function of this process is unknown. Here we demonstrate that membrane-proximal cleavage of L1 can be detected in tumors and in the developing mouse brain. The shedding of L1 involved a disintegrin and metalloproteinase (ADAM)10, as transfection with dominant-negative ADAM10 completely abolishes L1 release. L1-transfected CHO cells (L1-CHO) showed enhanced haptotactic migration on fibronectin and laminin, which was blocked …

CytoplasmIntegrinsL1; shedding; ADAM10; cell migration; integrinsADAM10IntegrinGene ExpressionCHO CellsBiologyArticle03 medical and health sciencesParacrine signallingMice0302 clinical medicineCell MovementCricetinaeEndopeptidasesTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansReceptors VitronectinFibrinolysinNeural Cell Adhesion Molecules030304 developmental biology0303 health sciencesBinding SitesMembrane GlycoproteinsCell adhesion moleculeCell MembraneAntibodies MonoclonalBrainCell migrationBiological TransportCell BiologyMolecular biologyPeptide FragmentsCell biologyFibronectinAutocrine CommunicationEctodomainSolubility030220 oncology & carcinogenesisbiology.proteinNeural cell adhesion moleculeAmyloid Precursor Protein SecretasesLeukocyte L1 Antigen ComplexOligopeptidesThe Journal of cell biology
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Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein

2005

Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved in APP endocytosis. Here, we show that the APP homolog APLP1 (amyloid precursor-like protein 1) influences APP shedding. In human embryonic kidney 293 cells expression of APLP1 strongly activated APP shedding by alpha-secretase and slightly reduced beta-secretase cleavage. As revealed by domain deletion analysis, the increase in APP shedding re…

CytoplasmTime FactorsRecombinant Fusion ProteinsAmino Acid MotifsBlotting WesternGenetic VectorsEndocytic cycleCHO CellsTransfectionEndocytosisBiochemistryCell LineAmyloid beta-Protein PrecursorGenes ReporterCricetinaeChlorocebus aethiopsEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansImmunoprecipitationAPLP1Molecular BiologyModels GeneticbiologyChemistryHEK 293 cellsP3 peptideCell BiologyEndocytosisProtein Structure TertiaryMicroscopy FluorescenceBiochemistryAlpha secretaseEctodomainCOS Cellsbiology.proteinAmyloid Precursor Protein SecretasesPeptidesGene DeletionPlasmidsJournal of Biological Chemistry
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Cytotoxic effects of antibodies to proteinase 3 (C-ANCA) on human endothelial cells.

1994

SUMMARY Autoantibodies directed against cytoplasmic antigens of neutrophils (ANCA), especially those with specificity for proteinase 3 (PR-3) and myeloperoxidase, are valuable markers for differential diagnosis and monitoring of disease activity in Wegener's granulomatosis (WG) and other vasculitides. Till now, several concepts concerning a direct role of antibodies against PR-3 in the pathogenesis of WG have been discussed. Recently we were able to show that these antibodies recognize PR-3 translocated into the membrane of human endothelial cells. The aim of this study was to investigate putative cytotoxic effects of antibodies to PR-3 on human endothelial cells. Antibodies were obtained b…

Cytotoxicity ImmunologicC-ANCAEndotheliumMyeloblastinImmunologyAutoantigensChromatography AffinityAntibodies Antineutrophil CytoplasmicAntigenProteinase 3medicineImmunology and AllergyCytotoxic T cellHumansLupus Erythematosus SystemicCells CulturedAutoantibodiesMixed Connective Tissue DiseasebiologySerine EndopeptidasesAntibody-Dependent Cell CytotoxicityGranulomatosis with PolyangiitisEndothelial stem cellmedicine.anatomical_structureSjogren's SyndromeMyeloperoxidaseImmunologybiology.proteinEndothelium VascularAntibodyResearch ArticleClinical and experimental immunology
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An Ovalbumin Peptide-Specific Cytotoxic T Cell Clone with Antigen Self-Presentation Capacity Uses Two Distinct Mechanisms to Kill Target Cells

1993

Abstract Cloned 10BK.1 T cells with specificity for the ovalbumin peptide OVA257-264 are representative of a novel cell type within the CD8 + subset of T cells. In the presence and in the absence of added antigen presenting cells these T cells react toward antigen (Ag) by proliferation and lymphokine production. These data suggest self-presentation of the Ag by 10BK.1 cells. Here we present evidence that 10BK.1 cells exhibit cytotoxic activity that involves two different cytotoxic effector mechanisms. (i) One mechanism is fast killing activity, apparent within 4 hr. Constitutive mouse T cell-specific proteinase-1 (MTSP-1) activity, constitutive expression of MTSP-1 RNA, increased by Ag chal…

Cytotoxicity ImmunologicPore Forming Cytotoxic ProteinsOvalbuminImmunologyAntigen presentationAntigen-Presenting CellsBiologyCytoplasmic GranulesLymphocyte ActivationGranzymesCell LineMiceInterleukin 21AntigenAnimalsCytotoxic T cellIL-2 receptorAntigen-presenting cellLymphotoxin-alphaMembrane GlycoproteinsCD40PerforinTumor Necrosis Factor-alphaSerine EndopeptidasesDegranulationMolecular biologyClone Cellsbiology.proteinInterleukin-2T-Lymphocytes CytotoxicCellular Immunology
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity

2005

The cellular prion protein (PrP(c)) is physiologically cleaved in the middle of its 106-126 amino acid neurotoxic region at the 110/111 downward arrow112 peptidyl bond, yielding an N-terminal fragment referred to as N1. We recently demonstrated that two disintegrins, namely ADAM10 and ADAM17 (TACE, tumor necrosis factor alpha converting enzyme) participated in both constitutive and protein kinase C-regulated generation of N1, respectively. These proteolytic events were strikingly reminiscent of those involved in the so-called "alpha-secretase pathway" that leads to the production of secreted sAPPalpha from betaAPP. We show here, by transient and stable transfection analyses, that ADAM9 also…

DNA ComplementaryADAM10Gene ExpressionTransfectionBiochemistryDNA AntisenseCell LineAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansPrPC Proteins[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein kinase AMolecular Biology030304 developmental biologyMice Knockout0303 health sciencesbiologyHEK 293 cells030302 biochemistry & molecular biologyMembrane ProteinsTransfectionCell BiologyFibroblastsPeptide FragmentsADAM ProteinsBiochemistryCell culturebiology.proteinAdditions and CorrectionsAmyloid Precursor Protein SecretasesADAM9Amyloid precursor protein secretase030217 neurology & neurosurgery
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Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulat…

2003

Tumor necrosis factor-alpha converting enzyme (TACE or ADAM17) is a member of the ADAM (a disintegrin and metalloproteinase) family of type I membrane proteins and mediates the ectodomain shedding of various membrane-anchored signaling and adhesion proteins. TACE is synthesized as an inactive zymogen, which is subsequently proteolytically processed to the catalytically active form. We have identified the proprotein-convertases PC7 and furin to be involved in maturation of TACE. This maturation is negatively influenced by the phorbol ester phorbol-12-myristate-13-acetate (PMA), which decreases the cellular amount of the mature form of TACE in PMA-treated HEK293 and SH-SY5Y cells. Furthermore…

DNA ComplementaryTime FactorsADAM10Blotting WesternGenetic VectorsADAM17 ProteinTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorAlzheimer DiseaseZymogenEndopeptidasesPhorbol EstersCell AdhesionTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein kinase A signalingFurinProtein Kinase CProtein kinase CFurinMetalloproteinasebiologyChemistryMetalloendopeptidasesCyclic AMP-Dependent Protein KinasesPeptide FragmentsRatsCell biologyADAM ProteinsEctodomainBiochemistrybiology.proteinTetradecanoylphorbol AcetateCattleTumor necrosis factor alphaProprotein ConvertasesAmyloid Precursor Protein SecretasesSignal TransductionEuropean Journal of Biochemistry
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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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Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities

2014

Abstract Six structurally diverse cytotoxic gold compounds are reported to cause profound and differential inhibition of the three main catalytic activities of purified 20S proteasome whilst auranofin , an established gold(I) drug in clinical use, is nearly ineffective. In particular, the gold(I) complex [( pbiH ) Au ( PPh 3 )] PF 6 , turns out to be the most potent inhibitor of all three enzyme activities with sub-micromolar IC 50 values. The present results further support the view that proteasome inhibition may play a major – yet not exclusive – role in the cytotoxic actions of gold based anticancer agents.

DrugProteasome Endopeptidase ComplexAuranofinmedia_common.quotation_subjectAntineoplastic AgentsPharmacologyBiochemistry20s proteasomeProteasome Gold compounds Anticancer drugs Enzyme inhibitionCatalysisInorganic ChemistryInhibitory Concentration 50Structure-Activity RelationshipGold CompoundsCoordination ComplexesAuranofinmedicineHumansCytotoxic T cellmedia_commonchemistry.chemical_classificationCytotoxinsChemistryEnzymeProteasomeBiochemistryBiocatalysisOrganogold CompoundsProteasome Inhibitorsmedicine.drug
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