Search results for "DASE"

showing 10 items of 1891 documents

Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding act…

1998

AbstractGlycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.

ProteasesBasement membraneRecombinant proteinmedicine.medical_treatmentMolecular Sequence DataBiophysicsPerlecanBiochemistrySubstrate SpecificityStructural BiologyLamininEndopeptidasesGeneticsmedicineAnimalsAmino Acid SequenceBinding siteSite-directed mutagenesisMolecular BiologyGlycosaminoglycansSite-directed mutagenesisBinding SitesProteasebiologyChemistryMutagenesisCell BiologyRecombinant ProteinsBiochemistryProteoglycanProteoglycanProteolysisMutagenesis Site-Directedbiology.proteinProteoglycansHeparitin SulfateLamininHeparan Sulfate ProteoglycansProtein BindingFEBS Letters
researchProduct

Role of toxin activation on binding and pore formation activity of the Bacillus thuringiensis Cry3 toxins in membranes of Leptinotarsa decemlineata (…

2004

AbstractBinding and pore formation constitute key steps in the mode of action of Bacillus thuringiensis δ-endotoxins.In this work, we present a comparative analysis of toxin-binding capacities of proteolytically processed Cry3A, Cry3B and Cry3C toxins to brush border membranes (BBMV) of the Colorado potato beetle Leptinotarsa decemlineata (CPB), a major potato coleopteran-insect pest. Competition experiments showed that the three Cry3 proteolytically activated toxins share a common binding site. Also heterologous competition experiments showed that Cry3Aa and Cry3Ca toxins have an extra binding site that is not shared with Cry3Ba toxin. The pore formation activity of the three different Cry…

ProteasesBrush borderBacterial ToxinsBacillus thuringiensisBiophysicsmedicine.disease_causeBinding CompetitiveBiochemistryHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEndopeptidasesmedicineAnimalsProtoxin activationBinding siteProtein PrecursorsChymotrypsinBinding SitesbiologyBacillus thuringiensis ToxinsMicrovilliToxinColorado potato beetleCell MembranefungiCell Biologybiology.organism_classificationTrypsinColeopteraEndotoxinsBiochemistryMode of actionbiology.proteinmedicine.drugBiochimica et Biophysica Acta (BBA) - Biomembranes
researchProduct

Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.

2003

Objective—Modification with proteases and cholesterylesterase transforms LDL to a moiety that resembles lipoproteins isolated from atherosclerotic lesions and possesses atherogenic properties. To identify changes in monocyte-derived foam cells laden with enzymatically modified LDL (E-LDL), we compared patterns of the most abundant transcripts in these cells after incubation with LDL or E-LDL.Methods and Results—Serial analyses of gene expression (SAGE) libraries were constructed from human monocytes after treatment with LDL or E-LDL. Several tags were differentially expressed in LDL-treated versus E-LDL–treated cells, whereby marked selective induction by E-LDL of cathepsin H was conspicuou…

ProteasesCathepsin HCoronary Artery DiseaseBiologyCathepsin HCathepsin L1medicineMacrophageHumansFoam cellGene LibraryCathepsinMonocyteGene Expression ProfilingColocalizationSterol EsteraseMolecular biologyCathepsinsLipoproteins LDLCysteine Endopeptidasesmedicine.anatomical_structureCholesterolBiochemistryGene Expression Regulationlipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineFoam CellsArteriosclerosis, thrombosis, and vascular biology
researchProduct

The role of bestatin, an inhibitor of cell surface proteases, in the interaction of serum with untransformed cells in culture.

1981

Bestatin is an inhibitor of cell surface-associated aminopeptidase B and leucine aminopeptidase. This microbial product simulates the role of serum as an activator of uridine uptake in quiescent BHK cells. The compound significantly stimulates the incorporation of labelled thymidine into the acid-insoluble fraction of serum-starved Nil 8 cells in the presence of low concentration of serum. The possible mechanisms of these interactions are discussed.

ProteasesCellBiologyArginineAminopeptidaseAminopeptidaseschemistry.chemical_compoundAminopeptidase BLeucyl AminopeptidaseLeucineDrug DiscoverymedicineUridineCells CulturedPharmacologyActivator (genetics)Cell MembraneDNABlood Physiological PhenomenaMolecular biologyUridineStimulation Chemicalmedicine.anatomical_structurechemistryBiochemistryLeucineThymidineThymidineThe Journal of antibiotics
researchProduct

Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors.

1996

The extracellular domains of a diverse group of membrane proteins are shed in response to protein kinase C activators such as phorbol 12-myristate 13-acetate (PMA). The lack of sequence similarity in the cleavage sites suggests the involvement of many proteases of diverse specificity in this process. However, a mutant Chinese hamster ovary cell line recently isolated for being defective in PMA-activated shedding of the membrane-anchored growth factor transforming growth factor alpha precursor (proTGF-alpha) is concomitantly defective in the shedding of many other unrelated membrane proteins. Here we show that independent mutagenesis and selection experiments yield shedding mutants having th…

ProteasesCellCHO CellsBiologyHydroxamic AcidsTransfectionBiochemistryAmyloid beta-Protein PrecursorAntigens CDCricetinaemedicineAnimalsProtease InhibitorsL-SelectinProtein PrecursorsCell adhesionMolecular BiologyProtein kinase CMetalloproteinaseChinese hamster ovary cellCell MembraneGenetic Complementation TestMembrane ProteinsMetalloendopeptidasesCell BiologyReceptors InterleukinTransforming Growth Factor alphaReceptors Interleukin-6Cell biologyKineticsmedicine.anatomical_structurePhenotypeEctodomainMembrane proteinMutagenesisTetradecanoylphorbol AcetatePhenanthrolinesThe Journal of biological chemistry
researchProduct

A cellular metalloproteinase activates Vibrio cholerae pro-cytolysin.

2004

Many strains of Vibrio cholerae produce a cytolysin (VCC) that forms oligomeric transmembrane pores in animal cells. The molecule is secreted as a procytolysin (pro-VCC) of 79 kDa that must be cleaved at the N terminus to generate the active 65-kDa toxin. Processing can occur in solution, and previous studies have described the action of mature VCC thus generated. However, little is known about the properties of pro-VCC itself. In this study, it is shown that pro-VCC exist as a monomer in solution and binds as a monomer to eukaryotic cells. Bound pro-VCC can then be activated either by exogenous, extracellular, or by endogenous, cell-bound proteases. In both cases, cleavage generates the 65…

ProteasesCholera Toxingenetic structuresCHO CellsBiologyADAM17 Proteinmedicine.disease_causeBiochemistryMiceCricetinaemedicineADAM17 ProteinAnimalsHumansProtein PrecursorsMolecular BiologyFurinMetalloproteinaseCytotoxinsCell MembraneMetalloendopeptidasesCell BiologyADAM Proteinseye diseasesTransmembrane proteinADAM ProteinsBiochemistryVibrio choleraebiology.proteinsense organsCytolysinRabbitsThe Journal of biological chemistry
researchProduct

Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenes…

2011

AbstractOver the past years the members of the type II transmembrane serine protease (TTSP) family have emerged as new players in mammalian biology. TMPRSS4 (transmembraneprotease/serine) is overexpressed in several human cancer tissues, promoting invasion, migration, and metastasis. However, the physiological function has not yet been elucidated. Here, we present morpholino knockdown studies targeting TMPRSS4a, a homolog of human TMPRSS4 in zebrafish embryos. By RT-PCR, we could demonstrate an expression of this protease already 5 h post-fertilization, suggesting important functions in the early stages of embryonic development. Indeed,in vivogene silencing caused severe defects in tissue d…

ProteasesEmbryo NonmammalianMorpholinoOrganogenesisCellular differentiationmedicine.medical_treatmentMolecular Sequence DataClinical BiochemistryBiologyBiochemistry03 medical and health sciences0302 clinical medicineCell AdhesionmedicineAnimalsHumansAmino Acid SequenceCell adhesionMolecular BiologyPhylogenyZebrafish030304 developmental biologySerine protease0303 health sciencesProteaseCell adhesion moleculeGene Expression ProfilingSerine EndopeptidasesProteolytic enzymesGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationZebrafish ProteinsMolecular biologyGene Knockdown Techniques030220 oncology & carcinogenesisbiology.proteinSequence AlignmentBiological Chemistry
researchProduct

Kinetics of thrombomodulin release and endothelial cell injury by neutrophil-derived proteases and oxygen radicals

2002

Thrombomodulin is a transmembranous glycoprotein of endothelial cells. In vitro it is a marker of endothelial cell injury. In vivo the levels of serum thrombomodulin are regarded as a parameter of activity in vasculitides. The latter are pathophysiologically determined by neutrophil-derived inflammation and endothelial cell injury caused by secretion of proteases and hydrogen peroxide. It was the objective of this study to determine whether thrombomodulin is only a late marker of advanced endothelial cell injury or whether it indicates also earlier stages of cell alterations. Over 24 hr endothelial cell cultures were incubated with hydrogen peroxide or the neutrophil proteases proteinase-3,…

ProteasesEndotheliumCell SurvivalNeutrophilsThrombomodulinImmunologyCell Culture TechniquesApoptosisBiologyCathepsin GThrombomodulinchemistry.chemical_compoundEndopeptidasesCell AdhesionmedicineHumansImmunology and AllergyViability assayCathepsinHydrogen PeroxideOriginal ArticlesMolecular biologyEndothelial stem cellmedicine.anatomical_structureMicroscopy FluorescencechemistryApoptosisEndothelium VascularReactive Oxygen SpeciesImmunology
researchProduct

Neutrophil Extracellular Traps as a Drug Target to Counteract Chronic and Acute Inflammation

2019

Neutrophil extracellular traps (NET), extruded decondensated chromatin entangled with neutrophil proteases, have been first identified in neutrophils stimulated with bacteria or phorbol myristate acetate (PMA) via activation of NADPH oxidase and the generation of reactive oxygen species. Although the first findings demonstrated the beneficial role of NET formation by trapping the bacteria and limiting their dissemination, numerous studies in the recent decade revealed the multifunctional aspects of NET formation which manifests itself not only in the context of anti-microbial effect but also as a pathological trigger. Uncontrolled and exaggerated NET formation or inability to digest and rem…

ProteasesNeutrophilsPharmaceutical ScienceInflammationExtracellular TrapsmedicineHumansMolecular Targeted TherapyInflammationchemistry.chemical_classificationReactive oxygen speciesNADPH oxidasebiologyNADPH OxidasesNeutrophil extracellular trapsChromatinCell biologyHistonechemistryAcute DiseaseChronic Diseasebiology.proteinSignal transductionmedicine.symptomReactive Oxygen SpeciesOxidation-ReductionSignal TransductionBiotechnologyCurrent Pharmaceutical Biotechnology
researchProduct

Processing without proteolytic cleavage is required for recognition of insulin by T cells.

1990

Beef insulin as well as a chymotryptic A-chain fragment [BI-A1-14(SSO3-)3] need uptake by antigen-presenting cells (APC) for efficient presentation in combination with major histocompatibility complex class II molecules to insulin-specific T cells. This could be shown by the inability of aldehyde-fixed APC to present these antigens to T cells. Furthermore, presentation of the insulin fragment as well as presentation of ovalbumin (OVA) was inhibited by treatment of APC with chloroquine, cerulenin or tunicamycin. This was not the case for a processing-independent OVA peptide. Treatment of APC during antigen pulsing with various protease inhibitors, active on all classes of proteases, did not …

ProteasesOvalbuminmedicine.medical_treatmentT-LymphocytesImmunologyAntigen presentationAntigen-Presenting CellsBiologyIn Vitro TechniquesEpitopeCell Linechemistry.chemical_compoundMiceAntigenEndopeptidasesmedicineImmunology and AllergyAnimalsInsulinProtease InhibitorsAntigen-presenting cellProteaseInsulinTunicamycinChloroquineTunicamycinEndocytosischemistryBiochemistryEuropean journal of immunology
researchProduct