Search results for "Trypsin"

showing 10 items of 217 documents

Binding of human fibronectin to Aspergillus fumigatus conidia.

1996

Aspergillus fumigatus conidia exhibited the ability to bind purified human fibronectin, whereas mycelial forms did not bind the ligand, as detected by an indirect immunofluorescence assay with an antifibronectin polyclonal antibody after incubation of the cells with fibronectin. Flow cytometry confirmed that binding of the ligand to conidia was dose dependent and saturable. Pretreatment of the cells with trypsin markedly reduced binding, which suggested a protein nature for the binding sites present at the surface of conidia. Intact conidia were also able to adhere to fibronectin or antifibronectin antibodies, a significant reduction (from 88 to 92%) in the binding of conidia was noticed, t…

ImmunologyMicrobiologyAspergillus fumigatusFungal ProteinsMicemedicineAnimalsAspergillosisHumansTrypsinBinding siteGel electrophoresisFungal proteinbiologyAspergillus fumigatusLigand (biochemistry)biology.organism_classificationTrypsinFlow CytometryFibronectinsFibronectinInfectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinParasitologymedicine.drugResearch ArticleInfection and immunity
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Microarray analysis in sperm from fertile and infertile men without basic sperm analysis abnormalities reveals a significantly different transcriptom…

2007

Sperm analysis following World Health Organization guidelines is unable to explain the molecular causes of male infertility when basic sperm parameters are within a normal range and women do not present gynecologic pathology. Consequently, there is a need for accurate diagnostic tools in this area, and microarray technology emerges as promising. We present, for the first time, preliminary results of a comparison of sperm mRNA expression profiles between fertile and infertile men with normal semen parameters, discovering profound discrepancies between groups, with potential diagnostic and therapeutic possibilities.

InfertilityMaleSemenBiologyMale infertilityTranscriptomeAndrologyAntigens NeoplasmSemenmedicineHumansTrypsinRNA MessengerInfertility MaleOligonucleotide Array Sequence Analysisurogenital systemGynecologic pathologyGene Expression ProfilingObstetrics and GynecologyDNAgamma-Glutamyltransferasemedicine.diseaseSpermSpermatozoaGene expression profilingFertilityReproductive MedicineGene chip analysisTrypsinogenApoptosis Regulatory ProteinsFertility and sterility
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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Myoglobin on Silica: A Case Study of the Impact of Adsorption on Protein Structure and Dynamics

2013

International audience; If protein structure and function changes upon adsorption are well documented, modification of adsorbed protein dynamics remains a blind spot, despite its importance in biological processes. The adsorption of metmyoglobin on a silica surface was studied by isotherm measurements, microcalorimetry, circular dichroïsm, and UV-visible spectroscopy to determine the thermodynamic parameters of protein adsorption and consequent structure modifications. The mean square displacement and the vibrational densities of states of the adsorbed protein were measured by elastic and inelastic neutron scattering experiments. A decrease of protein flexibility and depletion in low freque…

Isothermal microcalorimetrytrypsin inhibitorCircular dichroismspectroscopySurface Propertiesserum albuminwaterAnalytical chemistrymetmyoglobin02 engineering and technology010402 general chemistry01 natural sciencesCondensed Matter::Materials Sciencechemistry.chemical_compoundAdsorptionProtein structureElectrochemistryAnimalsGeneral Materials Science[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPhysics::Chemical PhysicsQuantitative Biology::BiomoleculesProtein dynamicsnanoparticleneutron scatteringtransitionSurfaces and Interfacesstability021001 nanoscience & nanotechnologyCondensed Matter PhysicsSilicon Dioxide0104 chemical sciencesCondensed Matter::Soft Condensed MatterMyoglobinchemistryMetmyoglobinChemical physicsNanoparticlesThermodynamicsnormal modeAdsorption0210 nano-technologyProtein adsorption
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Collagenolytic proteinases in keratoconus.

2006

To study the proteolytic phenomena contributing to the pathogenesis of keratoconus, corneal enzymes with potential to cleave fibrillar collagen were studied.Immunohistochemical labeling was undertaken of conventional and novel mammalian collagenases (MMP-1, -2, -8, -13, and -14) of the matrix metalloproteinase (MMP) family and other collagenolytic proteinases of the serine (human trypsin-2) and cysteine (cathepsin K) endoproteinase families. The results were analyzed using a semiquantitative scoring system.Labeling of MMP-8 was moderate in healthy controls, but weak in keratoconus. Moderate MMP-2 and weak MMP-14 expressions were similar in controls and keratoconus. MMP-1 was slightly overex…

KeratoconusPathologymedicine.medical_specialtygenetic structuresCathepsin KMatrix metalloproteinaseKeratoconusPathogenesisCorneaImmunoenzyme TechniquesCorneamedicineCathepsin KHumansTrypsinCollagenaseschemistry.chemical_classificationmedicine.diseaseCathepsinseye diseasesMatrix MetalloproteinasesOphthalmologyEnzymemedicine.anatomical_structurechemistryCollagenaseTrypsinogenImmunohistochemistrysense organsKeratoplasty Penetratingmedicine.drugCornea
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Study of the bacillus thuringiensis Cry1Ia protein oligomerization promoted by midgut brush border membrane vesicles of lepidopteran and coleopteran …

2020

Bacillus thuringiensis (Bt) produces insecticidal proteins that are either secreted during the vegetative growth phase or accumulated in the crystal inclusions (Cry proteins) in the stationary phase. Cry1I proteins share the three domain (3D) structure typical of crystal proteins but are secreted to the media early in the stationary growth phase. In the generally accepted mode of action of 3D Cry proteins (sequential binding model), the formation of an oligomer (tetramer) has been described as a major step, necessary for pore formation and subsequent toxicity. To know if this could be extended to Cry1I proteins, the formation of Cry1Ia oligomers was studied by Western blot, after the incuba…

Leptinotarsa decemlineataBrush borderHealth Toxicology and MutagenesisBacillus thuringiensislcsh:MedicineSf21 cell lineOstrinia nubilalisToxicologyOligomer formationHemolysin Proteins<i>leptinotarsa decemlineata</i>03 medical and health sciencesWestern blotBacillus thuringiensisLobesia botranaSf9 CellsmedicineAnimalsProtein oligomerizationCry1AbIncubation<i>ostrinia nubilalis</i>030304 developmental biology0303 health sciencesBinding SitesBacillus thuringiensis ToxinsMicrovillimedicine.diagnostic_testbiology030306 microbiologyChemistryCommunicationVesiclelcsh:RfungiMembrane ProteinsMidgut<i>lobesia botrana</i>Trypsinbiology.organism_classificationColeopteraEndotoxinsLepidopteraBiochemistryBioassayProtein MultimerizationProtein Bindingmedicine.drug
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Alpha-1-antitrypsin-induced inhibition of complement-dependent phagocytosis.

1981

Abstract In a previous investigation, inhibition of complement-dependent rosette formation by alpha1-antitrypsin (α1-AT) was observed, and it was demonstrated that α1-AT interacts through its carbohydrate portion with C3 and its fragments. In the present study, the effect of α1-AT on the complement-receptor-mediated phagocytosis by human peripheral blood monocytes was examined. Purified α1-AT inhibited in a dose-dependent manner phagocytosis of C3-carrying yeast particles. Inhibition was selective, concerned only C3-receptor-mediated phagocytosis, neither Fc-receptor-mediated phagocytosis nor uptake of untreated yeast particles was blocked by α1-AT. It was demonstrated that α1-AT exerted it…

LeukemiaPhagocytosisImmunologyAlpha (ethology)Blood DonorsHematologyComplement receptorComplement C3Saccharomyces cerevisiaeCarbohydrateBiologyOpsonin ProteinsYeastPeripheral bloodMonocytesImmune systemBiochemistryPhagocytosisRosette formationalpha 1-AntitrypsinImmunology and AllergyHumansImmunobiology
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Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomes

1996

AbstractThe transcription factor c-Fos is a short-lived protein and calpains and ubiquitin-dependent systems have been proposed to be involved in its degradation. In this report, we consider a lysosomal degradation pathway for c-Fos. Using a cell-free assay, we have found that freshly isolated lysosomes can take up and degrade c-Fos with high efficiency. v-Fos, the oncogenic counterpart of c-Fos, can also be taken up by lysosomes, yet the amount of incorporated protein is much lower. c-Fos uptake is independent of its phosphorylation state but it appears to be regulated by dimerization with differentially phosphorylated forms of c-Jun, while v-Fos escapes this regulation. Moreover, we show …

LeupeptinsProto-Oncogene Proteins c-junBiophysicsProtein degradationProtein degradationTransfectionBiochemistryc-FosCell Linechemistry.chemical_compoundStructural BiologyLysosomeGeneticsmedicineAnimalsHumansProtease InhibitorsTrypsinPhosphorylationMolecular BiologyTranscription factorc-FosCell-Free Systembiologyc-junLeupeptinc-Junv-FosCalpainCell BiologyLysosomeRecombinant ProteinsRatsKineticsOncogene Proteins v-fosmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinPhosphorylationElectrophoresis Polyacrylamide GelLysosomesProto-Oncogene Proteins c-fosHeLa CellsFEBS Letters
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Photoaffinity Labeling and Photoaffinity Cross-Linking of Phosphofructokinase-1 from Saccharomyces cerevisiae by 8-Azidoadeninenucleotides

2001

Phosphofructokinase-1 from Saccharomyces cerevisiae is composed of four alpha- and four beta-subunits, each of them carrying catalytic and regulatory bindings sites for MgATP. In this paper, various photoaffinity labels, such as 8-azidoadenosine 5'-triphosphate, 8-azido-1,N6-ethenoadenosine 5'-triphosphate, and 8-N3-3'(2')-O-biotinyl-8-azidoadenosine 5'-triphosphate have been used to study their interaction with the enzyme in the dark and during irradiation. All nucleotidetriphosphates function as phosphate donor forming fructose 1,6-bisphosphate from fructose 6-phosphate. However, the kinetic analysis revealed distinctly differences between them. Photolabeling causes a decrease in enzyme a…

LightPhosphofructokinase-1Blotting WesternSaccharomyces cerevisiaeBiophysicsPhotoaffinity LabelsSaccharomyces cerevisiaePhotoaffinity LabelsBiochemistryAdenosine TriphosphateFructosediphosphatesChymotrypsinMagnesiumPhosphofructokinase 1Molecular Biologychemistry.chemical_classificationGel electrophoresisBinding SitesAffinity labelingbiologyPhotoaffinity labelingFructosephosphatesDarknessbiology.organism_classificationEnzyme assayKineticsProtein SubunitsCross-Linking ReagentsEnzymechemistryBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelArchives of Biochemistry and Biophysics
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The prophenoloxidase system is activated during the tunic inflammatory reaction of Ciona intestinalis

2008

Phenoloxidase (PO) activity was examined in the tunic tissue of Ciona intestinalis following lipopolysaccharide (LPS) intratunic injection. Tunic homogenate supernatant (THS), assayed with the Dopa-MBTH reaction, displayed Ca(2+)-independent PO activity that was raised by LPS and further enhanced by proteases. Specific inhibitors (tropolone, phenylthiourea, diethylthiocarbamate) supported the specificity of the reaction. Assay with soybean trypsin inhibitor showed that, in the tunic, PO activation with trypsin was not significantly inhibited suggesting that proteases diverse from serine proteases were involved. In vivo experiments were carried out by injecting isosmotic medium or LPS, and T…

LipopolysaccharidesProteasesHistologyBlotting WesternSettore BIO/05 - ZoologiaEnzyme-Linked Immunosorbent AssayPathology and Forensic MedicinemedicineAnimalsCiona intestinalisInflammationchemistry.chemical_classificationEnzyme PrecursorsbiologyKunitz STI protease inhibitorprophenoloxidase Ciona intestinalisCell BiologyProphenoloxidasebiology.organism_classificationTrypsinImmunohistochemistryMolecular biologyIn vitroCiona intestinalisUp-RegulationCionaEnzymechemistryPhenoloxidase . Hemocyte . Tunic . Inflammation . Lipopolysaccharide . SDS-polyacrylamide gel electrophoresis . Ciona intestinalisElectrophoresis Polyacrylamide GelCatechol Oxidasemedicine.drugCell and Tissue Research
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