Search results for "aminopeptidase"

showing 10 items of 56 documents

Morphological studies on CLN2

2001

Electron microscopic, fluorescence microscopic, and immunohistochemical studies earlier performed on archivalcerebral tissue from Max Bielchowsky's original three patients revealed curvilinear bodies rich in subunit C of mitochondrial ATP synthase (SCMAS). Recent progress in the elucidation of CLN2, i.e. identification of the defective lysosomal enzyme tripeptidyl-peptidase I (TPP-I) and mutations in the CLN2 gene have further corroborated earlier data. Immunohistochemically the absence of the TPP-I protein could be confirmed in the archival tissues using pathological controls. Unlike biochemistry, immunohistochemistry enables examination of these archival tissues elucidating the causative …

MaleCell typePathologymedicine.medical_specialtyProtein subunitEncephalopathyBiologymedicine.disease_causeAminopeptidasesNeuronal Ceroid-LipofuscinosesChloroquineEndopeptidasesmedicineHumansChildDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMyopathyGeneMutationTripeptidyl-Peptidase 1BrainGeneral MedicineMitochondrial Proton-Translocating ATPasesmedicine.diseaseImmunohistochemistryProton-Translocating ATPasesMutationPediatrics Perinatology and Child HealthImmunohistochemistryFemaleNeurology (clinical)Serine Proteasesmedicine.symptomPeptide Hydrolasesmedicine.drugEuropean Journal of Paediatric Neurology
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Shotgun Proteomics of Isolated Urinary Extracellular Vesicles for Investigating Respiratory Impedance in Healthy Preschoolers

2021

Urine proteomic applications in children suggested their potential in discriminating between healthy subjects from those with respiratory diseases. The aim of the current study was to combine protein fractionation, by urinary extracellular vesicle isolation, and proteomics analysis in order to establish whether different patterns of respiratory impedance in healthy preschoolers can be characterized from a protein fingerprint. Twenty-one 3–5-yr-old healthy children, representative of 66 recruited subjects, were selected: 12 late preterm (LP) and 9 full-term (T) born. Children underwent measurement of respiratory impedance through Forced Oscillation Technique (FOT) and no significant differen…

MaleProteomePharmaceutical SciencePhysiologyUrineUrineProteomicsAminopeptidasesAnalytical Chemistry0302 clinical medicineDrug DiscoveryElectric ImpedanceMedicineRespiratory systemproteomic0303 health sciencesTripeptidyl-Peptidase 1urine fractionationExtracellular vesicleTripeptidyl peptidase IRespiratory Function Testsforced oscillation techniqueChemistry (miscellaneous)Child PreschoolMolecular MedicineFemaleUrinary systemReceptors Cell SurfaceArticlelcsh:QD241-441Extracellular Vesicles03 medical and health sciencesproteomicslcsh:Organic chemistryHumansNerve Growth FactorsPhysical and Theoretical ChemistryDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEye ProteinsShotgun proteomicsAngiopoietin-Like Protein 2Serpins030304 developmental biologypreschooler healthy childrenbusiness.industryOrganic ChemistryCubilinAngiopoietin-like Proteins030228 respiratory systemThy-1 Antigensextracellular vesicleSerine Proteasesbusiness
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Identification and properties of the cell membrane bound leucine aminopeptidase interacting with the potential immunostimulant and chemotherapeutic a…

1983

Bestatin was found to be a competitive inhibitor (with respect to the Leu-NA substrate) not only of the isolated microsomal and cytosolic leucine aminopeptidases (Leu-APm and Leu-APc) but also of the aminopeptidases (APs) present in membrane preparations (from mouse liver) and on the cell surface of L5178Y cells. Kinetic parameters indicate that cellular AP is identical to Leu-APm. To rule out the possibility that AP-B is involved in the inhibition reactions, comparable studies with amastatin were performed. Electrophoretical studies revealed the solubilized cell membrane bound AP to co-migrate with Leu-APm in polyacrylamide gels. The activity of the separated membrane AP was inhibited by b…

MaleSurface PropertiesCellBiochemistryAminopeptidaseBinding CompetitiveCell membranechemistry.chemical_compoundLeucyl AminopeptidaseMiceAmastatinCytosolLeucinemedicineAnimalsCells CulturedPharmacologyBinding SitesChemistryCell CycleCell MembraneCell cycleCytosolmedicine.anatomical_structureBiochemistryMicrosomeMice Inbred CBALeucineProtein BindingBiochemical pharmacology
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Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa

2007

Abstract Background The presence of small membranous particles characterizes the male genital fluids of different mammalian species. The influence of semen vesicles, denominated prostasomes, on sperm functional properties has been well documented in humans, but their biological activity is scarcely known in other species. The present work investigated prostasome-like vesicles in pig semen for their ability to interact with spermatozoa and to affect acrosome reaction. Methods Prostasome-like vesicles have been isolated from pig seminal plasma by high-speed centrifugation and Sephadex G-200 gel chromatography. Morphology of purified vesicles has been checked by scanning electron microscopy wh…

Maleendocrine systemlcsh:QH471-489SwineAcrosome reactionSemenCentrifugationBiologyAminopeptidaseslcsh:Gynecology and obstetricsEndocrinologySemenAnimalslcsh:ReproductionCentrifugationlcsh:RG1-991urogenital systemVesicleAcrosome ReactionSecretory VesiclesResearchObstetrics and GynecologyProteinsBiological activitySecretory VesicleSpermMolecular biologySpermatozoaCell biologyReproductive MedicineMicroscopy Electron ScanningProstasomesElectrophoresis Polyacrylamide GelDevelopmental BiologyReproductive Biology and Endocrinology
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Intracellular localisation of some peptidases and alpha-mannosidase in cotyledons of resting kidney bean, Phaseolus vulgaris

1986

Cotyledons of resting kidney beans (Phaseolus vulgaris, L., cv. “Processor”) contain high activities of two alkaline peptidases, an aminopeptidase (EC 3.4.11) acting on Leu-Tyr and Leu-Gly-Gly and a dipeptidase (EC 3.4.13) hydrolysing Ala-Gly together with low activities of neutral naphthyiamidases (marker substrate Leu-β-NA) and of acid carboxypeptidases (EC 3.4.16; marker substrate Z-Phe-Ala). The intracellular localisation of these peptidases and that of α-mannosidase (EC 3.2.1.24) was studied by subcellular fractionations in different media. In density gradient centrifugations in non-aqueous glycerol-potassium iodide media the alkaline peptidases remained mainly in the application zone …

MannosidaseDipeptidasebiologyPhysiologyCell BiologyPlant ScienceGeneral Medicinebiology.organism_classificationCarboxypeptidaseAminopeptidaseCytosolBiochemistryProtein bodyGeneticsbiology.proteinCell fractionationPhaseolusPhysiologia Plantarum
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Structure-Guided, Single-Point Modifications in the Phosphinic Dipeptide Structure Yield Highly Potent and Selective Inhibitors of Neutral Aminopepti…

2014

Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides (the etiological agent of meningitis, NmAPN) complexed with organophosphorus compounds were resolved to determine the optimal inhibitor–enzyme interactions. The enantiomeric phosphonic acid analogs of Leu and hPhe, which correspond to the P1 amino acid residues of well-processed substrates, were used to assess the impact of the absolute configuration and the stereospecific hydrogen bond network formed between the aminophosphonate polar head and the active site residues on the binding affinity. For the hPhe analog, an imperfect stereochemical complementarity could be overcome by incorporating an appropriate P1 side…

MeningitidesStereochemistryHeteroatomAminopeptidases01 natural sciencesArticleLeucyl AminopeptidaseStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundDrug DiscoveryHumansProtease Inhibitors030304 developmental biology0303 health sciencesBinding SitesDipeptidebiology010405 organic chemistryHydrogen bondAbsolute configurationActive siteLigand (biochemistry)0104 chemical scienceschemistryAminophosphonateDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Leucine aminopeptidase is an immunodominant antigen of Fasciola hepatica excretory and secretory products in human infections.

2007

ABSTRACT The liver fluke Fasciola hepatica parasitizes humans and ruminant livestock worldwide, and it is now being considered a reemerging zoonotic disease, especially in areas in which it is endemic, such as South America. This study investigates the immune response to excretory and secretory products produced by F. hepatica in a group of patients from the Peruvian Altiplano, where the disease is highly endemic. Using a proteomic approach and immunoblotting techniques, we have identified the enzymes leucine aminopeptidase (LAP) and phosphoenolpyruvate carboxykinase as immunodominant antigens recognized by sera from fasciolosis patients. An indirect enzyme-linked immunosorbent assay using …

Microbiology (medical)FascioliasisAdolescentClinical BiochemistryImmunologyBlotting WesternMolecular Sequence DataSheep DiseasesEnzyme-Linked Immunosorbent AssayAminopeptidasePolymerase Chain ReactionLeucyl AminopeptidaseImmune systemAntigenHepaticaparasitic diseasesmedicineImmunology and AllergyFasciola hepaticaAnimalsHumansElectrophoresis Gel Two-DimensionalFasciolosisChildDNA PrimersSheepbiologyBase SequenceImmunodominant EpitopesClinical and Diagnostic Laboratory ImmunologyLiver flukeFasciola hepaticabiology.organism_classificationmedicine.diseaseVirologyExcretory systemAntigens HelminthChild PreschoolClinical and vaccine immunology : CVI
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The Streptomyces coelicolor Small ORF trpM Stimulates Growth and Morphological Development and Exerts Opposite Effects on Actinorhodin and Calcium-De…

2020

In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many others still deserve further investigations. In this regard, the possible role of many small open reading frames (smORFs) in actinomycete morpho-physiological differentiation is still elusive. In Streptomyces coelicolor, inactivation of the smORF trpM (SCO2038) – whose product modulates L-tryptophan biosynthesis – impairs production of antibiotics and morphological differentiation. Indeed, it was demonstrated that TrpM is able to interact w…

Microbiology (medical)Primary and secondary metabolismlcsh:QR1-502cytosol aminopeptidaseStreptomyces coelicoloractinorhodin productionSettore BIO/19 - Microbiologia GeneraletrpM.MicrobiologyAminopeptidaselcsh:MicrobiologyActinorhodin03 medical and health scienceschemistry.chemical_compoundBiosynthesisTRPMSmall open reading frameProtein biosynthesis030304 developmental biologychemistry.chemical_classificationsmall open reading frame0303 health sciencescalcium-dependent antibioticCalcium-dependent antibioticbiologysmall open reading frame trpM actinorhodin production Streptomyces coelicolor cytosol aminopeptidase calcium-dependent antibiotic primary and secondary metabolism030306 microbiologyActinorhodin productionStreptomyces coelicolorprimary and secondary metabolismtrpMbiology.organism_classificationAmino acidMetabolic pathwaychemistryBiochemistryCytosol aminopeptidaseFrontiers in Microbiology
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Phosphonic Acid Analogs of Fluorophenylalanines as Inhibitors of Human and Porcine Aminopeptidases N: Validation of the Importance of the Substitutio…

2020

International audience; A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results fro…

Models MolecularMolecular modelPhosphorous AcidsSwineStereochemistrylcsh:QR1-502chemistry.chemical_elementPhenylalanine[CHIM.THER]Chemical Sciences/Medicinal ChemistryCD13 AntigensRing (chemistry)Biochemistrylcsh:MicrobiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinefluorineinhibitorsChlorineSide chainAnimalsHumansMolecular BiologyEnzyme Assays030304 developmental biologyphosphonic acid analogschemistry.chemical_classification0303 health sciencesTrifluoromethyl[CHIM.ORGA]Chemical Sciences/Organic chemistrymolecular modelingReproducibility of ResultsStereoisomerismMolecular Docking SimulationEnzymechemistry030220 oncology & carcinogenesishuman and porcine aminopeptidaseEnantiomerMolecules
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Mutations in the Bacillus thuringiensis Cry1Ca toxin demonstrate the role of domains II and III in specificity towards Spodoptera exigua larvae

2004

Several mutants of the Bacillus thuringiensis Cry1Ca toxin affected with regard to specific activity towards Spodoptera exigua were studied. Alanine was used to replace single residues in loops 2 and 3 of domain II (mutant pPB19) and to replace residues 541– 544 in domain III (mutant pPB20). Additionally, a Cry1Ca mutant combining all mutations was constructed (mutant pPB21). Toxicity assays showed a marked decrease in toxicity against S. exigua for all mutants, while they retained their activity against Manduca sexta, confirming the importance of these residues in determining insect specificity. Parameters for binding to the specific receptors in BBMV (brush border membrane vesicles) of S.…

Models MolecularMutantLaboratory of Virologyaminopeptidase nmedicine.disease_causeBiochemistrybrush-border membraneToxin oligomerizationSubstrate SpecificityBacterial toxin; Manduca sexta; Mode of action; Protoxin activation; Toxin oligomerization; Toxin receptor bindingHemolysin Proteinsmanduca-sextaBacillus thuringiensisheliothis-virescensAlanine:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MicrovillibiologyPRI BioscienceBiochemistryMode of actionLarvaThermodynamicsResearch ArticleProtein BindingBacterial Toxinspink-bollwormBacillus thuringiensisSpodopteraSpodopteraBinding CompetitiveManduca sextaLaboratorium voor VirologieBacterial ProteinsExiguamedicineirreversible bindingAnimalscrystal proteinsProtoxin activationProtein Structure QuaternaryMode of actionMolecular BiologyBacillus thuringiensis ToxinsToxin receptor bindingToxininsecticidal toxinpore formationCytoplasmic VesiclesfungiUNESCO::CIENCIAS DE LA VIDA::BioquímicaBacterial toxinCell Biologybiology.organism_classificationProtein Structure TertiaryEndotoxinsManduca sextaMutationcryia delta-endotoxins
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