Search results for "peptide fragments"

showing 10 items of 353 documents

Addressing substrate glutamine requirements for tissue transglutaminase using substance P analogues

1999

AbstractWe have investigated the effect on the substrate requirements for guinea pig liver (tissue) transglutaminase of a set of 11 synthetic glutamine substitution analogues making up the full sequence of the naturally occurring tissue transglutaminase substrate substance P. While a number of peptide sequences derived from proteins that are well-recognized as tissue transglutaminase substrates have been studied, the enzyme activity using substitution analogues of full-length natural substrates has not been investigated as thoroughly. Thus, our set of substance P analogues only differs from one to other by one amino acid mutation while the length (of the peptide) is maintained as in the nat…

Tissue transglutaminaseStereochemistryGlutamineGuinea PigsMolecular Sequence DataBiophysicsPeptideSubstance PBiochemistrySubstance P analogueSubstrate SpecificityResidue (chemistry)Structural BiologyGeneticsAnimalsAmino Acid SequenceMolecular Biologychemistry.chemical_classificationTransglutaminasesbiologySubstrate (chemistry)Cell BiologyTransglutaminasePeptide FragmentsEnzyme assayMultiple peptide synthesisAmino acidGlutamineEnzymeLiverchemistryBiochemistryMutationbiology.proteinFEBS Letters
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Insensitivity to Aβ42-lowering Nonsteroidal Anti-inflammatory Drugs and γ-Secretase Inhibitors Is Common among Aggressive Presenilin-1 Mutations

2007

Abeta42-lowering nonsteroidal anti-inflammatory drugs (NSAIDs) constitute the founding members of a new class of gamma-secretase modulators that avoid side effects of pan-gamma-secretase inhibitors on NOTCH processing and function, holding promise as potential disease-modifying agents for Alzheimer disease (AD). These modulators are active in cell-free gamma-secretase assays indicating that they directly target the gamma-secretase complex. Additional support for this hypothesis was provided by the observation that certain mutations in presenilin-1 (PS1) associated with early-onset familial AD (FAD) change the cellular drug response to Abeta42-lowering NSAIDs. Of particular interest is the P…

TransgeneMolecular Sequence DataMutantMice TransgenicCHO CellsBiologyPharmacologymedicine.disease_causeBiochemistryPresenilinMiceExonCricetulusAlzheimer DiseaseIn vivoCricetinaePresenilin-1medicineAnimalsHumansAmino Acid SequenceEnzyme InhibitorsMolecular BiologyMutationAmyloid beta-PeptidesSequence Homology Amino AcidDrug discoveryAnti-Inflammatory Agents Non-SteroidalCell BiologyPeptide FragmentsMutationbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseJournal of Biological Chemistry
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Longitudinal analysis of Mycobacterium tuberculosis 19-kDa antigen-specific T cells in patients with pulmonary tuberculosis: association with disease…

2003

CD8(+) T cells play a central role in immune protection against infection with Mycobacterium tuberculosis. One of the target epitopes for anti-M. tuberculosis directed CD8(+) T cells is the HLA-A2-restricted 19-kDa lipoprotein peptide VLTDGNPPEV. T cell clones directed against this epitope recognized not only the nominal peptide ligand, but also a closely related peptide (VPTDPNPPEV) from the HIV envelope gp120 (HIV(env) gp120) protein characterized by IFN-gamma release. This cross-reactivity was confirmed in ex vivo in M. tuberculosis 19-kDa tetramer-sorted T cells from patients with tuberculosis and in HIVgp120 tetramer-reactive T cells sorted from HIV(+) patients. M. tuberculosis 19-kDa …

TuberculosisHIV AntigensT cellImmunologyEpitopes T-LymphocyteHIV InfectionsCD146 AntigenBiologyCD8-Positive T-LymphocytesCross ReactionsHIV Envelope Protein gp120medicine.disease_causeEpitopeMycobacterium tuberculosisInterferon-gammaViral ProteinsAntigenBacterial ProteinsAntigens CDT-Lymphocyte SubsetsHLA-A2 AntigenmedicineImmunology and AllergyHumansTuberculosisLongitudinal StudiesNeural Cell Adhesion MoleculesAntigens BacterialMembrane GlycoproteinsMolecular MimicryGranulocyte-Macrophage Colony-Stimulating FactorT lymphocyteMycobacterium tuberculosisOncogene Proteins Viralmedicine.diseasebiology.organism_classificationVirologyPeptide FragmentsDNA-Binding ProteinsMolecular mimicrymedicine.anatomical_structureImmunologyInterleukin-4CD8BiomarkersEuropean journal of immunology
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Influence of photo-initiators in the preparation of methacrylate monoliths into poly(ethylene-co-tetrafluoroethylene) tubing for microbore HPLC.

2020

[EN] In this study, poly(butyl methacrylate-co-ethyleneglycol dimethacrylate) polymeric monoliths were in situ developed within 0.75 mm i.d. poly(ethylene-co-tetrafluoroethylene) (ETFE) tubing by UV polymerization via three different free-radical initiators fscce-azobisisobutyronitrile (AIBN), 2,2-dimethoxy-2-phenylacetophenone (DMPA) and 2-methyl-4'-(methylthio)-2-morpholinopropiophenone (MTMPP). The influence of the nature of each photo-initiator and irradiation time on the morphological features of the polymer was investigated by scanning electron microscopy, and the chromatographic properties of the resulting microbore columns were evaluated using alkyl benzenes as test substances. The …

Ultraviolet RaysMorpholines02 engineering and technologyPoly(ethylene-co-tetrafluoroethylene)Methacrylate01 natural sciencesBiochemistryAnalytical ChemistryPolymerizationchemistry.chemical_compoundETFEPolymethacrylic AcidsPhotograftingQUIMICA ANALITICANitrilesEnvironmental ChemistryReversed-phase liquid chromatographyPolytetrafluoroethyleneSpectroscopyAlkylChromatography High Pressure Liquidchemistry.chemical_classificationPropiophenonesChemistryHerbicidesPhenylurea Compounds010401 analytical chemistryAcetophenonesCaseinsPolymer monolithPolymerReversed-phase chromatography021001 nanoscience & nanotechnologyPhoto-initiatorPeptide Fragments0104 chemical sciencesPolymerizationPhotograftingMethacrylatesTetrafluoroethylene0210 nano-technologyNuclear chemistryAnalytica chimica acta
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In vitro and in vivo arterial differentiation of human multipotent adult progenitor cells

2006

Many stem cell types have been shown to differentiate into endothelial cells (ECs); however, their specification to arterial or venous endothelium remains unexplored. We tested whether a specific arterial or venous EC fate could be induced in human multipotent adult progenitor cells (hMAPCs) and AC133(+) cells (hAC133(+)). In vitro, in the presence of VEGF(165), hAC133(+) cells only adopted a venous and microvascular EC phenotype, while hMAPCs differentiated into both arterial and venous ECs, possibly because hMAPCs expressed significantly more sonic hedgehog (Shh) and its receptors as well as Notch 1 and 3 receptors and some of their ligands. Accordingly, blocking either of those pathways …

Vascular Endothelial Growth Factor ACellular differentiationImmunologyMice NudeNeovascularization PhysiologicCell SeparationBiochemistryMiceAntigens CDAnimalsHumansHedgehog ProteinsAC133 AntigenSonic hedgehogProgenitor cellNotch 1Cells CulturedGlycoproteinsMatrigelbiologyReceptors NotchEndothelial CellsCell DifferentiationCell BiologyHematologyPeptide FragmentsCell biologyEndothelial stem cellAdult Stem CellsMicroscopy ElectronImmunologybiology.proteinStem cellPeptidesAdult stem cellSignal Transduction:Ciencias de la Salud::Oncología [Materias Investigacion]
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Agonist and antagonist-dependent internalization of the human vasopressin V2 receptor.

1998

Abstract In this report we demonstrate that in HEK293 cells stably expressing the human V2vasopressin receptor, ligand-induced internalization of the hormone receptor occurs via the clathrin-dependent pathway. Studies of receptor trafficking either by direct visualization of the V2receptor by confocal microscopy or binding experiments show a rapid internalization (half-time 6–7 min). Blocking of the clathrin-dependent pathway by hypertonic sucrose increased vasopressin-induced cellular cAMP production and decreased the desensitization of the V2receptor–adenylyl cyclase system. Thus, internalization appears to be a major regulatory mechanism terminating vasopressin action in HEK293 cells. Tw…

VasopressinReceptors VasopressinTime Factorsmedia_common.quotation_subjectRecombinant Fusion ProteinseducationBiologyKidneyLigandsTransfectionlaw.inventionCell LineEpitopesDesensitization (telecommunications)Confocal microscopylawEnzyme-linked receptorHumansInternalizationReceptormedia_commonAntagonistCell BiologyClathrinPeptide FragmentsCell biologyHormone receptorAntidiuretic Hormone Receptor AntagonistsExperimental cell research
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Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion

2003

AbstractThe fusogenic subdomain of the Ebola virus envelope glycoprotein is an internal sequence located ca. 20 residues downstream the N-terminus of the glycoprotein transmembrane subunit. Partitioning of the Ebola fusion peptide into membranes containing phosphatidylinositol in the absence of Ca2+ stabilizes an α-helical conformation, and gives rise to vesicle efflux but not vesicle fusion. In the presence of millimolar Ca2+ the membrane-bound peptide adopts an extended β-structure, and induces inter-vesicle mixing of lipids. The peptide conformational polymorphism may be related to the flexibility of the virus–cell intermembrane fusogenic complex.

Vesicle fusionEbola glycoproteinSpectrophotometry InfraredProtein ConformationvirusesBiophysicsPeptideBiologymedicine.disease_causePhosphatidylinositolsBiochemistryMembrane FusionProtein Structure Secondarychemistry.chemical_compoundProtein structureFusion peptideMembranes (Biologia)Structural BiologyGeneticsmedicinePhosphatidylinositolMolecular Biologychemistry.chemical_classificationEbola virusVesicleCircular DichroismLipid bilayer fusionViral fusionWaterMembranes ArtificialCell BiologyEbolavirusLipidsTransmembrane proteinPeptide FragmentsBiochemistrychemistryLiposomesBiophysicsCalciumPèptidsPeptide–lipid interactionViral Fusion Proteins
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The Efficacy of Antigen Processing Is Critical for Protection against Cytomegalovirus Disease in the Presence of Viral Immune Evasion Proteins▿

2009

ABSTRACT Cytomegaloviruses (CMVs) code for immunoevasins, glycoproteins that are specifically dedicated to interfere with the presentation of antigenic peptides to CD8 T cells. Nonetheless, the biological outcome is not an immune evasion of the virus, since CD8 T cells can control CMV infection even when immunoevasins are expressed. Here, we compare the processing of a protective and a nonprotective epitope derived from the same viral protein, the antiapoptotic protein M45 in the murine model. The data provide evidence to conclude that protection against CMVs critically depends on antigenic peptides generated in an amount sufficient to exhaust the inhibitory capacity of immunoevasins.

Viral proteinImmunologyAntigen presentationCytomegalovirusBiologyCD8-Positive T-Lymphocytesmedicine.disease_causeMicrobiologyVirusEpitopeEpitopesMiceViral ProteinsImmune systemAntigenVirologyRibonucleotide ReductasesmedicineCytotoxic T cellAnimalsHumansAntigen PresentationAntigen processingVirologyPeptide FragmentsInsect ScienceImmunologyCytomegalovirus InfectionsPathogenesis and ImmunityApoptosis Regulatory Proteins
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The deubiquitinase USP11 is a versatile and conserved regulator of autophagy

2021

Autophagy is a major cellular quality control system responsible for the degradation of proteins and organelles in response to stress and damage to maintain homeostasis. Ubiquitination of autophagy-related proteins or regulatory components is important for the precise control of autophagy pathways. Here, we show that the deubiquitinase ubiquitin-specific protease 11 (USP11) restricts autophagy and that KO of USP11 in mammalian cells results in elevated autophagic flux. We also demonstrate that depletion of the USP11 homolog H34C03.2 in Caenorhabditis elegans triggers hyperactivation of autophagy and protects the animals against human amyloid-β peptide 42 aggregation-induced paralysis. USP11…

autophagyhAβ42 human amyloid-β protein 1 to 42Lipid kinase activityPI(3)P phosphatidylinositol-3-phosphatemTORC1BiochemistryCell LineGene Knockout Techniqueschemistry.chemical_compoundubiquitinAnimalsHumansULK1 unc-51-like autophagy activating kinase 1WIPI WD-repeat domain phosphoinositide-interacting proteinPI3KC3-C1Caenorhabditis elegansCaenorhabditis elegans ProteinsmTORC1Molecular BiologyMechanistic target of rapamycinUSP11 ubiquitin-specific protease 11proteostasisAmyloid beta-PeptidesS6K S6 kinasebiologyPhosphatidylinositol 3-phosphateAutophagyDUB deubiquitinaseLFQ label-free quantificationIP immunoprecipitationNHT nonhuman targetingPI3KC3-C1 class III phosphatidylinositol 3-kinase complex ICell BiologyACN acetonitrile amyloid-βNRBF2 nuclear receptor-binding factor 2Peptide FragmentsCell biologydeubiquitinase (DUB)ProteostasischemistryProteotoxicitymTORC1 mechanistic target of rapamycin complex 1biology.proteinAutophagy-Related Protein-1 HomologBSA bovine serum albuminThiolester HydrolasesResearch ArticleJournal of Biological Chemistry
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Iron and zinc bioavailability in Caco-2 cells: Influence of caseinophosphopeptides

2013

Abstract A study has been made of the influence of two pools of caseinophosphopeptides (CPPs) obtained from α s - and β-casein (CN) fractions, and of three specific CPPs (β-CN(1–25)4P, α s1 -CN(64–74)4P and α s2 -CN(1–19)4P), on iron bioavailability (ferritin synthesis) and zinc bioavailability (retention, transport and uptake of zinc) in Caco-2 cells. α-CPP and β-CPP pools did not improve ferritin synthesis, but the three specific CPPs showed an increase in ferritin synthesis in Caco-2 cells versus iron sulphate, β-CN(1–25)4P being the most effective. In relation to zinc bioavailability, α-CPPs, β-CPPs, α s1 -CN(64–74)4P and β-CN(1–25)4P increased zinc uptake. However, this increase was of…

biologyChemistryIronBiological AvailabilityCaseinsIron sulphatechemistry.chemical_elementBiological TransportGeneral MedicineZincPeptide FragmentsAnalytical ChemistryBioavailabilityFerritinZincBiochemistryCaco-2Ferritinsbiology.proteinHumansCaco-2 CellsZinc uptakeFood ScienceNuclear chemistryFood Chemistry
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