Search results for "FRAGMENTS"

showing 10 items of 422 documents

Exacerbated experimental autoimmune encephalomyelitis in mast-cell-deficient KitW-sh/W-sh mice

2011

Mast cell (MC)-deficient c-Kit mutant Kit(W/W-v) mice are protected against experimental autoimmune encephalomyelitis (EAE), an animal model of multiple sclerosis, suggesting a detrimental role for MCs in this disease. To further investigate the role of MCs in EAE, we took advantage of a recently characterized model of MC deficiency, Kit(W-sh/W-sh). Surprisingly, we observed that myelin oligodendrocyte glycoprotein (MOG)(35-55)-induced chronic EAE was exacerbated in Kit(W-sh/W-sh) compared with Kit(+/+) mice. Kit(W-sh/W-sh) mice showed more inflammatory foci in the central nervous system (CNS) and increased T-cell response against myelin. To understand whether the discrepant results obtaine…

Central Nervous SystemT-LymphocytesEncephalomyelitisexperimental autoimmune encephalomyelitismast cellsInbred C57BLSeverity of Illness IndeximmunologyMiceMyelinPeptide Fragmentimmune system diseasesMast CellEncephalomyelitisMyelin SheathbiologyExperimental autoimmune encephalomyelitisMast cellProto-Oncogene Proteins c-kitPhenotypemedicine.anatomical_structuremastcell-deficient miceBone Marrow Cellgenetics/immunology/pathology/prevention /&/ controlc-kit mutationsc-kit mutations; experimental autoimmune encephalomyelitis; granulocytes; mast cellsEncephalomyelitis Autoimmune ExperimentalCentral nervous systemBone Marrow CellsPathology and Forensic MedicineMyelin oligodendrocyte glycoproteinExperimentalAnimals Antibody Formation Bone Marrow Cells; pathology Central Nervous System; pathology Encephalomyelitis; Autoimmune; Experimental; genetics/immunology/pathology/prevention /&/ control Glycoproteins; immunology Granulocytes; pathology Immunization Mast Cells; pathology Mice Mice; Inbred C57BL Mutation Myelin Sheath; immunology Myelin-Oligodendrocyte Glycoprotein Peptide Fragments; immunology Phenotype Proto-Oncogene Proteins c-kit; deficiency/genetics/metabolism Severity of Illness Index T-Lymphocytes; pathologyAntigendeficiency/genetics/metabolismmedicineAnimalsMolecular BiologyGlycoproteinsAnimalMultiple sclerosismast-cell-deficient Kit W-sh/W-sh mice.Experimental autoimmune encephalomyelitis; mast-cell-deficient Kit W-sh/W-sh mice.GranulocytegranulocytesCell Biologymedicine.diseaseEncephalomyelitiExperimental autoimmune encephalomyelitiPeptide FragmentsMice Inbred C57BLT-LymphocyteAntibody FormationMutationImmunologybiology.proteinexperimental autoimmune encephalomyelitis; mastcell-deficient mice; mast cellspathologyImmunizationMyelin-Oligodendrocyte GlycoproteinGlycoproteinAutoimmuneLaboratory Investigation
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Making Broad Proteome Protein Measurements in 1−5 min Using High-Speed RPLC Separations and High-Accuracy Mass Measurements

2005

The throughput of proteomics measurements that provide broad protein coverage is limited by the quality and speed of both the separations as well as the subsequent mass spectrometric analysis; at present, analysis times can range anywhere from hours (high throughput) to days or longer (low throughput). We have explored the basis for proteomics analyses conducted on the order of minutes using high-speed capillary RPLC combined through on-line electrospray ionization interface with high-accuracy mass spectrometry (MS) measurements. Short 0.8-microm porous C18 particle-packed 50-microm-i.d. capillaries were used to speed the RPLC separations while still providing high-quality separations. Both…

Chemical ionizationElectrosprayTime FactorsChromatographyProteomeChemistryElutionElectrospray ionizationAnalytical chemistryMass spectrometryMass SpectrometryPeptide FragmentsFourier transform ion cyclotron resonanceFourier transform spectroscopyAnalytical ChemistrySpectroscopy Fourier Transform InfraredAnimalsHumansTrypsinHydrophobic and Hydrophilic InteractionsIon cyclotron resonanceChromatography LiquidAnalytical Chemistry
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Influenza A virus infection inhibits the efficient recruitment of Th2 cells into the airways and the development of airway eosinophilia.

2003

Abstract Most infections with respiratory viruses induce Th1 responses characterized by the generation of Th1 and CD8+ T cells secreting IFN-γ, which in turn have been shown to inhibit the development of Th2 cells. Therefore, it could be expected that respiratory viral infections mediate protection against asthma. However, the opposite seems to be true, because viral infections are often associated with the exacerbation of asthma. For this reason, we investigated what effect an influenza A (flu) virus infection has on the development of asthma. We found that flu infection 1, 3, 6, or 9 wk before allergen airway challenge resulted in a strong suppression of allergen-induced airway eosinophil…

ChemokineEpitopes T-LymphocyteImmunoglobulin Emedicine.disease_causeMiceCell MovementInfluenza A virusImmunology and AllergyEosinophiliaChemokine CCL5LungCells CulturedChemokine CCL2Mice KnockoutMice Inbred BALB Cbiologymedicine.diagnostic_testrespiratory systemUp-Regulationmedicine.anatomical_structureInfluenza A virusChemokines CCGoblet CellsNippostrongylusmedicine.symptomBronchial HyperreactivityChemokine CCL11OvalbuminImmunologyDown-RegulationMice TransgenicCCL5VirusInterferon-gammaTh2 CellsOrthomyxoviridae InfectionsLymphopeniamedicineAnimalsLymphocyte CountPulmonary EosinophiliaStrongylida InfectionsGoblet cellMetaplasiaAllergensPeptide Fragmentsrespiratory tract diseasesMice Inbred C57BLBronchoalveolar lavageImmunologyCell Migration Inhibitionbiology.proteinInterleukin-5Journal of immunology (Baltimore, Md. : 1950)
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Combination of clinical risk profile, early exercise testing and circulating biomarkers for evaluation of patients with acute chest pain without ST-s…

2007

Objective: To investigate the combination of clinical data, exercise testing and biomarkers for the evaluation of patients with chest pain without ST-segment deviation or troponin elevation. Design: Prospective cohort design. Settting: Two teaching hospitals in Spain. Patients: 422 patients presenting to the emergency department were studied. Leukocyte count, C-reactive protein (CRP), pregnancy-associated plasma protein A (PAPP-A) and N-terminal pro-brain natriuretic peptide (NTproBNP) were determined. A validated clinical risk score (number of points according to pain characteristics and risk factors) was used for clinical evaluation and early exercise testing was performed. Main outcome m…

Chest Painmedicine.medical_specialtyMyocardial InfarctionPhysical exerciseChest painInternal medicineNatriuretic Peptide BrainmedicineHumansMyocardial infarctionRisk factorProspective cohort studyFramingham Risk Scorebiologybusiness.industryST elevationMiddle Agedmedicine.diseaseTroponinPeptide FragmentsTroponinSurgeryExercise Testbiology.proteinCardiologymedicine.symptomEpidemiologic MethodsCardiology and Cardiovascular MedicinebusinessBiomarkersHeart
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Entrapment of A Beta 1-40 peptide in unstructured aggregates

2012

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…

Circular dichroismAmyloidKineticsPeptideProtein Structure SecondaryFIBRIL FORMATIONDynamic light scatteringMEMBRANE DISRUPTIONGeneral Materials ScienceFiberATOMIC-FORCE MICROSCOPYchemistry.chemical_classificationAmyloid beta-PeptidesChemistryProtein StabilityOsmolar ConcentrationTemperatureFibrillogenesisCondensed Matter PhysicsReceptor–ligand kineticsPeptide FragmentsAMYLOID-BETA-PROTEINALZHEIMERS-DISEASECrystallographyKineticsSpectrometry FluorescenceBiophysicsProtein Multimerization
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Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
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Carnosine Inhibits Aβ42Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster

2013

Aggregation of the amyloid-β peptide (Aβ) into fibrillar structures is a hallmark of Alzheimer's disease. Thus, preventing self-assembly of the Aβ peptide is an attractive therapeutic strategy. Here, we used experimental techniques and atomistic simulations to investigate the influence of carnosine, a dipeptide naturally occurring in the brain, on Aβ aggregation. Scanning force microscopy, circular dichroism and thioflavin T fluorescence experiments showed that carnosine does not modify the conformational features of Aβ42 but nonetheless inhibits amyloid growth. Molecular dynamics (MD) simulations indicated that carnosine interacts transiently with monomeric Aβ42 by salt bridges with charge…

Circular dichroismMagnetic Resonance Spectroscopy1303 BiochemistryStereochemistryStatic ElectricityCarnosinePeptideMolecular Dynamics SimulationBiochemistryproteinprotein interactionsProtein–protein interactionchemistry.chemical_compoundMolecular dynamicsnutraceutical compounds10019 Department of Biochemistry1312 Molecular BiologyMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesDipeptideHydrogen bondOrganic ChemistryIntermolecular forceTemperatureneuroprotective agentHydrogen BondingAlzheimer's diseasePeptide Fragmentsmolecular dynamicscarnosinechemistry1313 Molecular Medicine570 Life sciences; biologyMolecular MedicineHydrophobic and Hydrophilic Interactionsprotein aggregation fibrillogenesis carnosine AFM1605 Organic ChemistryChemBioChem
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Aß(25-35) and its C-and/or N-blocked derivatives: copper driven structural features and neurotoxicity

2006

The toxic properties of beta-amyloid protein, Abeta(1-42), the major component of senile plaques in Alzheimer's disease, depend on nucleation-dependent oligomerization and aggregation. In addition, Abeta(1-42) toxicity is favored by the presence of trace metals, which affect the secondary structure of the peptide. A peptide comprising 11 residues within Abeta(1-42) [Abeta(25-35)] aggregates and retains the neurotoxic activity of Abeta(1-42). We have used both Abeta(25-35) and its C-amidated or N-acetylated/C-amidated derivatives to investigate the role of copper(II) in modulating the conformation and aggregation state as well as the neurotoxic properties of amyloid peptides. Electrospray io…

Circular dichroismSpectrometry Mass Electrospray IonizationAmyloidProtein Conformationb-amyloidNeurotoxinsPeptideMicroscopy Atomic ForceCellular and Molecular NeuroscienceProtein structuremental disordersmedicineAnimalsSenile plaqueschemistry.chemical_classificationCerebral CortexNeuronsAmyloid beta-PeptidesCircular DichroismCopper toxicityNeurotoxicityP3 peptideElectron Spin Resonance SpectroscopyAlzheimer's diseasemedicine.diseasePeptide Fragmentsnervous system diseasesRatschemistryBiochemistrycopperModels AnimalBiophysicsAlzheimer’s disease
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Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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The reconstitution of human C1, the first complement component Binding of C1r and C1s to C1q influences the C1q conformation

1981

Complement Activating EnzymesMacromolecular SubstancesProtein ConformationBiophysicsPlasma protein bindingBiochemistryProtein structureComplement C1Structural BiologyGeneticsHumansTrypsinMolecular BiologyComplement C1qComplement C1sEnzyme PrecursorsComplement C1sComplement C1rChemistryComponent (thermodynamics)Complement C1qComplement component 7Immunoglobulin Fc FragmentsCell BiologyHydrogen-Ion ConcentrationImmunoglobulin Fc FragmentsComplement (complexity)BiophysicsProtein BindingFEBS Letters
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