Search results for "AMyloid"

showing 10 items of 494 documents

Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism.

2005

Deposition of the amyloid beta-protein (Abeta) in senile or diffuse plaques is a distinctive feature of Alzheimer's disease. The role of Abeta aggregates in the etiology of the disease is still controversial. The formation of linear aggregates, known as amyloid fibrils, has been proposed as the onset and the cause of pathological deposition. Yet, recent findings suggest that a more crucial role is played by prefibrillar oligomeric assemblies of Abeta that are highly toxic in the extracellular environment. In the present work, the mechanism of protofibril formation is studied at pH 3.1, starting from a solution of oligomeric precursors. By combining static light scattering and photon correla…

Conformational changeTime FactorsAmyloidLightNucleationBiophysicsBiochemistryBiophysical PhenomenaDiffusionDynamic light scatteringAlzheimer DiseaseExtracellularHumansScattering RadiationStatic light scatteringMolecular BiologyCoalescence (physics)PhotonsAmyloid beta-PeptidesModels StatisticalDose-Response Relationship DrugChemistryTemperatureCell BiologyHydrogen-Ion ConcentrationModels TheoreticalCrystallographyKineticsSpectrophotometryBiophysicsThermodynamicsElongationPeptidesProtein BindingThe Journal of biological chemistry
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FERULIC ACID INHIBITS OXIDATE STRESS AND CELL DEATH INDUCED BY Ab OLIGOMERS: IMPROVED DELIVERY BY SOLID LIPID NANOPARTICLES.

2009

Oxidative stress and dysfunctional mitochondria are among the earliest events in AD, triggering neurodegeneration. The use of natural antioxidants could be a neuroprotective strategy for blocking cell death. Here, the antioxidant action of ferulic acid (FA) on different paths leading to degeneration of recombinant beta-amyloid peptide (rAbeta42) treated cells was investigated. Further, to improve its delivery, a novel drug delivery system (DDS) was used. Solid lipid nanoparticles (SLNs), empty or containing ferulic acid (FA-SNL), were developed as DDS. The resulting particles had small colloidal size and highly negative surface charge in water. Using neuroblastoma cells and rAbeta42 oligome…

Coumaric AcidsMitochondrionmedicine.disease_causeBiochemistryAntioxidantsFerulic acidchemistry.chemical_compoundAlzheimer DiseaseCell Line TumorSolid lipid nanoparticlemedicineHumansViability assayMembrane Potential MitochondrialNeuronsAmyloid beta-PeptidesCell DeathbiologyCytochrome cCytochromes cFERULIC ACID Ab OLIGOMERS LIPID NANOPARTICLES DELIVERY SYSTEM.General MedicineLipidsPeptide FragmentsRecombinant ProteinsMitochondriaOxidative StressBiochemistrychemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoDrug deliveryBiophysicsbiology.proteinNanoparticlesPeroxiredoxinOxidative stress
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Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease

2009

Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry ass…

CrystallinCircular dichroismAmyloidCarnosinePeptideMicroscopy Atomic ForceBiochemistryCataractLens proteinRats Sprague-Dawleychemistry.chemical_compoundOrgan Culture TechniquesCrystallinChaperone activityAnimalsalpha-CrystallinsSFM Scanning Force Microscopychemistry.chemical_classificationDipeptideCD Circular DichroismThT Thioflavin TCalorimetry Differential ScanningDSC Differential Scanning CalorimetryCircular DichroismCarnosineStereoisomerismIn vitroeye diseasesRatsSpectrometry FluorescencechemistryBiochemistryHEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidThioflavinCattleFemaleSpectrophotometry Ultravioletsense organsAmyloid fibrilMolecular Chaperones
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Curcumin-derived pyrazoles and isoxazoles: Swiss army knives or blunt tools for Alzheimer's disease?

2007

Curcumin binds to the amyloid beta peptide (Abeta) and inhibits or modulates amyloid precursor protein (APP) metabolism. Therefore, curcumin-derived isoxazoles and pyrazoles were synthesized to minimize the metal chelation properties of curcumin. The decreased rotational freedom and absence of stereoisomers was predicted to enhance affinity toward Abeta(42) aggregates. Accordingly, replacement of the 1,3-dicarbonyl moiety with isosteric heterocycles turned curcumin analogue isoxazoles and pyrazoles into potent ligands of fibrillar Abeta(42) aggregates. Additionally, several compounds are potent inhibitors of tau protein aggregation and depolymerized tau protein aggregates at low micromolar …

CurcuminMagnetic Resonance SpectroscopyAmyloid betaStereochemistryTau proteinPeptidetau ProteinsBiochemistrychemistry.chemical_compoundInhibitory Concentration 50Radioligand AssayAlzheimer Diseasemental disordersDrug DiscoveryAmyloid precursor proteinFluorescence Resonance Energy TransferMoietyAnimalsHumansGeneral Pharmacology Toxicology and PharmaceuticsEnzyme InhibitorsCells CulturedCell ProliferationPharmacologychemistry.chemical_classificationAmyloid beta-PeptidesbiologyOrganic ChemistryP3 peptideIsoxazolesBiochemistrychemistrybiology.proteinCurcuminMolecular MedicinePyrazolesAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseChickensChemMedChem
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Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins.

2001

The L1 adhesion molecule plays an important role in axon guidance and cell migration in the nervous system. L1 is also expressed by many human carcinomas. In addition to cell surface expression, the L1 ectodomain can be released by a metalloproteinase, but the biological function of this process is unknown. Here we demonstrate that membrane-proximal cleavage of L1 can be detected in tumors and in the developing mouse brain. The shedding of L1 involved a disintegrin and metalloproteinase (ADAM)10, as transfection with dominant-negative ADAM10 completely abolishes L1 release. L1-transfected CHO cells (L1-CHO) showed enhanced haptotactic migration on fibronectin and laminin, which was blocked …

CytoplasmIntegrinsL1; shedding; ADAM10; cell migration; integrinsADAM10IntegrinGene ExpressionCHO CellsBiologyArticle03 medical and health sciencesParacrine signallingMice0302 clinical medicineCell MovementCricetinaeEndopeptidasesTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansReceptors VitronectinFibrinolysinNeural Cell Adhesion Molecules030304 developmental biology0303 health sciencesBinding SitesMembrane GlycoproteinsCell adhesion moleculeCell MembraneAntibodies MonoclonalBrainCell migrationBiological TransportCell BiologyMolecular biologyPeptide FragmentsCell biologyFibronectinAutocrine CommunicationEctodomainSolubility030220 oncology & carcinogenesisbiology.proteinNeural cell adhesion moleculeAmyloid Precursor Protein SecretasesLeukocyte L1 Antigen ComplexOligopeptidesThe Journal of cell biology
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Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein

2005

Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved in APP endocytosis. Here, we show that the APP homolog APLP1 (amyloid precursor-like protein 1) influences APP shedding. In human embryonic kidney 293 cells expression of APLP1 strongly activated APP shedding by alpha-secretase and slightly reduced beta-secretase cleavage. As revealed by domain deletion analysis, the increase in APP shedding re…

CytoplasmTime FactorsRecombinant Fusion ProteinsAmino Acid MotifsBlotting WesternGenetic VectorsEndocytic cycleCHO CellsTransfectionEndocytosisBiochemistryCell LineAmyloid beta-Protein PrecursorGenes ReporterCricetinaeChlorocebus aethiopsEndopeptidasesmental disordersAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansImmunoprecipitationAPLP1Molecular BiologyModels GeneticbiologyChemistryHEK 293 cellsP3 peptideCell BiologyEndocytosisProtein Structure TertiaryMicroscopy FluorescenceBiochemistryAlpha secretaseEctodomainCOS Cellsbiology.proteinAmyloid Precursor Protein SecretasesPeptidesGene DeletionPlasmidsJournal of Biological Chemistry
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The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity

2005

The cellular prion protein (PrP(c)) is physiologically cleaved in the middle of its 106-126 amino acid neurotoxic region at the 110/111 downward arrow112 peptidyl bond, yielding an N-terminal fragment referred to as N1. We recently demonstrated that two disintegrins, namely ADAM10 and ADAM17 (TACE, tumor necrosis factor alpha converting enzyme) participated in both constitutive and protein kinase C-regulated generation of N1, respectively. These proteolytic events were strikingly reminiscent of those involved in the so-called "alpha-secretase pathway" that leads to the production of secreted sAPPalpha from betaAPP. We show here, by transient and stable transfection analyses, that ADAM9 also…

DNA ComplementaryADAM10Gene ExpressionTransfectionBiochemistryDNA AntisenseCell LineAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansPrPC Proteins[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein kinase AMolecular Biology030304 developmental biologyMice Knockout0303 health sciencesbiologyHEK 293 cells030302 biochemistry & molecular biologyMembrane ProteinsTransfectionCell BiologyFibroblastsPeptide FragmentsADAM ProteinsBiochemistryCell culturebiology.proteinAdditions and CorrectionsAmyloid Precursor Protein SecretasesADAM9Amyloid precursor protein secretase030217 neurology & neurosurgery
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Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulat…

2003

Tumor necrosis factor-alpha converting enzyme (TACE or ADAM17) is a member of the ADAM (a disintegrin and metalloproteinase) family of type I membrane proteins and mediates the ectodomain shedding of various membrane-anchored signaling and adhesion proteins. TACE is synthesized as an inactive zymogen, which is subsequently proteolytically processed to the catalytically active form. We have identified the proprotein-convertases PC7 and furin to be involved in maturation of TACE. This maturation is negatively influenced by the phorbol ester phorbol-12-myristate-13-acetate (PMA), which decreases the cellular amount of the mature form of TACE in PMA-treated HEK293 and SH-SY5Y cells. Furthermore…

DNA ComplementaryTime FactorsADAM10Blotting WesternGenetic VectorsADAM17 ProteinTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorAlzheimer DiseaseZymogenEndopeptidasesPhorbol EstersCell AdhesionTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein kinase A signalingFurinProtein Kinase CProtein kinase CFurinMetalloproteinasebiologyChemistryMetalloendopeptidasesCyclic AMP-Dependent Protein KinasesPeptide FragmentsRatsCell biologyADAM ProteinsEctodomainBiochemistrybiology.proteinTetradecanoylphorbol AcetateCattleTumor necrosis factor alphaProprotein ConvertasesAmyloid Precursor Protein SecretasesSignal TransductionEuropean Journal of Biochemistry
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Diabetes and cognitive decline

2022

Epidemiologic studies have documented an association between diabetes and increased risk of cognitive decline in the elderly. Based on animal model studies, several mechanisms have been proposed to explain such an association, including central insulin signaling, neurodegeneration, brain amyloidosis, and neuroinflammation. Nevertheless, the exact mechanisms in humans remain poorly defined. It is reasonable, however, that many pathways may be involved in these patients leading to cognitive impairment. A major aim of clinicians is identifying early onset of neurologic signs and symptoms in elderly diabetics to improve quality of life of those with cognitive impairment and reduce costs associa…

Diabetes mellituAmyloid beta-Peptidestau ProteinsAmyloid beta-peptideBiomarkerAmyloidosisVascular dementiaSettore BIO/12 - Biochimica Clinica E Biologia Molecolare ClinicaDiabetes mellitusGlycated hemoglobinSettore MED/13Alzheimer DiseaseTau proteinQuality of LifeBlood glucoseHumansDementiaCognitive DysfunctionBiomarkersRisk assessmentAged
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Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation

2019

Oxidation of amino acid side chains in protein structure can be induced by UV irradiation leading to critical changes in molecular structure possibly modifying protein stability and bioactivity. Here we show, by using a combination of multiple spectroscopic techniques and Fluorescence Lifetime Imaging, that UV-light exposure induces irreversible oxidation processes in Ubiquitin structure. In particular, the growth of a new autofluorescence peak in the blue region is detected, that we attribute to tyrosine oxidation products. Blue autofluorescence intensity is found to progressively increase also during aggregation processes leading to the formation of aggregates of non-amyloid nature. Signi…

Dityrosine formation0301 basic medicineAmyloidUltraviolet RaysBiophysicsPeptideProtein aggregationAmyloid autofluorescence; Dityrosine formation; Fluorescence lifetime imaging; Oxidative stress; UbiquitinFluorescence lifetime imagingBiochemistryFluorescenceAnalytical ChemistryProtein Aggregates03 medical and health sciences0302 clinical medicineProtein structureHumansTyrosineMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesUbiquitinChemistryFluorescenceAmino acidAutofluorescence030104 developmental biologyBiophysicsOxidative streAmyloid autofluorescenceOxidation-Reduction030217 neurology & neurosurgeryBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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