Search results for "AMYLOID"

showing 10 items of 494 documents

Aβ Oligomers and Fibrillar Aggregates Induce Different Apoptotic Pathways in LAN5 Neuroblastoma Cell Cultures

2009

Fibril deposit formation of amyloid beta-protein (Abeta) in the brain is a hallmark of Alzheimer's disease (AD). Increasing evidence suggests that toxicity is linked to diffusible Abeta oligomers, which have been found in soluble brain extracts of AD patients, rather than to insoluble fibers. Here we report a study of the toxicity of two distinct forms of recombinant Abeta small oligomers and fibrillar aggregates to simulate the action of diffusible Abeta oligomers and amyloid plaques on neuronal cells. Different techniques, including dynamic light scattering, fluorescence, and scanning electron microscopy, have been used to characterize the two forms of Abeta. Under similar conditions and …

Time FactorsAmyloidCell SurvivalBiophysicsApoptosisBiologyFibrilCaspase 8Substrate SpecificityNeuroblastomaCytosolCell Line TumormedicineHumansEnzyme InhibitorsProtein Structure QuaternaryCaspase-9Amyloid beta-PeptidesDose-Response Relationship DrugProteinCytochrome cNeurodegenerationCytochromes cHydrogen-Ion Concentrationmedicine.diseaseCaspase InhibitorsPeptide FragmentsCell biologyProtein TransportCytosolApoptosisMicroscopy Electron Scanningbiology.proteinProtein MultimerizationProtein BindingSignal TransductionBiophysical Journal
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Fluctuation Methods To Study Protein Aggregation in Live Cells: Concanavalin A Oligomers Formation

2011

Prefibrillar oligomers of proteins are suspected to be the primary pathogenic agents in several neurodegenerative diseases. A key approach for elucidating the pathogenic mechanisms is to probe the existence of oligomers directly in living cells. In this work, we were able to monitor the process of aggregation of Concanavalin A in live cells. We used number and brightness analysis, two-color cross number and brightness analysis, and Raster image correlation spectroscopy to obtain the number of molecules, aggregation state, and diffusion coefficient as a function of time and cell location. We observed that binding of Concanavalin A to the membrane and the formation of small aggregates paralle…

Time FactorsCell SurvivalCellSpectroscopy Imaging and Other TechniquesBiophysicsProtein aggregationCell morphologyCell membraneDiffusion03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineProtein structure2-NaphthylaminemedicineConcanavalin AAnimalsconfocal microscopy super resolution protein aggregation kinetics in live cells amyloid related pathologiesAnnexin A5Protein Structure QuaternaryCell Shape030304 developmental biology0303 health sciencesbiologySpectrum AnalysisCell MembraneFibroblastsEmbryo MammalianCell biologyMembranemedicine.anatomical_structurechemistryConcanavalin Abiology.proteinLaurdan030217 neurology & neurosurgeryFluorescein-5-isothiocyanateLaurates
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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009

The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coinci…

Time FactorsLipid BilayersMolecular Sequence DataBiophysicsPeptideFluorescence Polarization7. Clean energy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseErgosterolFluorescence Resonance Energy TransferAmino Acid SequenceLipid bilayer030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeAmyloid beta-PeptidesChemistryCholesterolSterolPeptide FragmentsCrystallographyFörster resonance energy transferMembraneCholesterolCell BiophysicsTyrosinelipids (amino acids peptides and proteins)030217 neurology & neurosurgeryFluorescence anisotropyProtein BindingBiophysical Journal
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α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Heterogeneity of aggregates in the fibrillation mechanisms of proteins probed by time resolved fluorescence

2010

Under appropriate conditions almost all proteins are able to aggregate to form long, well-ordered and beta-sheet rich arrays known as amyloid fibrils. The formation of such structures involves complex intra and intermolecular interactions modulated by the structure and dynamics of the native protein, and by the physico-chemical properties of the solvent. Multiple interactions and cross-feedback during the aggregation pathway cause different ultimate aggregates’ morphologies and the possible simultaneous occurrence of multiple species. The structural definition of such assemblies is complicated by the polymorphism of the amyloid fibrils. Aim of this study is to inquire on the different natur…

Time resolved fluorescenceprotein aggregation amyloid fibrilSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Increased AICD generation does not result in increased nuclear translocation or activation of target gene transcription.

2008

A sequence of amyloid precursor protein (APP) cleavages culminates in the sequential release of the APP intracellular domain (AICD) and the amyloid beta peptide (Abeta) and/or p3 fragment. One of the environmental factors favouring the accumulation of AICD appears to be a rise in intracellular pH. Here we further identified the metabolism and subcellular localization of artificially expressed constructs under such conditions. We also co-examined the mechanistic lead up to the AICD accumulation and explored possible significances for its increased expression. We found that most of the AICD generated under pH neutralized conditions is likely cleaved from C83. While the AICD surplus was unable…

Transcriptional ActivationTranscription GeneticAmyloid betaActive Transport Cell NucleusCHO CellsModels BiologicalTransactivationAmyloid beta-Protein PrecursorCricetulusTranscription (biology)CricetinaeAmyloid precursor proteinAnimalsHumansLuciferaseCells CulturedRegulation of gene expressionCell NucleusbiologyCell BiologyHydrogen-Ion ConcentrationSubcellular localizationMolecular biologyCell biologyProtein Structure TertiaryCytosolbiology.proteinProtein Processing Post-TranslationalProtein BindingExperimental cell research
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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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Clinical symptomatic de novo systemic transthyretin amyloidosis 9 years after domino liver transplantation

2009

Four years ago, Stangou et al. reported a patient who developed clinical symptoms of amyloidosis 8 years after domino liver transplantation (DLT). In order to alleviate the graft shortage, livers from patients with familial amyloidotic polyneuropathy (FAP) are used as domino grafts for other patients under the assumption that several decades will pass before clinical symptoms due to amyloid accumulation emerge. We now report on another case, the third reported case in the literature, of de novo systemic amyloidosis in a 75-year-old woman 9 years after DLT. The patient underwent DLT at 65 years of age for hepatocellular carcinoma exceeding the Milan criteria in hepatitis C cirrhosis. Transar…

Transplantationmedicine.medical_specialtyPathologyCirrhosisDysesthesiaHepatologybusiness.industrymedicine.medical_treatmentAmyloidosisHepatitis CLiver transplantationMilan criteriamedicine.diseaseSurgeryB symptomsMedicineSurgerymedicine.symptombusinessPolyneuropathyLiver Transplantation
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Progression of transthyretin (TTR) amyloidosis in donors and recipients after domino liver transplantation-a prospective single-center cohort study

2018

Liver transplantation (LT) is the first-line therapy in patients with transthyretin (TTR) amyloidosis and progressive familial amyloid polyneuropathy (FAP). Explanted organs from these patients can be used for domino liver transplantation (DLT). After DLT, de novo amyloidosis may develop in domino recipients (DR). Data were collected prospectively in a transplant database. Electroneurography by nerve conduction velocity (NCV), quantitative sensory testing, heart rate variability (HRV), sympathetic skin response, orthostatic reaction (tilt table test), transthoracic echocardiography, cardiac MRI and organ biopsy results were evaluated. The cohort included 24 FAP- (11 Val30Met, 13 nonVal30Met…

Transplantationmedicine.medical_specialtybiologymedicine.diagnostic_testbusiness.industrymedicine.medical_treatmentAmyloidosis030204 cardiovascular system & hematologyLiver transplantationmedicine.diseaseSingle CenterGastroenterology03 medical and health sciencesTransthyretinTilt table test0302 clinical medicineInternal medicineCohortBiopsybiology.proteinMedicinebusiness030217 neurology & neurosurgeryCohort studyTransplant International
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Modulation of α-Synuclein Aggregation Process and Fibril Stability by Co-solvents

2014

Amyloid fibrils are involved in several amyloid-related pathologies such as Parkinson's disease, Alzheimer's disease and type II diabetes. As a result, scientific community is nowadays addressing considerable efforts towards the comprehension of fibrillation mechanisms, particularly focusing on how they are affected by environmental conditions, small molecules and/or membrane presence. In this scenario, alpha-synuclein (aSN), a small protein involved in Parkinson's disease, represents a challenging model system for studying aggregation phenomena, and understanding the pathogenesis at molecular level. Indeed, it is poorly understood how fibril formation is linked to the progressive neurodege…

TrifluoroethanolAmyloid fibrilSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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