Search results for "amyloid beta-peptides"

showing 10 items of 131 documents

Increased blood mercury levels in patients with Alzheimer's disease.

1998

Alzheimer's disease (AD) is a common neurodegenerative disorder that leads to dementia and death. In addition to several genetic parameters, various environmental factors may influence the risk of getting AD. In order to test whether blood levels of the heavy metal mercury are increased in AD, we measured blood mercury concentrations in AD patients (n = 33), and compared them to age-matched control patients with major depression (MD) (n = 45), as well as to an additional control group of patients with various non-psychiatric disorders (n = 65). Blood mercury levels were more than two-fold higher in AD patients as compared to both control groups (p = 0.0005, and p = 0.0000, respectively). In…

Malemedicine.medical_specialtyPathologyNeurologychemistry.chemical_elementtau ProteinsCentral nervous system diseaseDegenerative diseaseAlzheimer DiseaseInternal medicineBlood plasmamedicineDementiaHumansBiological PsychiatryAgedAged 80 and overDepressive DisorderAmyloid beta-PeptidesNeurodegenerationMercuryMiddle Agedmedicine.diseaseMercury (element)Psychiatry and Mental healthEndocrinologyNeurologychemistryLinear ModelsFemaleNeurology (clinical)Alzheimer's diseasePsychologyBiomarkersJournal of neural transmission (Vienna, Austria : 1996)
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Cholesterol-Like Effects of Selective Cyclooxygenase Inhibitors and Fibrates on Cellular Membranes and Amyloid-β Production

2007

Strong evidence suggests a mechanistic link between cholesterol metabolism and the formation of amyloid-beta peptides, the principal constituents of senile plaques found in the brains of patients with Alzheimer's disease. Here, we show that several fibrates and diaryl heterocycle cyclooxygenase inhibitors, among them the commonly used drugs fenofibrate and celecoxib, exhibit effects similar to those of cholesterol on cellular membranes and amyloid precursor protein (APP) processing. These drugs have the same effects on membrane rigidity as cholesterol, monitored here by an increase in fluorescence anisotropy. The effect of the drugs on cellular membranes was also reflected in the inhibitory…

Membrane lipidsCHO CellsPharmacologyAmyloid beta-Protein PrecursorMicechemistry.chemical_compoundCricetulusFenofibrateCell Line TumorCricetinaeAmyloid precursor proteinmedicineMembrane fluidityAnimalsAspartic Acid EndopeptidasesCyclooxygenase InhibitorsClofibrateSenile plaquesPharmacologySulfonamidesAmyloid beta-PeptidesFenofibratebiologyCholesterolCell MembraneCholesterolMembranechemistryBiochemistryCelecoxibbiology.proteinPyrazolesMolecular MedicineCyclooxygenaseAmyloid Precursor Protein Secretasesmedicine.drugMolecular Pharmacology
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Astrocytes Protect Neurons from Aβ1-42 Peptide-Induced Neurotoxicity Increasing TFAM and PGC-1 and Decreasing PPAR-γ and SIRT-1

2015

One of the earliest neuropathological events in Alzheimer's disease is accumulation of astrocytes at sites of Aβ1-42 depositions. Our results indicate that Aβ1-42 toxic peptide increases lipid peroxidation, apoptosis and cell death in neurons but not in astrocytes in primary culture. Aβ1-42-induced deleterious neuronal effects are not present when neurons and astrocytes are mixed cultured. Stimulation of astrocytes with toxic Aβ1-42 peptide increased p-65 and decreased IκB resulting in inflammatory process. In astrocytes Aβ1-42 decreases protein expressions of sirtuin 1 (SIRT-1) and peroxisome proliferator-activated receptor γ (PPAR-γ) and over-expresses peroxisome proliferator-activated re…

MnSODProgrammed cell deathPPAR-γPeroxisome proliferator-activated receptorMitochondrionBiologyBioinformaticsmedicine.disease_causeAlzheimer's DiseaseNeurologiaPGC-1Sirtuin 1medicineAnimalsTFAMCells Culturedchemistry.chemical_classificationNeuronsAmyloid beta-PeptidesCell DeathSirtuin 1Caspase 3Superoxide DismutaseNeurotoxicityTranscription Factor RelAGeneral MedicineTFAMmedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaCoculture TechniquesPeptide FragmentsCell biologyMitochondriaPeroxidesRatsPPAR gammachemistryMitochondrial biogenesisNF-κB.Astrocytesbiology.proteinFisiologia humanaLipid PeroxidationOxidative stressResearch PaperTranscription FactorsInternational Journal of Medical Sciences
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High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

2020

AbstractDuring storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag. This tool e…

Models Molecular0301 basic medicineProtein domainBiophysicslcsh:MedicinePeptideBiosynthesis010402 general chemistryBiochemistry01 natural sciencesArticlelaw.invention03 medical and health sciencesProtein DomainslawAnimalsSpider silkAmino Acid SequenceNeurodegenerationlcsh:SciencePeptide sequencechemistry.chemical_classificationAmyloid beta-PeptidesMultidisciplinarybiologySpidroinlcsh:RNeurodegenerative diseasesNephila clavipesProteinsbiology.organism_classification0104 chemical sciences030104 developmental biologyBiochemistrychemistryYield (chemistry)Recombinant DNAlcsh:QPeptidesFibroinsScientific Reports
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Molecular topology as novel strategy for discovery of drugs with aβ lowering and anti-aggregation dual activities for Alzheimer's disease.

2014

Background and Purpose: In this study, we demonstrate the use of Molecular topology (MT) in an Alzheimer's disease (AD) drug discovery program. MT uses and expands upon the principles governing the molecular connectivity theory of numerically characterizing molecular structures, in the present case, active anti-AD drugs/agents, using topological descriptors to build models. Topological characterization has been shown to embody sufficient molecular information to provide strong correlation to therapeutic efficacy. Experimental Approach: We used MT to include multiple bioactive properties that allows for the identification of multifunctional single agent compounds, in this case, the dual func…

Models MolecularDrug Evaluation Preclinicallcsh:MedicineDiseaseProtein aggregationBioinformaticsBiochemistryMechanical Treatment of SpecimensAnimal CellsMolecular Cell BiologyDrug DiscoveryMedicine and Health Scienceslcsh:ScienceTopology (chemistry)NeuronsMultidisciplinaryDrug discoveryMedicine (all)Anti aggregationNeurodegenerative DiseasesAnimal ModelsElectroporationTreatment OutcomeNeurologySpecimen DisruptionDatabases as TopicFemaleMolecular topologyAlzheimer's diseaseCellular TypesResearch ArticleDrug Research and DevelopmentMouse ModelsMice TransgenicComputational biologyBiologyResearch and Analysis MethodsProtein AggregatesModel OrganismsAlzheimer DiseaseMental Health and PsychiatrymedicineAnimalsHumansPharmacologyAmyloid beta-PeptidesBiochemistry Genetics and Molecular Biology (all)lcsh:RBiology and Life SciencesProteinsComputational BiologyCell BiologyDUAL (cognitive architecture)medicine.diseaseDisease Models AnimalAgricultural and Biological Sciences (all)Specimen Preparation and TreatmentFeasibility StudiesDementialcsh:QClinical MedicineProtein MultimerizationPLoS ONE
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Beta-amyloid monomers are neuroprotective

2009

The 42-aa-long β-amyloid protein—Aβ1-42—is thought to play a central role in the pathogenesis of Alzheimer's disease (AD) (Walsh and Selkoe, 2007). Data from AD brain (Shankar et al., 2008), transgenic APP (amyloid precursor protein)-overexpressing mice (Lesné et al., 2006), and neuronal cultures treated with synthetic Aβ peptides (Lambert et al., 1998) indicate that self-association of Aβ1-42monomers into soluble oligomers is required for neurotoxicity. The function of monomeric Aβ1-42is unknown. The evidence that Aβ1-42is present in the brain and CSF of normal individuals suggests that the peptide is physiologically active (Shoji, 2002). Here we show that synthetic Aβ1-42monomers support …

N-MethylaspartateStimulationPeptideNeuroprotectionNeuro-degenerative diseasePathogenesismental disordersNitrilesmedicineAmyloid precursor proteinButadienesExcitatory Amino Acid AgonistsAnimalsEnzyme InhibitorsReceptorCells CulturedPodophyllotoxinchemistry.chemical_classificationCerebral CortexNeuronsAnalysis of VarianceAmyloid beta-PeptidesbiologyCell DeathDose-Response Relationship DrugGeneral NeuroscienceNeurodegenerationβ-Amyloid proteinNeurotoxicityself-assemblyTyrphostinsmedicine.diseaseEmbryo MammalianPeptide FragmentsCell biologyRatsNeuroprotective Agentschemistrybiology.proteinBrief CommunicationsNeuroscienceβ-Amyloid protein; Neuro-degenerative diseases; self-assembly
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From Small Peptides to Large Proteins against Alzheimer'sDisease.

2022

Alzheimer’s disease (AD) is the most common neurodegenerative disorder in the elderly. The two cardinal neuropathological hallmarks of AD are the senile plaques, which are extracellular deposits mainly constituted by beta-amyloids, and neurofibrillary tangles formed by abnormally phosphorylated Tau (p-Tau) located in the cytoplasm of neurons. Although the research has made relevant progress in the management of the disease, the treatment is still lacking. Only symptomatic medications exist for the disease, and, in the meantime, laboratories worldwide are investigating disease-modifying treatments for AD. In the present review, results centered on the use of peptides of different sizes invol…

NeuronsAmyloid beta-Peptidesamyloid-beta protein: amyloid fibrillationAlzheimer DiseaseTau proteinHumanstau ProteinsPlaque AmyloidNeurofibrillary TanglesMolecular BiologyBiochemistryAlzheimer’s diseaseAgedBiomolecules
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Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease

2015

Neurofibrillary tangles (aggregates of cytoskeletal Tau protein) and senile plaques (aggregates mainly formed by amyloid β peptide) are two landmark lesions in Alzheimer׳s disease. Some researchers have proposed tangles, whereas others have proposed plaques, as primary lesions. For a long time, these were thought of as independent mechanisms. However, experimental evidence suggests that both lesions are intimately related. We review here some molecular pathways linking amyloid β and Tau toxicities involving, among others, glycogen synthase kinase 3β, p38, Pin1, cyclin-dependent kinase 5, and regulator of calcineurin 1. Understanding amyloid β and Tau toxicities as part of a common pathophys…

Pathologymedicine.medical_specialtyAmyloid beta-PeptidesbiologyChemistryKinaseNeurodegenerationTau proteinBACE1-AStau Proteinsmedicine.diseaseProtein Aggregation PathologicalBiochemistryBiochemistry of Alzheimer's diseaseAlzheimer DiseaseGSK-3Physiology (medical)mental disordersmedicinebiology.proteinCancer researchPIN1HumansSenile plaquesPhosphorylationFree Radical Biology and Medicine
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Protection of Flupirtine on β-Amyloid-Induced Apoptosis in Neuronal Cells In Vitro: Prevention of Amyloid-Induced Glutathione Depletion

2002

Effective drugs are not available to protect against beta-amyloid peptide (A beta)-induced neurotoxicity. Cortical neurons from rat embryos were treated with the toxic fragment A beta25-35 at 1 microM in the presence or absence of flupirtine, a triaminopyridine, successfully applied clinically as a nonopiate analgesic drug. Five days later 1 microM A beta25-35 caused reduction of cell viability to 31.1%. Preincubation of cells with flupirtine (1 or 5 microg/ml) resulted in a significant increase of the percentage of viable cells (74.6 and 65.4%, respectively). During incubation with A beta25-35 the neurons undergo apoptosis as determined by appearance of the characteristic stepladder-like D…

Pathologymedicine.medical_specialtyCell SurvivalAminopyridinesApoptosisPharmacologymedicine.disease_causeBiochemistryAntioxidantsCellular and Molecular NeurosciencemedicineAnimalsViability assaySenile plaquesRats WistarCerebral CortexNeuronsAmyloid beta-PeptidesChemistryNeurotoxicitymedicine.diseaseGlutathionePeptide FragmentsRatsOxidative StressNeuroprotective AgentsApoptosisCell cultureDNA fragmentationFlupirtineOxidative stressmedicine.drugJournal of Neurochemistry
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The unsolved relationship of brain aging and late-onset Alzheimer disease.

2009

Late-onset Alzheimer disease is the most common form of dementia and is strongly associated with age. Today, around 24 million people suffer from dementia and with aging of industrial populations this number will significantly increase throughout the next decades. An effective therapy that successfully decelerates or prevents the progressive neurodegeneration does not exist. Histopathologically Alzheimer disease is characterized by extensive extracellular amyloid beta (Abeta) plaques, intracellular neurofibrillary tangles (NFTs), synaptic loss and neuronal cell death in distinct brain regions. The molecular correlation of Abeta or NFTs and development of late-onset Alzheimer disease needs f…

Programmed cell deathAgingAmyloid βFree RadicalsBiophysicsmedicine.disease_causeBiochemistryModels BiologicalAtrophyAlzheimer DiseasemedicineExtracellularDementiaAnimalsHumansMolecular BiologyAmyloid beta-Peptidesbusiness.industryBrainNeurodegenerative Diseasesmedicine.diseaseDementiaAlzheimer's diseasebusinessNeuroscienceOxidative stressIntracellularBiochimica et biophysica acta
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