Search results for "Amyloid β"

showing 10 items of 11 documents

Amyloid in Alzheimer’s Disease: Guilty Beyond Reasonable Doubt?

2017

Recently failed antiamyloidogenic trials call for an objective reassessment of the dominating amyloid cascade hypothesis of Alzheimer's disease (AD). Ongoing efforts focusing on amyloid β protein (Aβ), its deposition, and its removal need to be complemented by more intensive research in new directions. Those may either integrate amyloid pathology or will propose pathogenetic routes independent of Aβ in the search for the causes of AD.

0301 basic medicinePharmacologyAmyloidReasonable doubtAmyloid pathologyAmyloidAmyloid βDiseaseToxicology03 medical and health sciences030104 developmental biology0302 clinical medicineAlzheimer DiseaseAnimalsHumansAmyloid cascadePsychologyNeuroscience030217 neurology & neurosurgeryTrends in Pharmacological Sciences
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Tryptophan-Containing Dual Neuroprotective Peptides: Prolyl Endopeptidase Inhibition and Caenorhabditis elegans Protection from β-Amyloid Peptide Tox…

2018

Neuroprotective peptides represent an attractive pharmacological strategy for the prevention or treatment of age-related diseases, for which there are currently few effective therapies. Lactoferrin (LF)-derived peptides (PKHs) and a set of six rationally-designed tryptophan (W)-containing heptapeptides (PACEIs) were characterized as prolyl endopeptidase (PEP) inhibitors, and their effect on β-amyloid peptide (Aβ) toxicity in a Caenorhabditis elegans model of Alzheimer’s disease (AD) was evaluated. Two LF-derived sequences, PKH8 and PKH11, sharing a W at the C-terminal end, and the six PACEI heptapeptides (PACEI48L to PACEI53L) exhibited significant in vitro PEP inhibition. The inhibitory pe…

0301 basic medicineprolyl endopeptidase inhibitionPeptidelactoferrin-derived peptidesPharmacologyNeuroprotectionCatalysislcsh:ChemistryInorganic Chemistry03 medical and health sciencesneurodegenerative diseases; amyloid β peptide; <i>Caenorhabditis elegans</i>; prolyl endopeptidase inhibition; lactoferrin-derived peptides; rationally-designed peptides; tryptophan; molecular docking0302 clinical medicineProlyl endopeptidaseIn vivomedicineneurodegenerative diseasestryptophanPhysical and Theoretical ChemistryCaenorhabditis eleganslcsh:QH301-705.5Molecular BiologySpectroscopyCaenorhabditis elegansamyloid β peptidechemistry.chemical_classificationbiologyOrganic ChemistryTryptophanmolecular dockingGeneral Medicinebiology.organism_classificationIn vitroComputer Science Applications030104 developmental biologylcsh:Biology (General)lcsh:QD1-999chemistryrationally-designed peptidesToxicity030217 neurology & neurosurgerymedicine.drugInternational Journal of Molecular Sciences; Volume 19; Issue 5; Pages: 1491
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Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier

2012

The blood—brain barrier (BBB) facilitates amyloid-β (Aβ) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating Aβ neurotoxicity in Alzheimer's disease (AD), participates in Aβ transcytosis across the BBB. Using an in vitro BBB model, [125I]-Aβ1–40 transcytosis was reduced by genetic knockout of PrPc or after addition of a competing PrPc-specific antibody. Furthermore, we provide evidence that PrPc is expressed in endothelial cells and, that monomeric Aβ1–40 binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD.

Amyloid βanimal diseasesBiologyBrief CommunicationBlood–brain barrierModels BiologicalMiceAlzheimer Diseasemental disordersmedicineAnimalsPrPC ProteinsPrion proteinReceptorCells CulturedAmyloid beta-PeptidesNeurotoxicitymedicine.diseaseMolecular biologyPeptide FragmentsIn vitronervous system diseasesCell biologymedicine.anatomical_structureNeurologyTranscytosisBlood-Brain BarrierGene Knockdown Techniquesbiology.proteinNeurology (clinical)AntibodyTranscytosisCardiology and Cardiovascular MedicineProtein BindingJournal of Cerebral Blood Flow &amp; Metabolism
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The use of Stokes-Mueller polarimetry for assessment of amyloid-β progression in a mouse model of Alzheimer’s disease

2020

Abstract Alzheimer’s disease, being a major societal burden, demands improvement of current techniques for its treatment and diagnostics. Currently only autopsy histology is able to provide the definite diagnosis for Alzheimer’s disease. However, the procedure is rather time consuming and costly. In the current study, we utilized Stokes and Mueller polarimetry techniques to screen for amyloid-β (Aβ) deposits in formalin-fixed, paraffin-embedded mouse brain tissue at different stages of Alzheimer’s disease. The study has shown that the presence of Aβ plaques influences the properties of scattered polarized light. The Poincaré sphere was used as a graphical tool for the visualization of the a…

Amyloid βbrainPolarimetryDiseaselight scatteringScattering03 medical and health sciencessymbols.namesake0302 clinical medicinestatistical analysisScreening methodStokes parameterstissuesComputingMilieux_MISCELLANEOUS030304 developmental biologyPoincare spherepolarimetryPhysics0303 health sciencespolarizationDisease progressionDepolarizationAlzheimer's diseaseAlzheimer's[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsStatistical analysisAmyloid-ß plaque[SPI.OPTI]Engineering Sciences [physics]/Optics / PhotonicsymbolsAnisotropyDepolarizationNeuroscience030217 neurology & neurosurgeryOptical Biopsy XVIII: Toward Real-Time Spectroscopic Imaging and Diagnosis
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Detection of Amyloid-β Fibrils Using Track-Etched Nanopores: Effect of Geometry and Crowding

2021

Several neurodegenerative diseases have been linked to proteins or peptides that are prone to aggregate in different brain regions. Aggregation of amyloid-β (Aβ) peptides is recognized as the main cause of Alzheimer's disease (AD) progression, leading to the formation of toxic Aβ oligomers and amyloid fibrils. The molecular mechanism of Aβ aggregation is complex and still not fully understood. Nanopore technology provides a new way to obtain kinetic and morphological aspects of Aβ aggregation at a single-molecule scale without labeling by detecting the electrochemical signal of the peptides when they pass through the hole. Here, we investigate the influence of nanoscale geometry (conical an…

AmyloidAmyloidAmyloid βSonicationBioengineeringGeometrymacromolecular substances02 engineering and technologyPolyethylene glycol010402 general chemistryFibril01 natural sciencesNanoporeschemistry.chemical_compoundAlzheimer DiseasePEG ratioHumansInstrumentationNanoscopic scaleFluid Flow and Transfer ProcessesAmyloid beta-PeptidesChemistryProcess Chemistry and Technology021001 nanoscience & nanotechnology0104 chemical sciencesKineticsNanopore0210 nano-technologyACS Sensors
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Gamma-secretase modulation with Abeta42-lowering nonsteroidal anti-inflammatory drugs and derived compounds.

2006

The amyloid-beta (Abeta) peptides and specifically the highly amyloidogenic isoform Abeta42 appear to be key agents in the pathogenesis of familial and sporadic forms of Alzheimer's disease (AD). The final step in the generation of Abeta from the amyloid precursor protein is catalyzed by the multiprotein complex gamma-secretase, which constitutes a prime drug target for prevention and therapy of the disease. However, highly potent gamma-secretase inhibitors that block formation of all Abeta peptides have provoked troubling side effects in preclinical animal models of AD. This toxicity can be readily explained by the promiscuous substrate specificity of gamma-secretase and its essential role…

Gene isoformendocrine systemClinical Trials as TopicNonsteroidalAmyloid beta-Peptidesmedicine.drug_classAnti-Inflammatory Agents Non-SteroidalPharmacologyIbuprofenAmyloid β peptideAnti-inflammatoryPathogenesischemistry.chemical_compoundNeurologychemistryAlzheimer DiseasemedicineAnimalsHumansNeurology (clinical)γ secretaseAmyloid Precursor Protein SecretasesGamma secretasemedicine.drugNeuro-degenerative diseases
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Neuronal activity and secreted amyloid β lead to altered amyloid β precursor protein and presenilin 1 interactions.

2013

Deposition of amyloid β (Aβ) containing plaques in the brain is one of the neuropathological hallmarks of Alzheimer's disease (AD). It has been suggested that modulation of neuronal activity may alter Aβ production in the brain. We postulate that these changes in Aβ production are due to changes in the rate-limiting step of Aβ generation, APP cleavage by γ-secretase. By combining biochemical approaches with fluorescence lifetime imaging microscopy, we found that neuronal inhibition decreases endogenous APP and PS1 interactions, which correlates with reduced Aβ production. By contrast, neuronal activation had a two-phase effect: it initially enhanced APP-PS1 interaction leading to increased …

ImmunoprecipitationBlotting WesternEndogenyMice TransgenicCleavage (embryo)PresenilinArticlelcsh:RC321-571Amyloid beta-Protein PrecursorMiceAlzheimer Diseasemental disordersmedicinePresenilin-1Premovement neuronal activityAnimalsHumansImmunoprecipitationlcsh:Neurosciences. Biological psychiatry. NeuropsychiatryFeedback PhysiologicalNeuronsPresenilin 1Neuronal activityAmyloid beta-PeptidesChemistryP3 peptideNeurotoxicityAlzheimer's diseasemedicine.diseaseImmunohistochemistryCell biologyNeurologyBiochemistrynervous systemAlzheimer's diseaseAmyloid β precursor proteinFLIM (fluorescence lifetime imaging microscopy)Neurobiology of disease
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A New Tool for the Analysis of the Effect of Intracerebrally Injected Anti-Amyloid-β Compounds

2021

Background: A wide range of techniques has been developed over the past decades to characterize amyloid-β (Aβ) pathology in mice. Until now, no method has been established to quantify spatial changes in Aβ plaque deposition due to targeted delivery of substances using ALZET® pumps. Objective: Development of a methodology to quantify the local distribution of Aβ plaques after intracerebral infusion of compounds. Methods: We have developed a toolbox to quantify Aβ plaques in relation to intracerebral injection channels using Zeiss AxioVision® and Microsoft Excel® software. For the proof of concept, intracerebral stereotactic surgery was performed in 50-day-old APP-transgenic mice injected wit…

Intracerebral injectionAmyloid βMice TransgenicPlaque Amyloidamyloid-βtransgenic miceStereotaxic TechniqueshistologyMiceAlzheimer DiseaseAnimalsHumansDistribution (pharmacology)implantable infusion pumpdistributional activityAmyloid beta-PeptidesChemistryGeneral NeuroscienceBrainGeneral MedicineImmunohistochemistryplaquesAβ depositionquantificationDisease Models AnimalPsychiatry and Mental healthClinical PsychologyGeriatrics and GerontologyAlzheimer’s diseaseResearch ArticleBiomedical engineeringJournal of Alzheimer's Disease
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Impact of Resilience on the Association Between Amyloid-β and Longitudinal Cognitive Decline in Cognitively Healthy Older Adults

2019

The present study aims at investigating if the association between amyloid-β and longitudinal cognitive decline in cognitively healthy elderly is modulated by resilience capacity. Resilience capacity was quantified by education, which is a common proxy of resilience and has been shown to be related to a wide range of behaviors promoting resilience. Analyses were conducted with longitudinal cognitive data from the Alzheimer's Disease Neuroimaging Initiative (ADNI). 276 cognitively healthy older individuals (≥56 years) were included in the study. Baseline amyloid pathology was quantified using CSF amyloid-β 1-42 measurements. Longitudinal cognitive decline was assessed using ADAS13, Clinical …

Male0301 basic medicineGerontologyAmyloid pathologyAmyloid βClinical Dementia RatingDiseaseNeuropsychological Tests03 medical and health sciences0302 clinical medicineNeuroimagingAlzheimer Diseasemental disordersHumansMedicineCognitive DysfunctionLongitudinal StudiesCognitive declineAgedAged 80 and overAmyloid beta-Peptidesbusiness.industryGeneral NeuroscienceCognitionGeneral MedicineMiddle AgedResilience PsychologicalPeptide FragmentsPsychiatry and Mental healthClinical Psychology030104 developmental biologyMixed effectsFemaleGeriatrics and GerontologybusinessBiomarkers030217 neurology & neurosurgeryFollow-Up StudiesJournal of Alzheimer's Disease
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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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