Search results for "Amyloid"

showing 10 items of 494 documents

Techniques to Analyze sRNA Protein Cofactor Self-Assembly In Vitro

2018

Post-transcriptional control of gene expression by small regulatory noncoding RNA (sRNA) needs protein accomplices to occur. Past research mainly focused on the RNA chaperone Hfq as cofactor. Nevertheless, recent studies indicated that other proteins might be involved in sRNA-based regulations. As some of these proteins have been shown to self-assemble, we describe in this chapter protocols to analyze the nano-assemblies formed. Precisely, we focus our analysis on Escherichia coli Hfq as a model, but the protocols presented here can be applied to analyze any polymer of proteins. This chapter thus provides a guideline to develop commonly used approaches to detect prokaryotic protein self-ass…

0301 basic medicine030103 biophysicsbiologyChemistryNoncoding RNA cofactorComputational biologyNon-coding RNAmedicine.disease_causeIn vitroCofactorProtein self-assembly03 medical and health sciences030104 developmental biologyGene expressionTransfer RNARNA chaperoneFunctional amyloidmedicinebiology.proteinEscherichia coli
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LRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric State.

2017

The low-density lipoprotein receptor-related protein 1, LRP1, interacts with APP and affects its processing. This is assumed to be mostly caused by the impact of LRP1 on APP endocytosis. More recently, also an interaction of APP and LRP1 early in the secretory pathway was reported whereat retention of LRP1 in the ER leads to decreased APP cell surface levels and in turn, to reduced Aβ secretion. Here, we extended the biochemical and immunocytochemical analyses by showing via live cell imaging analyses in primary neurons that LRP1 and APP are transported only partly in common (one third) but to a higher degree in distinct fast axonal transport vesicles. Interestingly, co-expression of LRP1 a…

0301 basic medicineADAM10amyloid precursor protein (APP)Endocytosislcsh:RC321-57103 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinemental disordersSecretionReceptorMolecular Biologylcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySecretory pathwayOriginal ResearchdimerizationChemistryVesicleLRP1030104 developmental biologyBiochemistrytransportBiophysicsAxoplasmic transportprocessinglow density lipoprotein receptor-related protein 1 (LRP1)030217 neurology & neurosurgeryNeuroscienceFrontiers in molecular neuroscience
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The Role of Chemokines in Alzheimer's Disease

2019

Objective: The most common multifactorial neurodegenerative disorder occurring in old age is Alzheimer’s disease. The neuropathological hallmarks of that disorder are amyloid plaques with the presence of β -amyloid aggregates, intraneuronal tau protein tangles, and chronic inflammation. Brain cells such as microglia and astrocytes are inflammatory cells associated with Alzheimer’s disease and involved in the production of inflammatory mediators, such as cytokines and chemokines. Chemokines consist of a large family of protein mediators with low molecular weight, which able to control the migration and residence of all immune cells. In pathological conditions, such as Alzheimer’s disease, c…

0301 basic medicineAgingChemokineAmyloidEndocrinology Diabetes and MetabolismTau protein030209 endocrinology & metabolismInflammation03 medical and health sciences0302 clinical medicineImmune systemAlzheimer DiseaseAmyloid precursor proteinAnimalsHumansImmunology and AllergyMedicineSenile plaquesInflammationbiologyMicrogliabusiness.industryBrainOxidative Stress030104 developmental biologymedicine.anatomical_structureImmunologybiology.proteinReceptors ChemokineChemokinesmedicine.symptombusinessEndocrine, Metabolic & Immune Disorders - Drug Targets
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Drosophila Full-Length Amyloid Precursor Protein is Required for Visual Working Memory and Prevents Age-Related Memory Impairment

2018

Summary The β-amyloid precursor protein (APP) plays a central role in the etiology of Alzheimer's disease (AD). However, its normal physiological functions are still unclear. APP is cleaved by various secretases whereby sequential processing by the β- and γ-secretases produces the β-amyloid peptide that is accumulating in plaques that typify AD. In addition, this produces secreted N-terminal sAPPβ fragments and the APP intracellular domain (AICD). Alternative cleavage by α-secretase results in slightly longer secreted sAPPα fragments and the identical AICD. Whereas the AICD has been connected with transcriptional regulation, sAPPα fragments have been suggested to have a neurotrophic and neu…

0301 basic medicineAgingFasciclin 2Nerve Tissue ProteinsGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciences0302 clinical medicineAmyloid precursor proteinMemory impairmentAnimalsDrosophila ProteinsOlfactory memorybiologyWorking memoryfungiMembrane ProteinsLong-term potentiationCell biology030104 developmental biologyDrosophila melanogasterMemory Short-Termbiology.proteinVisual PerceptionAmyloid Precursor Protein SecretasesGeneral Agricultural and Biological SciencesAmyloid precursor protein secretase030217 neurology & neurosurgeryNeurotrophin
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Biological and biophysics aspects of metformin-induced effects: cortex mitochondrial dysfunction and promotion of toxic amyloid pre-fibrillar aggrega…

2016

The onset of Alzheimer disease (AD) is influenced by several risk factors comprising diabetes. Within this context, antidiabetic drugs, including metformin, are investigated for their effect on AD. We report that in the C57B6/J mice, metformin is delivered to the brain where activates AMP-activated kinase (AMPK), its molecular target. This drug affects the levels of β- secretase (BACE1) and β-amyloid precursor protein (APP), promoting processing and aggregation of β-amyloid (Aβ), mainly in the cortex region. Moreover, metformin induces mitochondrial dysfunction and cell death by affecting the level and conformation of Translocase of the Outer Membrane 40 (TOM40), voltage-dependent anion-sel…

0301 basic medicineAgingmedicine.medical_specialtyMitochondrial poreAmyloidTranslocase of the outer membraneContext (language use)AMP-Activated Protein KinasesBiologyAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineβ-amyloid aggregationAlzheimer DiseaseHexokinaseInternal medicine?-amyloid aggregationmitochondrial dysfunctionmedicineAnimalsHypoglycemic Agentsmitochondrial poresMitochondrial transportAmyloid beta-PeptidesVoltage-Dependent Anion Channel 1BrainAMPKcell degenerationCell BiologyAlzheimer's diseasemedicine.diseaseMitochondriaMetformin030104 developmental biologyEndocrinologyAmyloid Precursor Protein SecretasesAlzheimer's diseasemetforminVDAC1030217 neurology & neurosurgeryResearch Papermedicine.drug
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Tocotrienol Affects Oxidative Stress, Cholesterol Homeostasis and the Amyloidogenic Pathway in Neuroblastoma Cells: Consequences for Alzheimer’s Dise…

2016

One of the characteristics of Alzheimer´s disease (AD) is an increased amyloid load and an enhanced level of reactive oxidative species (ROS). Vitamin E has known beneficial neuroprotective effects, and previously, some studies suggested that vitamin E is associated with a reduced risk of AD due to its antioxidative properties. However, epidemiological studies and nutritional approaches of vitamin E treatment are controversial. Here, we investigate the effect of α-tocotrienol, which belongs to the group of vitamin E, on AD-relevant processes in neuronal cell lines. In line with the literature, α-tocotrienol reduced the ROS level in SH-SY5Y cells. In the presence of tocotrienols, cholesterol…

0301 basic medicineAlzheimer´s diseasemedicine.medical_treatmentvitamin Eγ-secretasemedicine.disease_causeAntioxidantslcsh:ChemistryNeuroblastomachemistry.chemical_compoundAβ degradation0302 clinical medicineβ-secretaselcsh:QH301-705.5SpectroscopyNeuronschemistry.chemical_classificationbiologyTocotrienolsGeneral Medicinetocopherol3. Good healthComputer Science ApplicationsCholesterolNeuroprotective AgentsTocotrienolmedicine.medical_specialtyAmyloidamyloid-βNeuroprotectionArticleGene Expression Regulation EnzymologicCatalysisCell LineInorganic Chemistry03 medical and health sciencesAlzheimer DiseaseInternal medicinemedicineHumanstocotrienolPhysical and Theoretical ChemistryMolecular BiologyReactive oxygen speciesAmyloid beta-PeptidesCholesterolVitamin EOrganic Chemistrytocotrienol; vitamin E; Alzheimer´s disease; amyloid-β; tocopherol; Aβ degradation; β-secretase; γ-secretaseOxidative Stress030104 developmental biologyEndocrinologychemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinAmyloid Precursor Protein SecretasesReactive Oxygen SpeciesAmyloid precursor protein secretase030217 neurology & neurosurgeryOxidative stressInternational Journal of Molecular Sciences
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Curcumin-like compounds designed to modify amyloid beta peptide aggregation patterns

2017

International audience; Curcumin is a natural polyphenol able to bind the amyloid beta peptide, which is related to Alzheimer's disease, and modify its self-assembly pathway. This paper focuses on a multi-disciplinary study that starts from the design of curcumin-like compounds with the key chemical features required for inhibiting amyloid beta aggregation, and reports the effects of these compounds on the in vitro aggregation of amyloid beta peptides. Chemoinformatic screening was performed through the calculation of molecular descriptors that were able to highlight the drug-like profile, followed by docking studies with an amyloid beta peptide fibril. The computational design underlined t…

0301 basic medicineAmyloid betaGeneral Chemical Engineering[SDV]Life Sciences [q-bio]PeptideFibrillaw.inventionChemical compounds03 medical and health scienceschemistry.chemical_compoundConfocal microscopylawMolecular descriptorDiagnosisFluorescence spectroscopyGlycoproteinschemistry.chemical_classificationbiologyNeurodegenerative diseasesProteinsAlzheimer amyloid peptide oxadiazole curcuminGeneral ChemistrySettore CHIM/06 - Chimica OrganicaIn vitro030104 developmental biologychemistryBiochemistryDocking (molecular)Curcuminbiology.proteinCell culturePeptides
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The Blood-Brain Barrier in Alzheimer’s Disease

2020

The accumulation of neurotoxic amyloid-beta (Aβ) in the brain is one of the characteristic hallmarks of Alzheimer's disease (AD). Aβ-peptide brain homeostasis is governed by its production and various clearance mechanisms. The blood-brain barrier provides a large surface area for influx and efflux mechanisms into and out of the brain. Different transporters and receptors have been implicated to play crucial roles in Aβ clearance from brain. Besides Aβ transport, the blood-brain barrier tightly regulates the brain's microenvironment; however, vascular alterations have been shown in patients with AD. Here, we summarize how the blood-brain barrier changes during aging and in disease and focus …

0301 basic medicineAmyloid beta-PeptidesChemistryBrainATP-binding cassette transporterTransporterBlood–brain barrierLRP1ArticlePeptide Fragments03 medical and health sciences030104 developmental biology0302 clinical medicinemedicine.anatomical_structureReceptors LDLAlzheimer DiseaseBlood-Brain BarriermedicineHumansEffluxReceptorNeuroscience030217 neurology & neurosurgeryHomeostasisLipoprotein
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Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution

2016

The conversion of proteins into amyloid fibrils and other amyloid-like aggregates is closely connected to the onset of a series of age-related pathologies. Upon changes in environmental conditions, amyloid-like aggregates may also undergo disassembly into oligomeric aggregates, the latter being recognized as key effectors in toxicity. This indicates new possible routes for in vivo accumulation of toxic species. In the light of the recognized implication of α-Synuclein (αSN) in Parkinson's disease, we present an experimental study on supramolecular assembly of αSN with a focus on stability and disassembly paths of such supramolecular aggregate species. Using spectroscopic techniques, two-pho…

0301 basic medicineAmyloidAmyloidBiophysicsSupramolecular chemistryProtein aggregationBiochemistrySupramolecular assembly03 medical and health scienceschemistry.chemical_compoundProtein AggregatesHumansDissolutionAlpha-synucleinProtein Stabilityproteins amyloid fibrils amyloid-like aggregates oligomeric aggregatesSpectrum AnalysisOrganic ChemistryAggregate (data warehouse)TemperatureTrifluoroethanolAmyloid fibrilCrystallography030104 developmental biologychemistryBiophysicsalpha-Synuclein
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Hsp60, amateur chaperone in amyloid-beta fibrillogenesis

2016

BACKGROUND: Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD. METHODS: Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), t…

0301 basic medicineAmyloidMolecular chaperonesAmyloid betaBiophysicsPlasma protein bindingInhibition mechanismsBiochemistryChaperoninChaperonin03 medical and health sciences0302 clinical medicinemedicineHumansInhibition mechanismMolecular BiologyAmyloid aggregationAmyloid beta-PeptidesbiologyNeurodegenerationP3 peptideFibrillogenesisChaperonin 60medicine.diseaseAlzheimer's disease treatmentCell biology030104 developmental biologyChaperone (protein)biology.proteinHSP60030217 neurology & neurosurgeryProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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