Search results for "Amyloid"

showing 10 items of 494 documents

Mice are not Men: ADAM30 Findings Emphasize a Broader Look Towards Murine Alzheimer's Disease Models

2016

Due to the growing population of people at advanced age, the number of patients affected by Alzheimer's disease (AD) is increasing tremendously. In 2015 about 46.8 million people suffered from AD worldwide which is estimated to increase to 131.5 million by 2050. Brains of AD patients all show a common histopathology; they are marked by an atrophy and degeneration that is caused by a severe loss of neurons and synapses (Braak and Del Tredici, 2012). Moreover, so-called extracellular senile plaques that consist of predominantly amyloid β (Aβ) peptides can be detected in the grey matter where they surround neurons. Since generation of Aβ peptides is hypothesized to play a major role in AD path…

0301 basic medicinePathologymedicine.medical_specialtyADAM10Populationlcsh:MedicineMice TransgenicGrey matterBiologyGeneral Biochemistry Genetics and Molecular BiologyPathogenesisMice03 medical and health sciences0302 clinical medicineAtrophyAlzheimer DiseasemedicineAmyloid precursor proteinAnimalsHumansSenile plaqueseducationlcsh:R5-920education.field_of_studylcsh:RP3 peptideGeneral Medicinemedicine.diseaseADAM ProteinsDisease Models Animal030104 developmental biologymedicine.anatomical_structureDisease ProgressionCommentarybiology.proteinlcsh:Medicine (General)Neuroscience030217 neurology & neurosurgeryEBioMedicine
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Subchronic administration of auranofin reduced amyloid-β plaque pathology in a transgenic APPNL-G-F/NL-G-F mouse model

2020

Abstract Alzheimer’s disease (AD) is the most common cause of dementia. Neuropathological processes, including the accumulation of amyloid-β (Aβ) plaques and neurofibrillary tangles, and neuroinflammation, lead to cognitive impairment at middle and eventually later stages of AD progression. Over the last decade, focused efforts have explored repurposed drug approaches for AD pathophysiological mechanisms. Recently, auranofin, an anti-inflammatory drug, was shown to have therapeutic potential in a number of diseases in addition to rheumatoid arthritis. Surprisingly, no data regarding the effects of auranofin on cognitive deficits in AD mice or the influence of auranofin on Aβ pathology and n…

0301 basic medicinePathologymedicine.medical_specialtyAuranofinGlial fibrillary acidic proteinbiologybusiness.industryAmyloid betaGeneral NeuroscienceGlutamate decarboxylaseHippocampusPathophysiology03 medical and health sciences030104 developmental biology0302 clinical medicineSynaptic plasticitybiology.proteinMedicineNeurology (clinical)businessMolecular Biology030217 neurology & neurosurgeryNeuroinflammationDevelopmental Biologymedicine.drugBrain Research
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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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Identification of Phlogacantholide C as a Novel ADAM10 Enhancer from Traditional Chinese Medicinal Plants

2016

Background: Alzheimer’s disease is one of the most prevalent dementias in the elderly population with increasing numbers of patients. One pivotal hallmark of this disorder is the deposition of protein aggregates stemming from neurotoxic amyloid-beta peptides. Synthesis of those peptides has been efficiently prevented in AD model mice by activation of an enzyme called alpha-secretase. Therefore, drugs with the capability to increase the expression of this enzyme, named ADAM10, have been suggested as a valuable therapeutic medication. Methods: We investigated 69 substances from a drug library derived from traditional Chinese medicine by luciferase reporter assay in human neuronal cells for th…

0301 basic medicinePhlogacanthus curviflorusADAM10lcsh:MedicineProtein aggregationBiologyPharmacologyArticle03 medical and health sciences0302 clinical medicineWestern blotGene expressionPhlogacantholide CmedicineAmyloid precursor proteinSecretionEnhancerADAM10; Amyloid precursor protein; Alzheimer’s disease; Norkurarinol; Phlogacantholide C; <i>Phlogacanthus curviflorus</i>; <i>Sophora flavescens</i>chemistry.chemical_classificationmedicine.diagnostic_testlcsh:RADAM10Norkurarinol030104 developmental biologyEnzymechemistrySophora flavescensAmyloid precursor proteinbiology.proteinAlzheimer’s disease030217 neurology & neurosurgeryMedicines
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PTEN recruitment controls synaptic and cognitive function in Alzheimer's models

2016

Dyshomeostasis of amyloid-β peptide (Aβ) is responsible for synaptic malfunctions leading to cognitive deficits ranging from mild impairment to full-blown dementia in Alzheimer's disease. Aβ appears to skew synaptic plasticity events toward depression. We found that inhibition of PTEN, a lipid phosphatase that is essential to long-term depression, rescued normal synaptic function and cognition in cellular and animal models of Alzheimer's disease. Conversely, transgenic mice that overexpressed PTEN displayed synaptic depression that mimicked and occluded Aβ-induced depression. Mechanistically, Aβ triggers a PDZ-dependent recruitment of PTEN into the postsynaptic compartment. Using a PTEN kno…

0301 basic medicinePrimary Cell CulturePDZ DomainsMice TransgenicMolecular neuroscienceBiologyNeurotransmissionSynaptic TransmissionMice03 medical and health sciences0302 clinical medicineAlzheimer DiseasePostsynaptic potentialmedicineAnimalsPTENGene Knock-In TechniquesAmyloid beta-PeptidesGeneral NeurosciencePTEN PhosphohydrolaseLong-term potentiationmedicine.diseaseRatsDisease Models Animal030104 developmental biologySynaptic fatigueSynaptic plasticitybiology.proteinAlzheimer's diseaseCognition DisordersNeuroscience030217 neurology & neurosurgeryNature Neuroscience
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Aβ Induces Excitotoxicity Mediated by APC/C-Cdh1 Depletion That Can Be Prevented by Glutaminase Inhibition Promoting Neuronal Survival

2016

AbstractThe E3 ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) is activated by the fizzy-related protein homolog/CDC20-like protein 1 (cdh1) in post-mitotic neurons. Growing evidence suggests that dysregulation of APC/C-Cdh1 is involved in neurodegenerative diseases. Here we show in neurons that oligomers of amyloid beta (Aβ), a peptide related to Alzheimer’s disease, cause proteasome-dependent degradation of cdh1. This leads to a subsequent increase in glutaminase (a degradation target of APC/C-Cdh1), which causes an elevation of glutamate levels and further intraneuronal Ca2+ dysregulation, resulting in neuronal apoptosis. Glutaminase inhibition prevents glutamate excitotoxi…

0301 basic medicineProteasome Endopeptidase ComplexCell SurvivalAmyloid betaBlotting WesternExcitotoxicityHippocampusmedicine.disease_causeHippocampusArticleAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsAnimals Genetically ModifiedMice03 medical and health sciences0302 clinical medicineGlutaminasemedicineAnimalsRats WistarNeuronsAmyloid beta-PeptidesMultidisciplinarybiologyGlutaminaseCyclin-dependent kinase 5Glutamate receptorCyclin-Dependent Kinase 5Molecular biologyRatsUbiquitin ligase030104 developmental biologyApoptosisbiology.protein030217 neurology & neurosurgeryScientific Reports
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Phosphorylation of meprin β controls its cell surface abundance and subsequently diminishes ectodomain shedding

2021

Meprin β is a zinc-dependent metalloprotease exhibiting a unique cleavage specificity with strong preference for acidic amino acids at the cleavage site. Proteomic studies revealed a diverse substrate pool of meprin β including the interleukin-6 receptor (IL-6R) and the amyloid precursor protein (APP). Dysregulation of meprin β is often associated with pathological conditions such as chronic inflammation, fibrosis, or Alzheimer's disease (AD). The extracellular regulation of meprin β including interactors, sheddases, and activators has been intensively investigated while intracellular regulation has been barely addressed in the literature. This study aimed to analyze C-terminal phosphorylat…

0301 basic medicineProtein Kinase C-alphaImmunoprecipitationmedia_common.quotation_subjectBiochemistry03 medical and health sciences0302 clinical medicineProtein Kinase C betaTumor Cells CulturedGeneticsAmyloid precursor proteinHumansPhosphorylationInternalizationMolecular BiologyProtein kinase Cmedia_commonbiologyChemistryCell MembraneMetalloendopeptidasesSheddaseCell biology030104 developmental biologyGene Expression RegulationEctodomainColonic NeoplasmsProteolysisbiology.proteinPhosphorylationExtracellular Space030217 neurology & neurosurgeryIntracellularBiotechnologyThe FASEB Journal
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Regulatory effects of simvastatin and apoJ on APP processing and amyloid-beta clearance in blood-brain barrier endothelial cells

2017

Amyloid-β peptides (Aβ) accumulate in cerebral capillaries indicating a central role of the blood-brain barrier (BBB) in the pathogenesis of Alzheimer’s disease (AD). Although a relationship between apolipoprotein-, cholesterol- and Aβ metabolism is evident, the interconnecting mechanisms operating in brain capillary endothelial cells (BCEC) are poorly understood. ApoJ (clusterin) is present in HDL that regulates cholesterol metabolism which is disturbed in AD. ApoJ levels are increased in AD brains and in plasma of cerebral amyloid angiopathy (CAA) patients. ApoJ may bind, prevent fibrillization, and enhance clearance of Aβ. We here define a connection of apoJ and cellular cholesterol home…

0301 basic medicineSimvastatinmedicine.medical_specialtyAmyloidSwineMice TransgenicBiologyBlood–brain barrierAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineInternal medicinemedicineAmyloid precursor proteinAnimalsMolecular BiologyCells CulturedAmyloid beta-PeptidesClusterinEndothelial CellsCell Biologymedicine.diseaseLRP1Peptide FragmentsMice Inbred C57BLClusterin030104 developmental biologyEndocrinologymedicine.anatomical_structureBlood-Brain Barrierbiology.proteinFemaleCerebral amyloid angiopathyblood-brain barrier ; amyloid-β ; cholesterol ; simvastatin ; clusterin/apoJ ; LRP1Protein Processing Post-Translational030217 neurology & neurosurgeryIntracellularLipoprotein
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Pressure effects on α-synuclein amyloid fibrils: An experimental investigation on their dissociation and reversible nature

2017

α–synuclein amyloid fibrils are found in surviving neurons of Parkinson's disease affected patients, but the role they play in the disease development is still under debate. A growing number of evidences points to soluble oligomers as the major cytotoxic species, while insoluble fibrillar aggregates could even play a protection role. In this work, we investigate α–synuclein fibrils dissociation induced at high pressure by means of Small Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy. Fibrils were produced from wild type α–synuclein and two familial mutants, A30P and A53T. Our results enlighten the different reversible nature of α–synuclein fibrils fragmentati…

0301 basic medicineSmall AngleAmyloidHigh-pressureMutantBiophysicsmacromolecular substances010402 general chemistryFibril01 natural sciencesBiochemistryDissociation (chemistry)Scattering03 medical and health scienceschemistry.chemical_compoundX-Ray DiffractionScattering Small AngleSpectroscopy Fourier Transform InfraredPressureHumansPoint MutationFourier transform infrared spectroscopyMolecular BiologySpectroscopyAlpha-synucleinAmyloid; FTIR; High-pressure; SAXS; α-synuclein; Amyloid; Humans; Parkinson Disease; Point Mutation; Pressure; Scattering Small Angle; Solubility; Spectroscopy Fourier Transform Infrared; X-Ray Diffraction; alpha-Synuclein; Biophysics; Biochemistry; Molecular BiologySmall-angle X-ray scatteringWild typeα-synucleinParkinson DiseaseSAXSAmyloid fibril0104 chemical sciences?-synucleinCrystallography030104 developmental biologyBiophysicchemistryFTIRSolubilityFourier Transform InfraredBiophysicsalpha-SynucleinHuman
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A Shotgun Proteomics Approach Reveals a New Toxic Role for Alzheimer's Disease Aβ Peptide: Spliceosome Impairment.

2017

Proteomic changes have been described in many neurodegenerative diseases, including Alzheimer's disease (AD). However, the early events in the onset of the pathology are yet to be fully elucidated. A cell model system in which LAN5 neuroblastoma cells were incubated for a short time with a recombinant form of Aβ42 was utilized. Proteins extracted from these cells were subjected to shotgun proteomics analysis by LTQ-Orbitrap-MS followed by label-free quantitation. By bioinformatics tools we found that the most significant of those found to be up-regulated were related to cytoskeletal dynamics (Rho related) and membrane-related processes. The most significant of the down-regulated proteins we…

0301 basic medicineSpliceosomeAmyloid beta-PeptideProteomeComputational biologyDiseaseBiologyBiochemistrylaw.inventionearly events in AD03 medical and health sciencesNeuroblastoma0302 clinical medicinelawAlzheimer DiseaseCell Line TumorHumansShotgun proteomicsCytoskeletonCytoskeletonGeneticsAmyloid beta-PeptidesChemistry (all)Cell MembraneGeneral ChemistryRibosomal RNAAlzheimer's diseaseRecombinant Proteinshotgun proteomicRecombinant Proteins030104 developmental biologySpliceosomeGene Expression RegulationRNA splicingRecombinant DNASpliceosomes030217 neurology & neurosurgeryBiogenesisHumanJournal of proteome research
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