Search results for "YLOID"

showing 10 items of 526 documents

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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Beyond Amyloid - Widening the View on Alzheimer's Disease

2017

For 25 years, the amyloid cascade hypothesis, based on the finding that mutations in the amyloid precursor protein are closely linked to familial forms of Alzheimer's disease (AD), dominated the research on this disease. Recent failures of clinical anti-amyloidogenic trials, however, substantially support the reasoning (i) that the pathomechanisms that trigger familial AD, namely the generation, aggregation, and deposition of amyloid beta, cannot necessarily be extrapolated to sporadic cases and (ii) that amyloid beta represents a prominent histopathological feature in AD but not its exclusive causative factor. In autumn 2016, the Volkswagen Foundation hosted the Herrenhausen Symposium ‘Bey…

0301 basic medicineAmyloidbiologyAmyloid betabusiness.industryDiseaseBiochemistryMini review03 medical and health sciencesCellular and Molecular Neuroscience030104 developmental biology0302 clinical medicinemental disordersAmyloid precursor proteinbiology.proteinMedicineAmyloid cascadebusinessNeuroscience030217 neurology & neurosurgeryJournal of Neurochemistry
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Crosstalk between angiotensin and the nonamyloidogenic pathway of Alzheimer's amyloid precursor protein.

2017

The association between hypertension and an increased risk for Alzheimer's disease (AD) and dementia is well established. Many data suggest that modulation of the renin-angiotensin system may be meaningful for the prevention and therapy of neurodegenerative disorders, in particular AD. Proteolytic cleavage of the amyloid precursor protein (APP) by α-secretase precludes formation of neurotoxic Aβ peptides and is expected to counteract the development of AD. An established approach for the up-regulation of α-secretase cleavage is the activation of G protein-coupled receptors (GPCRs). Therefore, our study aimed to analyze whether stimulation of angiotensin AT1 or AT2 receptors stably expressed…

0301 basic medicineAngiotensin receptorAngiotensinsBiochemistryReceptor Angiotensin Type 2Receptor Angiotensin Type 103 medical and health sciencesAmyloid beta-Protein PrecursorAlzheimer DiseaseCyclohexanesGTP-Binding Protein gamma SubunitsAmyloid precursor proteinHumansMolecular Biologybeta-ArrestinsG protein-coupled receptorAngiotensin II receptor type 1biologyChemistryGTP-Binding Protein beta SubunitsP3 peptideCell BiologyAmyloidosisAngiotensin IIGTP-Binding Protein alpha SubunitsBiochemistry of Alzheimer's diseaseCell biology030104 developmental biologyHEK293 CellsPyrazinesProteolysisbiology.proteinAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseThe FEBS journal
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Clearing Amyloid-β through PPARγ/ApoE Activation by Genistein is a Treatment of Experimental Alzheimer’s Disease

2016

Amyloid-b (Ab) clearance from brain, which is decreased in Alzheimer's disease, is facilitated by apolipoprotein E (ApoE). ApoE is upregulated by activation of the retinoid X receptor moiety of the RXR/PPAR dimeric receptor. As we have previously demonstrated, estrogenic compounds, such as genistein, have antioxidant activity, which can be evidenced by increased expression of manganese superoxide dismutase (MnSOD). Furthermore, genistein is a non-toxic, well-tested, and inexpensive drug that activates PPARg receptor. We isolated and cultured cortical astrocytes from dissected cerebral cortices of neonatal mice (C57BL/6 J). Preincubation with genistein (5 mM) for 24 hours, prior to the addit…

0301 basic medicineApolipoprotein EApolipoprotein BPeroxisome proliferator-activated receptorGenisteinPlaque Amyloid01 natural sciencesBiochemistrychemistry.chemical_compound0302 clinical medicine030212 general & internal medicineReceptorCells CulturedNootropic Agentschemistry.chemical_classificationbiologyGeneral NeuroscienceBrainGeneral MedicineGenisteinPsychiatry and Mental healthClinical PsychologyNeuroprotective AgentsFemalePeroxisome proliferator-activated receptor gammamedicine.medical_specialtyTetrahydronaphthalenesMice TransgenicRetinoid X receptor03 medical and health sciencesApolipoproteins EDownregulation and upregulationAlzheimer DiseaseIn vivoPhysiology (medical)Internal medicineAvoidance LearningmedicineAnimalsHabituation PsychophysiologicMaze LearningAmyloid beta-PeptidesRecognition PsychologyOlfactory Perception0104 chemical sciencesMice Inbred C57BLPPAR gamma010404 medicinal & biomolecular chemistryDisease Models Animal030104 developmental biologyEndocrinologychemistryBexaroteneAstrocytesbiology.proteinPhytoestrogensGeriatrics and Gerontology030217 neurology & neurosurgeryJournal of Alzheimer's Disease
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β-amyloid wall deposit of temporal artery in subjects with spontaneous intracerebral haemorrhage.

2018

// Antonino Tuttolomondo 1 , Rosario Maugeri 4 , Elisabetta Orlando 2 , Giulio Giannone 2 , Francesco Ciccia 3 , Aroldo Rizzo 5 , Domenico Di Raimondo 1 , Francesca Graziano 4 , Rosaria Pecoraro 1 , Carlo Maida 1 , Irene Simonetta 1 , Anna Cirrincione 1 , Francesca Portelli 2 , Francesca Corpora 1 , Domenico Gerardo Iacopino 4 and Antonio Pinto 1 1 Internal Medicine and Stroke Care Ward, Dipartimento Biomedico di Medicina Interna e Specialistica, University of Palermo, Palermo, Italy 2 Human Pathology Section, Human Pathology Section, Department of Health Sciences, University of Palermo, Palermo, Italy 3 Rheumathology Ward, Dipartimento Biomedico di Medicina Interna e Specialistica, Univers…

0301 basic medicineApolipoprotein Emedicine.medical_specialtySettore MED/09 - Medicina InternaGastroenterologysuperficial temporal artery03 medical and health sciences0302 clinical medicineβ amyloidInternal medicinemedicine.arteryBiopsymedicineβ-amyloid temporal arterymedicine.diagnostic_testbusiness.industrySettore MED/27 - Neurochirurgiaβ-amyloidintracerebral haemorrhageUniversity hospitalControl subjectsmedicine.diseaseSuperficial temporal artery030104 developmental biologyOncologyTemporal arteryCerebral amyloid angiopathybusiness030217 neurology & neurosurgeryResearch PaperCAAH
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FMF is not always "fever": from clinical presentation to "treat to target".

2020

AbstractFamilial Mediterranean Fever, a monogenic autoinflammatory disease secondary to MEFV gene mutations in the chromosome 16p13, is characterized by recurrent self-limiting attacks of fever, arthritis, aphthous changes in lips and/or oral mucosa, erythema, serositis. It is caused by dysregulation of the inflammasome, a complex intracellular multiprotein structure, commanding the overproduction of interleukin 1. Familial Mediterranean Fever can be associated with other multifactorial autoinflammatory diseases, as vasculitis and Behçet disease.Symptoms frequently start before 20 years of age and are characterized by a more severe phenotype in patients who begin earlier.Attacks consist of …

0301 basic medicineAutoinflammatory diseasemedicine.medical_specialtyCanakinumabAutoinflammatory diseasesArthritisFamilial Mediterranean feverDiseaseReviewGene mutationFamilial Mediterranean feverDiagnosis Differential03 medical and health sciences0302 clinical medicineMedicineHumansChild030203 arthritis & rheumatologybusiness.industryAmyloidosislcsh:RJ1-570lcsh:Pediatricsmedicine.diseaseMEFVDermatologyTubulin ModulatorsCanakinumab030104 developmental biologyPhenotypebusinessColchicineSerositisBiomarkersmedicine.drugItalian journal of pediatrics
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Alzheimer's Disease and Molecular Chaperones: Current Knowledge and the Future of Chaperonotherapy

2016

Background: Alzheimer’s disease (AD) is a dementia, a neurodegenerative condition, and a protein-misfolding disease or proteinopathy, characterized by protein deposits, extracellular plaques and intracellular neurofibrillary tangles, which contain the AD’s typical pathological proteins, abnormal [1]-amyloid and hyperphosphorylated tau, respectively, and are located predominantly in the cortex of the frontal, parietal, and temporal brain lobes. What is the role of molecular chaperones in AD? Data indicate that molecular chaperones, also known as Hsp, are involved in AD, probably displaying protective roles and/or acting as pathogenic factors as it occurs in chaperonopathies in which case AD …

0301 basic medicineChaperonotherapyDisease03 medical and health sciencesAlzheimer DiseaseDrug DiscoveryProtein-misfolding diseasemedicineExtracellularAnimalsHumansDementiaAlzheimer’s disease; Chaperonopathies; Chaperonotherapy; Molecular chaperones; Protein-misfolding diseases; Tau; β-amyloid; Pharmacology; Drug Discovery3003 Pharmaceutical ScienceGenePharmacologybiologyβ-amyloidDrug Discovery3003 Pharmaceutical Sciencemedicine.diseaseHsp90030104 developmental biologyChaperone (protein)ImmunologyChaperonopathieMolecular chaperonebiology.proteinHSP60TauAlzheimer’s diseaseNeuroscienceIntracellularMolecular ChaperonesCurrent Pharmaceutical Design
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