Search results for "AMYLOID"

showing 10 items of 494 documents

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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Ethanol Controls the Self-Assembly and Mesoscopic Properties of Human Insulin Amyloid Spherulites.

2018

Protein self-assembly into amyloid fibrils or highly hierarchical superstructures is closely linked to neurodegenerative pathologies as Alzheimer's and Parkinson's diseases. Moreover, protein assemblies also emerged as building blocks for bioinspired nanostructured materials. In both the above mentioned fields, the main challenge is to control the growth and properties of the final protein structure. This relies on a more fundamental understanding of how interactions between proteins can determine structures and functions of biomolecular aggregates. Here, we identify a striking effect of the hydration of the single human insulin molecule and solvent properties in controlling hydrophobicity/…

0301 basic medicineCircular dichroismAmyloidAmyloidInsulins02 engineering and technologyMicroscopy Atomic Force03 medical and health scienceschemistry.chemical_compoundProtein structureMicroscopy Electron TransmissionScattering Small AngleSpectroscopy Fourier Transform InfraredMaterials ChemistryMoleculeHumansPhysical and Theoretical ChemistryAMYLOID SPECTROSOPY FLUORECENCE MICROSCOPYMesoscopic physicsEthanolMicroscopy ConfocalEthanolChemistryCircular DichroismOptical Imaging021001 nanoscience & nanotechnologySurfaces Coatings and FilmsNeutron Diffraction030104 developmental biologySpheruliteBiophysics0210 nano-technologySuperstructure (condensed matter)Hydrophobic and Hydrophilic Interactions
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Vascular pathology: Cause or effect in Alzheimer disease?

2018

Introduction: Alzheimer disease (AD) is the main cortical neurodegenerative disease. The incidence of this disease increases with age, causing significant medical, social and economic problems, especially in countries with ageing populations. Objective: This review aims to highlight existing evidence of how vascular dysfunction may contribute to cognitive impairment in AD, as well as the therapeutic possibilities that might arise from this evidence. Development: The vascular hypothesis emerged as an alternative to the amyloid cascade hypothesis as an explanation for the pathophysiology of AD. This hypothesis locates blood vessels as the origin for a variety of pathogenic pathways that lead …

0301 basic medicineContext (language use)DiseaseBlood–brain barrierlcsh:RC346-42903 medical and health sciences0302 clinical medicineAlzheimer DiseaseMaterials ChemistrymedicineDementiaHumanslcsh:Neurology. Diseases of the nervous systemNeuronsAmyloid beta-PeptidesVascular diseaseNeurodegenerationBrainmedicine.disease030104 developmental biologymedicine.anatomical_structureAgeingBlood-Brain BarrierCerebrovascular CirculationAlzheimer's diseasePsychologyNeuroscience030217 neurology & neurosurgeryNeurología (English Edition)
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ADAM10 in Alzheimer's disease: Pharmacological modulation by natural compounds and its role as a peripheral marker.

2019

Abstract Alzheimer’s disease (AD) represents a global burden in the economics of healthcare systems. Amyloid-β (Aβ) peptides are formed by amyloid-β precursor protein (AβPP) cleavage, which can be processed by two pathways. The cleavage by the α-secretase A Disintegrin And Metalloprotease 10 (ADAM10) releases the soluble portion (sAβPPα) and prevents senile plaques. This pathway remains largely unknown and ignored, mainly regarding pharmacological approaches that may act via different signaling cascades and thus stimulate non-amyloidogenic cleavage through ADAM10. This review emphasizes the effects of natural compounds on ADAM10 modulation, which eventuates in a neuroprotective mechanism. M…

0301 basic medicineFarmacologiaADAM10DiseaseRM1-950Natural compoundsCleavage (embryo)NeuroprotectionCatechin03 medical and health sciencesADAM10 ProteinAmyloid beta-Protein Precursor0302 clinical medicineAlzheimer DiseaseDisintegrinHumansSenile plaquesPharmacological modulationPharmacologyMetalloproteinaseAmyloid beta-PeptidesbiologyChemistryPlant ExtractsADAM10ProteinsGinkgo bilobaMembrane ProteinsGeneral Medicineα-SecretaseAlzheimer's disease030104 developmental biologyMalaltia d'AlzheimerNeuroprotective Agents030220 oncology & carcinogenesisPharmaceuticalbiology.proteinTherapeutics. PharmacologyAmyloid Precursor Protein SecretasesNeuroscienceAlzheimer’s diseaseProteïnesBiomarkersBiomedicinepharmacotherapy = Biomedecinepharmacotherapie
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Direct observation of alpha-lactalbumin, adsorption and incorporation into lipid membrane and formation of lipid/protein hybrid structures

2019

The interaction between proteins and membranes is of great interest in biomedical and biotechnological research for its implication in many functional and dysfunctional processes. We present an experimental study on the interaction between model membranes and alpha-lactalbumin (alpha-La). alpha-La is widely studied for both its biological function and its anti-tumoral properties. We use advanced fluorescence microscopy and spectroscopy techniques to characterize alpha-La-membrane mechanisms of interaction and alpha-La-induced modifications of membranes when insertion of partially disordered regions of protein chains in the lipid bilayer is favored. Moreover, using fluorescence lifetime imag…

0301 basic medicineFluorescence-lifetime imaging microscopyProtein ConformationLipid BilayersBiophysics02 engineering and technologyBiochemistryMembrane Lipids03 medical and health sciencesProtein structureMembrane fluidityFluorescence microscopeAnimalsHumansLipid bilayerMolecular BiologyFluorescent DyesChemistryMembrane structure021001 nanoscience & nanotechnologyLipids2-PHOTON FLUORESCENCE MICROSCOPY; MOLTEN GLOBULE STATE; PARTIALLY FOLDED CONFORMATIONS; PROTEIN INTERACTIONS; CIRCULAR-DICHROISM; AMPHITROPIC PROTEINS; AMYLOID AGGREGATION; PHASOR APPROACH; OLEIC-ACID; LAURDANSpectrometry Fluorescence030104 developmental biologyMembranefluorescence FLIM Protein membrane interaction IDPLactalbuminBiophysicsCattleAdsorption0210 nano-technologyProtein adsorptionBiochimica et Biophysica Acta (BBA) - General Subjects
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