Search results for "β-amyloid"

showing 7 items of 7 documents

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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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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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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Rebalancing β-Amyloid-Induced Decrease of ATP Level by Amorphous Nano/Micro Polyphosphate: Suppression of the Neurotoxic Effect of Amyloid β-Protein …

2017

Morbus Alzheimer neuropathology is characterized by an impaired energy homeostasis of brain tissue. We present an approach towards a potential therapy of Alzheimer disease based on the high-energy polymer inorganic polyphosphate (polyP), which physiologically occurs both in the extracellular and in the intracellular space. Rat pheochromocytoma (PC) 12 cells, as well as rat primary cortical neurons were exposed to the Alzheimer peptide Aβ25-35. They were incubated in vitro with polyphosphate (polyP); ortho-phosphate was used as a control. The polymer remained as Na+ salt; or complexed in a stoichiometric ratio to Ca2+ (Na-polyP[Ca2+]); or was processed as amorphous Ca-polyP microparticles (C…

Calcium Phosphates0301 basic medicineIntracellular SpacePeptidelcsh:Chemistrychemistry.chemical_compoundAdenosine TriphosphateX-Ray DiffractionPolyphosphatesSpectroscopy Fourier Transform Infraredprimary rat cortex neuronslcsh:QH301-705.5SpectroscopyCerebral CortexNeuronschemistry.chemical_classificationmicroparticlesChemistryβ-amyloidGeneral Medicinepathological conditions signs and symptomsComputer Science Applicationsneurotoxic effectsurgical procedures operativeBiochemistryAlzheimer's diseaseIntracellularCell Survivalβ-amyloid; calcium polyphosphate; microparticles; neurotoxic effect; adenosine triphosphate level; PC12 cells; primary rat cortex neuronsArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineExtracellularotorhinolaryngologic diseasesAnimalsPhysical and Theoretical ChemistryMolecular BiologyneoplasmsAmyloid beta-PeptidesPolyphosphateOrganic ChemistryNeurotoxicityPC12 cellsmedicine.diseaseIn vitrodigestive system diseasesRats030104 developmental biologylcsh:Biology (General)lcsh:QD1-999BiophysicsNanoparticlesAdenosine triphosphatecalcium polyphosphateadenosine triphosphate levelInternational Journal of Molecular Sciences
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Neuroprotective and Antioxidant Role of Oxotremorine-M, a Non-selective Muscarinic Acetylcholine Receptors Agonist, in a Cellular Model of Alzheimer …

2022

AbstractAlzheimer disease (AD) is a multifactorial and age-dependent neurodegenerative disorder, whose pathogenesis, classically associated with the formation of senile plaques and neurofibrillary tangles, is also dependent on oxidative stress and neuroinflammation chronicization. Currently, the standard symptomatic therapy, based on acetylcholinesterase inhibitors, showed a limited therapeutic potential, whereas disease-modifying treatment strategies are still under extensive research. Previous studies have demonstrated that Oxotremorine-M (Oxo), a non-selective muscarinic acetylcholine receptors agonist, exerts neurotrophic functions in primary neurons, and modulates oxidative stress and …

Cellular and Molecular NeuroscienceOxidative stressβ-amyloidCell BiologyGeneral MedicineSH-SY5Y cellsMitochondriaCellular and molecular neurobiology
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Naturally occurring autoantibodies interfere with β-amyloid metabolism and improve cognition in a transgenic mouse model of Alzheimer's disease 24 h …

2013

There is evidence that naturally occurring antibodies directed against Aβ (nAbs-Aβ) have a role in Aβ-metabolism and Aβ-clearance. The presence of nAbs-Aβ leads to a reduction in amyloid fibrillation and thus a reduction in their toxicity. We investigated the effects of nAbs-Aβ in respect to oligomerization and used the Tg2576 transgenic mouse model in order to investigate the rapid effect with a single-dose (24 h) on oligomer breakdown and cytokine secretion along with immunohistochemical characterization of synaptic plasticity. nAbs-Aβ were able to reduce toxic oligomer concentration with an increase in Aβ-monomers. Cytokine secretion was significantly reduced. Synaptic plasticity was als…

Genetically modified mousemedicine.medical_specialtytoxic oligomersAmyloidBlotting WesternEnzyme-Linked Immunosorbent AssayMice TransgenicBiologyAnimals Genetically ModifiedCellular and Molecular NeuroscienceMiceCognitionAlzheimer DiseaseInternal medicinemedicineAnimalsBiological PsychiatryAutoantibodiesAmyloid beta-Peptidesβ-amyloidbehaviorAutoantibodyAlzheimer's diseasemedicine.diseasenatural occurring autoantibodiesCell biologyPsychiatry and Mental healthDisease Models AnimalEndocrinologyinflammationSynaptic plasticityToxicitybiology.proteinCytokinesCytokine secretionOriginal ArticleFemaleAlzheimer's diseaseAntibodyTranslational Psychiatry
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Beta-amyloid monomers are neuroprotective

2009

The 42-aa-long β-amyloid protein—Aβ1-42—is thought to play a central role in the pathogenesis of Alzheimer's disease (AD) (Walsh and Selkoe, 2007). Data from AD brain (Shankar et al., 2008), transgenic APP (amyloid precursor protein)-overexpressing mice (Lesné et al., 2006), and neuronal cultures treated with synthetic Aβ peptides (Lambert et al., 1998) indicate that self-association of Aβ1-42monomers into soluble oligomers is required for neurotoxicity. The function of monomeric Aβ1-42is unknown. The evidence that Aβ1-42is present in the brain and CSF of normal individuals suggests that the peptide is physiologically active (Shoji, 2002). Here we show that synthetic Aβ1-42monomers support …

N-MethylaspartateStimulationPeptideNeuroprotectionNeuro-degenerative diseasePathogenesismental disordersNitrilesmedicineAmyloid precursor proteinButadienesExcitatory Amino Acid AgonistsAnimalsEnzyme InhibitorsReceptorCells CulturedPodophyllotoxinchemistry.chemical_classificationCerebral CortexNeuronsAnalysis of VarianceAmyloid beta-PeptidesbiologyCell DeathDose-Response Relationship DrugGeneral NeuroscienceNeurodegenerationβ-Amyloid proteinNeurotoxicityself-assemblyTyrphostinsmedicine.diseaseEmbryo MammalianPeptide FragmentsCell biologyRatsNeuroprotective Agentschemistrybiology.proteinBrief CommunicationsNeuroscienceβ-Amyloid protein; Neuro-degenerative diseases; self-assembly
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