Search results for "Amyloid"

showing 10 items of 494 documents

Oxidative stress in Alzheimer’s Disease: Implications for Prevention and Therapy

2006

Oxidative stress is a marker of neurodegeneration and has been recently shown to be also involved in the early stages of the pathogenesis of various neurodegenerative disorders. In general, all biomolecules of the cell can be oxidized and thereby damaged. Consequently, the concept of neuroprotection by antioxidants has been developed. In many cases the direct scavanging of free radicals have been used as a strategy to prevent oxidative stress damage and a variety of physiological and synthetic antioxidant molecules have been identified and synthesized including the female sex homone estrogen. In Alzheimer’s Disease amyloid-β protein on its way to brain deposition can also induce oxidative c…

Amyloidbusiness.industryNeurodegenerationInflammationDNA oxidationBlood–brain barrierBioinformaticsmedicine.disease_causemedicine.diseaseProtein oxidationNeuroprotectionmedicine.anatomical_structuremedicinemedicine.symptombusinessOxidative stress
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Rational Management of Macroglossia Due to Acquired Systemic Amyloidosis: Does Surgery Play a Role?

2008

Amyloidmedicine.medical_specialtyFatal outcomemedicine.medical_treatmentMEDLINEFatal OutcomeTracheostomyMacroglossiaTonguemedicineMacroglossiaHumansGastrostomyGlossectomybusiness.industryContraindicationsAmyloidosisAmyloidosisMiddle Agedmedicine.diseaseSystemic amyloidosisGastrostomySurgerymedicine.anatomical_structureOtorhinolaryngologyGlossectomyFemaleImmunoglobulin Light ChainsSurgeryOral Surgerymedicine.symptomMultiple MyelomabusinessJournal of Oral and Maxillofacial Surgery
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Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites

2022

AbstractAmyloid protein aggregates are not only associated with neurodegenerative diseases and may also occur as unwanted by-products in protein-based therapeutics. Surfactants are often employed to stabilize protein formulations and reduce the risk of aggregation. However, surfactants alter protein-protein interactions and may thus modulate the physicochemical characteristics of any aggregates formed. Human insulin aggregation was induced at low pH in the presence of varying concentrations of the surfactant polysorbate 80. Various spectroscopic and imaging methods were used to study the aggregation kinetics, as well as structure and morphology of the formed aggregates. Molecular dynamics s…

Amyloid-like Spherulites Fluorescence Lifetime Imaging Aggregate Stability Polysorbate 80 Protein FormulationsAmyloidMorphology (linguistics)AmyloidChemistryInsulinmedicine.medical_treatmentIntermolecular forcePolysorbatesPolyvinyl alcoholSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsBiomaterialsSurface-Active Agentschemistry.chemical_compoundMolecular dynamicsColloid and Surface ChemistryPulmonary surfactantCritical micelle concentrationmedicineBiophysicsHumansInsulinMicelles
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Corrigendum to “Polysorbate 80 controls Morphology, structure and stability of human insulin Amyloid-Like spherulites” [J. Colloid Interface Sci. 606…

2023

Amyloid-like Spherulites Fluorescence Lifetime Imaging Aggregate Stability Polysorbate 80 Protein FormulationsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)
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Doppler Myocardial Imaging for Early Detection of Cardiac Involvement in Patients with Systemic AL Amyloidosis.

2008

Amyloidosis doppler imaging.
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Lymphonodal amyloidosis: case report

2009

Amyloidosis lymphomaSettore MED/15 - Malattie Del Sangue
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Antioxidant Pathways in Alzheimers Disease: Possibilities of Intervention

2011

Alzheimer's disease (AD) is closely related to the occurrence of oxidative stress. It was claimed that all pathophysiological mechanisms involved in the onset and progression of AD are related to oxidative stress. Thus, it is important to evaluate if there is oxidative stress as well as the mechanism by which this happens in AD patients as well as in animal models of AD. Extracellular plaques of amyloid b peptides (Aβ), a hallmark of the disease, have been postulated to be more protective than damaging in terms of oxidative stress because they may be chemical sinks in which heavy metals are placed. More than a decade ago we reasoned that damage due to Ab might be caused not by extracellular…

AntioxidantAmyloidmedicine.medical_treatmentRespiratory chainNerve Tissue ProteinsBiologyPharmacologymedicine.disease_causeAntioxidantsAlzheimer DiseaseDrug DiscoverymedicineExtracellularAnimalsHumansMolecular Targeted TherapyPharmacologychemistry.chemical_classificationReactive oxygen speciesEstradiolVitamin Emedicine.diseaseUp-RegulationOxidative StressNeuroprotective AgentschemistryDietary SupplementsImmunologyAlzheimer's diseaseReactive Oxygen SpeciesOxidative stressCurrent Pharmaceutical Design
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Amyloid-β toxicity and tau hyperphosphorylation are linked via RCAN1 in Alzheimer's disease.

2011

Amyloid-β peptide (Aβ) toxicity and tau hyperphosphorylation are hallmarks of Alzheimer’s disease (AD). How their molecular relationships may affect the etiology, progression, and severity of the disease, however, has not been elucidated. We now report that incubation of foetal rat cortical neurons with Aβ up-regulates expression of the Regulator of Calcineurin gene RCAN1, and this is mediated by Aβ-induced oxidative stress. Calcineurin (PPP3CA) is a serine-threonine phosphatase that dephosphorylates tau. RCAN1 proteins inhibit this phosphatase activity of calcineurin. Increased expression of RCAN1 also causes up-regulation of glycogen synthase kinase-3beta (GSK3β), a tau kinase. Thus, incr…

Apolipoprotein EAdultMuscle Proteinstau ProteinsBiologymedicine.disease_causeTransfectionArticleDephosphorylationGlycogen Synthase Kinase 3GSK-3Alzheimer DiseasemedicineAnimalsHumansLymphocytesPhosphorylationRNA Small InterferingGSK3BCells CulturedChromatography High Pressure LiquidRegulation of gene expressionCerebral CortexNeuronsAmyloid beta-PeptidesGlycogen Synthase Kinase 3 betaGeneral NeuroscienceCalcineurinIntracellular Signaling Peptides and ProteinsGeneral MedicineMiddle Agedmedicine.diseaseEmbryo MammalianMolecular biologyGlutathionePeptide FragmentsCell biologyRatsCalcineurinDNA-Binding ProteinsPsychiatry and Mental healthClinical PsychologyOxidative StressGene Expression RegulationFemaleGeriatrics and GerontologyAlzheimer's diseaseOxidative stressJournal of Alzheimer's disease : JAD
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Functional Role of Lipoprotein Receptors in Alzheimers Disease

2008

The LDL receptor gene family constitutes a class of structurally closely related cell surface receptors fulfilling diverse functions in different organs, tissues, and cell types. The LDL receptor is the prototype of this family, which also includes the VLDLR, ApoER2/LRP8, LRP1 and LRP1B, as well as Megalin/GP330, SorLA/LR11, LRP5, LRP6 and MEGF7. Recently several lines of evidence have positioned the LDL receptor gene family as one of the key players in Alzheimer's disease (AD) research. Initially this receptor family was of high interest due to its key function in cholesterol/apolipoprotein E (ApoE) uptake, with the epsilon4 allele of ApoE as the strongest genetic risk factor for late-onse…

Apolipoprotein EAmyloid beta-PeptidesbiologyChemistryEndosomeLRP1BLRP1Cell biologyAmyloid beta-Protein PrecursorApolipoproteins ECholesterolReceptors LDLNeurologyAlzheimer DiseaseCell surface receptormental disordersLDL receptorAmyloid precursor proteinbiology.proteinAnimalsHumansNeurology (clinical)ReceptorCurrent Alzheimer Research
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Apolipoprotein E Regulates Amyloid Formation within Endosomes of Pigment Cells.

2015

International audience; Accumulation of toxic amyloid oligomers is a key feature in the pathogenesis of amyloid-related diseases. Formation of mature amyloid fibrils is one defense mechanism to neutralize toxic prefibrillar oligomers. This mechanism is notably influenced by apolipoprotein E variants. Cells that produce mature amyloid fibrils to serve physiological functions must exploit specific mechanisms to avoid potential accumulation of toxic species. Pigment cells have tuned their endosomes to maximize the formation of functional amyloid from the protein PMEL. Here, we show that ApoE is associated with intraluminal vesicles (ILV) within endosomes and remain associated with ILVs when th…

Apolipoprotein EAmyloidAmyloidEndosome[SDV.BC]Life Sciences [q-bio]/Cellular BiologyEndosomesBiologyExosomesGeneral Biochemistry Genetics and Molecular BiologyMiceApolipoproteins Emental disordersAnimalsHumansamyloid-related diseaseslcsh:QH301-705.5[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMelanosomeMice KnockoutMelanosomesEndosomal Sorting Complexes Required for TransportVesicleMicrovesiclesPMELCell biologyMice Inbred C57BLlcsh:Biology (General)BiochemistryGene Expression RegulationMelanocytesSignal transductionHeLa CellsSignal TransductionCell reports
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