Search results for "Prion disease"

showing 10 items of 13 documents

The cognitive profile of prion disease: a prospective clinical and imaging study

2015

Objectives Prion diseases are dementing illnesses with poorly defined neuropsychological features. This is probably because the most common form, sporadic Creutzfeldt-Jakob disease, is often rapidly progressive with pervasive cognitive decline making detailed neuropsychological investigation difficult. This study, which includes patients with inherited, acquired (iatrogenic and variant) and sporadic forms of the disease, is the only large-scale neuropsychological investigation of this patient group ever undertaken and aimed to define a neuropsychological profile of human prion diseases. Methods A tailored short cognitive examination of all of the patients (n = 81), with detailed neuropsycho…

Pediatricsmedicine.medical_specialtySettore M-PSI/02 - Psicobiologia E Psicologia Fisiologicabusiness.industryGeneral NeuroscienceNeuropsychologyCognitionDiseasePrion diseases cognitive declineBioinformaticsPRNPClinical trialBasal gangliamedicineNeurology (clinical)Differential diagnosisCognitive declinebusinessResearch ArticlesAnnals of Clinical and Translational Neurology
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Lenalidomide induced reversible parkinsonism, dystonia, and dementia in subclinical Creutzfeldt-Jakob disease

2018

DystoniaPediatricsmedicine.medical_specialtybusiness.industryParkinsonismPrion diseaseDiseaseParkinsonismmedicine.disease030226 pharmacology & pharmacyCreutzfeldt-Jakob disease03 medical and health sciences0302 clinical medicineNeurologymedicineDementiaNeurology (clinical)businessLenalidomide030217 neurology & neurosurgerySubclinical infectionLenalidomidemedicine.drugJournal of the Neurological Sciences
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Novel approaches in diagnosis and therapy of Creutzfeldt-Jakob disease.

2000

The scrapie prion protein, PrP(Sc), as well as its peptide fragment, PrP106-126, are toxic on neuronal cells, resulting in cell death by an apoptotic, rather than necrotic mechanism. The apoptotic process of neuronal cells induced by prion protein supports diagnosis and offers potential targets for therapeutic intervention of the prion diseases. Among the cerebrospinal fluid (CSF) proteins, which may serve as markers of neuronal cell death associated with prion diseases, the 14-3-3 protein(s) turned out to be the most promising one. A new sensitive assay allows the detection of even small changes in the normally low levels of these proteins. In vitro, the toxic effects displayed by PrP(Sc) …

NeuronsAgingCell DeathPrPSc ProteinsNeurotoxicityMemantinePrPSc ProteinsScrapieBiologyPharmacologymedicine.diseaseVirologyCreutzfeldt-Jakob Syndromenervous system diseasesPrion DiseasesmedicineNeurotoxinAnimalsHumansFlupirtineReceptor14-3-3 proteinDevelopmental Biologymedicine.drugMechanisms of ageing and development
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Neuroprotective effect of flupirtine in prion disease

2003

Apoptotic neuronal cell death is a hallmark of prion diseases. The apoptotic process in neuronal cells is thought to be caused by the scrapie prion protein, PrPSc, and can be experimentally induced by its peptide fragment, PrP106-126. This process is a target for potential drugs to combat prion disease or to ameliorate its symptoms. Flupirtine (Katadolon), a pyridine derivative that is in clinical use as a nonopioid analgesic, has a potent cytoprotective effect, at concentrations above 1 microg/mL, on neuronal cells treated with PrP(Sc) or PrP106-126. This drug acts as an N-methyl-D-aspartate (NMDA) antagonist, but does not bind to NMDA receptors. Flupirtine normalizes the level of intracel…

Pathologymedicine.medical_specialtyProgrammed cell deathanimal diseasesAnalgesicAminopyridinesScrapiePharmacologyNeuroprotectionPrion DiseasesmedicineAnimalsHumansPharmacology (medical)Pharmacologybusiness.industryAntagonistGeneral MedicineGlutathioneGenes bcl-2nervous system diseasesNeuroprotective Agentsnervous systemApoptosisNMDA receptorCalciumFlupirtinebusinessmedicine.drugDrugs of Today
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Influence of ADAM10 on prion protein processing and scrapie infectiosity in vivo.

2009

Abstract Both the cellular prion protein (PrPc) and the amyloid precursor protein (APP) are physiologically subjected to complex proteolytic processing events. While for APP the proteinases involved – alpha-, beta- and gamma-secretase – have been identified in vitro and in vivo, the cleavage of PrPc by now has been linked only to the shedding activity of the metalloproteinase ADAM10 and/or ADAM17 in cell culture. Here we show that neuronal overexpression of the alpha-secretase ADAM10 in mice reduces all PrPc species detected in the brain instead of leading to enhanced amounts of specific cleavage products of PrPc. Additionally, the incubation time of mice after scrapie infection is signific…

Prionsanimal diseasesADAM10Molecular Sequence DataPrion diseaseScrapieMice Transgeniclcsh:RC321-571ADAM10 ProteinMiceIn vivomental disordersNeurotoxicitymedicineAmyloid precursor proteinAnimalsHumansGliosisAmino Acid Sequencealpha-Secretaselcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySheddingMetalloproteinasebiologyChemistryBrainMembrane ProteinsMolecular biologyIn vitronervous system diseasesMice Inbred C57BLADAM ProteinsNeurologyAlpha secretaseGliosisbiology.proteinCattlemedicine.symptomAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalScrapieNeurobiology of disease
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Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform enc…

2004

The conversion into abnormally folded prion protein (PrP) plays a key role in prion diseases. PrP(C) carries two N-linked glycan chains at amino acid residues 180 and 196 (mouse). Previous in vitro data indicated that the conversion process may not require glycosylation of PrP. However, it is conceivable that these glycans function as intermolecular binding sites during the de novo infection of cells on susceptible organisms and/or play a role for the interaction of both PrP isoforms. Such receptor-like properties could contribute to the formation of specific prion strains. However, in earlier studies, mutations at the glycosylation sites of PrP led to intracellular trafficking abnormalitie…

Genetically modified mouseGlycanGlycosylationGlycosylationPrionsanimal diseasesBovine spongiform encephalopathyMutantBlotting WesternScrapieMice TransgenicCHO CellsCell SeparationBiologyBiochemistryCell LinePrion Diseaseschemistry.chemical_compoundMicePolysaccharidesCell Line TumorCricetinaemedicineAnimalsImmunoprecipitationProtein IsoformsBiotinylationDisulfidesTransgenesCloning MolecularMolecular BiologyBinding SitesWild typeBrainCell Biologymedicine.diseaseFlow CytometryVirologyMolecular biologyIn vitronervous system diseasesEncephalopathy Bovine SpongiformMice Inbred C57BLchemistryMutationbiology.proteinCattleScrapieThe Journal of biological chemistry
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Distinct neuropsychological profiles correspond to distribution of cortical thinning in inherited prion disease caused by insertional mutation

2012

Background The human prion diseases are a group of universally fatal neurodegenerative disorders associated with the auto-catalytic misfolding of the normal cell surface prion protein (PrP). Mutations causative of inherited human prion disease (IPD) include an insertion of six additional octapeptide repeats (6-OPRI) and a missense mutation (P102L) with large families segregating for each mutation residing in southern England. Here we report for the first time the neuropsychological and clinical assessments in these two groups. Method The cognitive profiles addressing all major domains were obtained for 26 patients (18 6-OPRI, 8 P102L) and the cortical thickness determined using 1.5T MRI in …

AdultMalePathologymedicine.medical_specialtyPrionsprion diseaseNeuroimagingDiseaseNeuropsychological Testsmedicine.disease_causePrion DiseasesExecutive FunctionYoung AdultHumansMedicineDementiaMissense mutationStrokeMemory DisordersMutationSettore M-PSI/02 - Psicobiologia E Psicologia Fisiologicabusiness.industryGenetic heterogeneityNeuropsychologyBrainMiddle Agedmedicine.diseaseMagnetic Resonance ImagingUnited KingdomMutagenesis InsertionalPsychiatry and Mental healthFemaleSurgeryNeurology (clinical)Cognition DisordersbusinessExecutive dysfunctionJournal of Neurology, Neurosurgery and Psychiatry
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Mathematical models for the diffusion magnetic resonance signal abnormality in patients with prion diseases

2014

In clinical practice signal hyperintensity in the cortex and/or in the striatum on magnetic resonance (MR) diffusion-weighted images (DWIs) is a marker of sporadic Creutzfeldt–Jakob Disease (sCJD). MR diagnostic accuracy is greater than 90%, but the biophysical mechanisms underpinning the signal abnormality are unknown. The aim of this prospective study is to combine an advanced DWI protocol with new mathematical models of the microstructural changes occurring in prion disease patients to investigate the cause of MR signal alterations. This underpins the later development of more sensitive and specific image-based biomarkers. DWI data with a wide a range of echo times and diffusion weightin…

MalePathologysCJD sporadic Creutzfeldt–Jakob diseaseROI region of interestPrion diseasePrPSc prion protein scrapieElectroencephalographyFOV field of viewlcsh:RC346-429Prion DiseasesADC apparent diffusion coefficientTI inversion timeRPE rapidly progressive encephalopathyAged 80 and overTE echo timeBrain Mappingmedicine.diagnostic_testBrainRegular ArticleMiddle AgedBIC Bayesian information criterionTR repetition timemedicine.anatomical_structureNeurologylcsh:R858-859.7FemaleMPRAGE magnetization-prepared rapid acquisition gradient-echoAbnormalitySS-SE single shot spin-echoAdultmedicine.medical_specialtyCognitive NeuroscienceCreutzfeldt–Jakob diseaseCNR contrast to noise ratioEPI echo-planar imagingNeuropathologyPrPC prion protein cellularGrey matterSpongiform degenerationlcsh:Computer applications to medicine. Medical informaticsEEG electroencephalogramDiffusion MRINeuroimagingImage Interpretation Computer-AssistedmedicineHumansRadiology Nuclear Medicine and imaginglcsh:Neurology. Diseases of the nervous systemAgedCJD Creutzfeldt–Jakob diseaseGSS Gerstmann–Sträussler–Scheinker syndromebusiness.industryDWI diffusion weighted imagingDiffusion MRI; Biophysical models; Creutzfeldt-Jakob disease; Prion disease; Spongiform degenerationMagnetic resonance imagingModels TheoreticalHyperintensityCreutzfeldt-Jakob diseaseDiffusion Magnetic Resonance ImagingNeurology (clinical)businessBiophysical modelsDiffusion MRINeuroImage: Clinical
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Pharmacological intervention in age-associated brain disorders by Flupirtine: Alzheimer’s and Prion diseases

1998

Alzheimer's disease, a major form of dementia in the elderly has become an increasingly important health problem in developed countries. In vitro studies on primary neurons demonstrate that Flupirtine (Katadolon) at a concentration of 1 microg/ml, significantly reduces the neurotoxic (apoptotic) effect displayed by A beta25-35, a segment of the amyloid beta-protein precursor the etiologic agent of Alzheimer's disease. Flupirtine, which has been in clinical use since 10 years ago, prevents the toxic effect of PrP, the presumed etiologic agent of the Creutzfeldt-Jakob disease as well as the excitatory amino acid glutamate on cortical neurons. Flupirtine displays a bimodal activity. Its strong…

AgingTime FactorsCell SurvivalPrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologyNeuroprotectionPrion Diseaseschemistry.chemical_compoundGlutamatesAlzheimer DiseasemedicineAnimalsAmino Acid SequenceRats WistarCells CulturedNeuronsAmyloid beta-PeptidesGlutamate receptorNeurotoxicityBiological activityGlutathionemedicine.diseasePeptide FragmentsRatsNeuroprotective Agentsmedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2BiochemistrychemistryCalciumNeuronAlzheimer's diseaseFlupirtineDevelopmental Biologymedicine.drugMechanisms of Ageing and Development
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Temporal dynamics of hippocampal neurogenesis in chronic neurodegeneration.

2014

Increased neurogenesis has been reported in neurodegenerative disease, but its significance is unclear. In a mouse model of prion disease, Gomez-Nicola et al. detect increased neurogenesis in the dentate gyrus that partially counteracts neuronal loss. Targeting neurogenesis may have therapeutic potential.

AdultMaleAntimetabolites AntineoplasticPatch-Clamp TechniquesTime FactorsPrionsNeurogenesisGenetic VectorsHippocampusTissue BanksBiologyHippocampal formationHippocampusCreutzfeldt-Jakob SyndromePrion DiseasesMiceYoung AdultNeural Stem CellsAlzheimer Diseasevariant CJDNeural PathwaysmedicineAnimalsHumansAgedCell ProliferationDentate gyrusNeurogenesisNeurodegenerationCytarabineNeurodegenerative DiseasesOriginal ArticlesMiddle Agedmedicine.diseaseNeural stem cellMice Inbred C57BLNeuroanatomical Tract-Tracing Techniquesadult neurogenesisDisease Models AnimalChronic DiseaseDentate GyrusMossy Fibers HippocampalDisease ProgressionFemaleNeurology (clinical)Alzheimer's diseaseNeuroscienceNeural developmentAlzheimer’s diseaseBrain : a journal of neurology
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