Search results for "synuclein"

showing 10 items of 42 documents

MicroRNAs Dysregulation and Metabolism in Multiple System Atrophy.

2019

Multiple system atrophy (MSA) is an adult onset, fatal disease, characterized by an accumulation of alpha-synuclein (α-syn) in oligodendroglial cells. MicroRNAs (miRNAs) are small non-coding RNAs involved in post-translational regulation and several biological processes. Disruption of miRNA-related pathways in the central nervous system (CNS) plays an important role in the pathogenesis of neurodegenerative diseases, including MSA. While the exact mechanisms underlying miRNAs in the pathogenesis of MSA remain unclear, it is known that miRNAs can repress the translation of messenger RNAs (mRNAs) that regulate the following pathogenesis associated with MSA: autophagy, neuroinflammation, α-syn …

0301 basic medicineautophagyalpha-synucleinCentral nervous systemmultiple system atrophyReviewBiologylcsh:RC321-571neuroinflammationPathogenesis03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAtrophystomatognathic systemmicroRNAmental disordersmedicinelcsh:Neurosciences. Biological psychiatry. NeuropsychiatryNeuroinflammationAlpha-synucleinmicroRNAGeneral NeuroscienceAutophagyTranslation (biology)medicine.diseaseCell biologynervous system diseases030104 developmental biologymedicine.anatomical_structurechemistrynervous system030217 neurology & neurosurgeryNeuroscienceFrontiers in neuroscience
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Current disease modifying approaches to treat Parkinson's disease

2015

Parkinson's disease (PD is a progressive neurological disorder characterized by the degeneration and death of midbrain dopamine and non-dopamine neurons in the brain leading to motor dysfunctions and other symptoms, which seriously influence the quality of life of PD patients. The drug L-dopa can alleviate the motor symptoms in PD, but so far there are no rational therapies targeting the underlying neurodegenerative processes. Despite intensive research, the molecular mechanisms causing neuronal loss are not fully understood which has hampered the development of new drugs and disease-modifying therapies. Neurotrophic factors are by virtue of their survival promoting activities attract candi…

0301 basic medicinemedicine.medical_specialtyParkinson's diseaseNeurturinNeurotrophic factorBiologySettore BIO/09 - Fisiologia03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineNeuroinflammationDopamineNeurotrophic factorsInternal medicineα-SynucleinmedicineGlial cell line-derived neurotrophic factorMolecular BiologyCerebral dopamine neurotrophic factorDopamine neuronPharmacologyDopaminergicCell Biologymedicine.diseaseDopamine neurons; ER stress; Mitochondria; Neuroinflammation; Neuropeptides; Neurotrophic factors; Protein aggregation; α-Synuclein; Molecular Medicine; Molecular Biology; Pharmacology; Cellular and Molecular Neuroscience; Cell Biology3. Good healthMitochondriaNeuropeptide030104 developmental biologyNerve growth factorEndocrinologybiology.proteinER streMolecular MedicineProtein aggregationNeuroscience030217 neurology & neurosurgerymedicine.drug
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p27Kip1 regulates alpha-synuclein expression

2018

Alpha-synuclein (α-SYN) is the main component of anomalous protein aggregates (Lewy bodies) that play a crucial role in several neurodegenerative diseases (synucleinopathies) like Parkinson’s disease and multiple system atrophy. However, the mechanisms involved in its transcriptional regulation are poorly understood. We investigated here the role of the cyclin-dependent kinase (Cdk) inhibitor and transcriptional regulator p27Kip1 (p27) in the regulation of α-SYN expression. We observed that selective deletion of p27 by CRISPR/Cas9 technology in neural cells resulted in increased levels of α-SYN. Knock-down of the member of the same family p21Cip1 (p21) also led to increased α-SYN levels, in…

0301 basic medicinep27Kip1[SDV]Life Sciences [q-bio]03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCyclin-dependent kinaseTranscriptional regulationalpha synucleinAlpha synucleinPsychological repressionE2F4Alpha-synucleinSynucleinopathiesbiologyPromoterEnzyme inhibitorsMolecular biologyExpressió gènica3. Good healthnervous system diseases030104 developmental biologyOncologychemistryInhibidors enzimàticsnervous systemE2F4biology.proteinGene expressionTranscription Factor E2F4transcriptionp21Cip1Transcription030217 neurology & neurosurgeryResearch Paper
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A53T-Alpha-Synuclein Overexpression Impairs Dopamine Signaling and Striatal Synaptic Plasticity in Old Mice

2010

BACKGROUND: Parkinson's disease (PD), the second most frequent neurodegenerative disorder at old age, can be caused by elevated expression or the A53T missense mutation of the presynaptic protein alpha-synuclein (SNCA). PD is characterized pathologically by the preferential vulnerability of the dopaminergic nigrostriatal projection neurons. METHODOLOGY/PRINCIPAL FINDINGS: Here, we used two mouse lines overexpressing human A53T-SNCA and studied striatal dysfunction in the absence of neurodegeneration to understand early disease mechanisms. To characterize the progression, we employed young adult as well as old mice. Analysis of striatal neurotransmitter content demonstrated that dopamine (DA…

AgingDopaminelcsh:MedicineMicechemistry.chemical_compoundHomer Scaffolding ProteinsReceptor Cannabinoid CB1lcsh:ScienceLong-term depressionNeurotransmitterChromatography High Pressure LiquidIn Situ Hybridization FluorescenceOligonucleotide Array Sequence AnalysisMice KnockoutNeuronal PlasticityMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionDopaminergicNeurodegenerationGenetics and Genomics/Gene ExpressionElectrophysiologyalpha-SynucleinResearch ArticleRadioimmunoprecipitation Assaymedicine.medical_specialtyNeuronal Calcium-Sensor ProteinsHOMER1Substantia nigraNeurotransmissionBiologyNeurological DisordersInternal medicinemedicineAnimalsHumansddc:610Cyclic Nucleotide Phosphodiesterases Type 7Activating Transcription Factor 2lcsh:RNeuropeptidesmedicine.diseaseMolecular biologyCorpus StriatumMice Mutant StrainsEndocrinologyGenetics and Genomics/Disease ModelschemistrySynaptic plasticitylcsh:QCarrier ProteinsPLoS ONE
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Stressor-related impairment of synaptic transmission in hippocampal slices from α-synuclein knockout mice

2004

The role of alpha-synuclein (alpha-Syn) has recently received considerable attention because it seems to play a role in Parkinson's disease (PD). Missense mutations in the alpha-Syn gene were found in autosomal dominant PD and alpha-Syn was shown to be a major constituent of protein aggregates in sporadic PD and other synucleinopathies. Under normal conditions, alpha-Syn protein is found exclusively in synaptic terminals. However, the potential participation of alpha-synuclein in maintaining and regulating synaptic efficacy is unknown. We have investigated the excitatory synaptic modulation of alpha-synuclein in CA1 pyramidal neurons, using the in vitro hippocampal slice technique. The 4-am…

Alpha-synucleinanimal diseasesGeneral NeuroscienceHippocampusNeurotransmissionBiologynervous system diseaseschemistry.chemical_compoundSynaptic fatiguenervous systemchemistrySynaptic augmentationSynaptic plasticityKnockout mouseExcitatory postsynaptic potentialNeuroscienceEuropean Journal of Neuroscience
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Biomarkers Related to Synaptic Dysfunction to Discriminate Alzheimer’s Disease from Other Neurological Disorders

2022

Recently, the synaptic proteins neurogranin (Ng) and α-synuclein (α-Syn) have attracted scientific interest as potential biomarkers for synaptic dysfunction in neurodegenerative diseases. In this study, we measured the CSF Ng and α-Syn concentrations in patients affected by AD (n = 69), non-AD neurodegenerative disorders (n-AD = 50) and non-degenerative disorders (n-ND, n = 98). The concentrations of CSF Ng and α-Syn were significantly higher in AD than in n-AD and n-ND. Moreover, the Aβ42/Ng and Aβ42/α-Syn ratios showed statistically significant differences between groups and discriminated AD patients from n-AD patients, better than Ng or α-Syn…

Alzheimer’s disease; biomarkers; neurogranin; α-synucleinAmyloid beta-PeptidesneurograninOrganic ChemistrybiomarkersNeurodegenerative Diseasestau ProteinsGeneral MedicineCatalysisSettore MED/01 - Statistica MedicaComputer Science ApplicationsInorganic Chemistryα-synucleinAlzheimer DiseaseFluorodeoxyglucose F18alpha-SynucleinHumansCognitive DysfunctionSettore MED/26 - NeurologiaPhysical and Theoretical ChemistryAlzheimer’s diseaseMolecular BiologySpectroscopyInternational Journal of Molecular Sciences; Volume 23; Issue 18; Pages: 10831
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Cholesterol facilitates interactions between α‐synuclein oligomers and charge‐neutral membranes

2015

AbstractOligomeric species formed during α-synuclein fibrillation are suggested to be membrane-disrupting agents, and have been associated with cytotoxicity in Parkinson’s disease. The majority of studies, however, have revealed that the effect of α-synuclein oligomers is only noticeable on systems composed of anionic lipids, while the more physiologically relevant zwitterionic lipids remain intact. We present experimental evidence for significant morphological changes in zwitterionic membranes containing cholesterol, induced by α-synuclein oligomers. Depending on the lipid composition, model membranes are either unperturbed, disrupt, or undergo dramatic morphological changes and segregate …

AmyloidParkinson's diseaseFluorescent DyeBiophysicsPlasma protein bindingBiochemistryOligomerProtein Structure SecondaryMultiphoton microscopyMembrane phase separationCell membranechemistry.chemical_compoundGeneticStructural Biology2-NaphthylamineLaurdan fluorescenceGeneticsFluorescence microscopemedicineMolecular BiologyFluorescent DyesLaurateα-SynucleinMembranesChemistryMedicine (all)2-NaphthylamineCell MembraneMembraneCell BiologySettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CholesterolMembranemedicine.anatomical_structureBiophysicBiochemistryStructural biologyOligomeralpha-SynucleinParkinson’s diseaseProtein MultimerizationLaurdanLauratesProtein BindingFEBS Letters
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Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers.

2014

Amyloid formation is associated with neurodegenerative diseases such as Parkinson's disease (PD). Significant α-synuclein (αSN) deposition in lipid-rich Lewy bodies is a hallmark of PD. Nonetheless, an unraveling of the connection between neurodegeneration and amyloid fibrils, including the molecular mechanisms behind potential amyloid-mediated toxic effects, is still missing. Interaction between amyloid aggregates and the lipid cell membrane is expected to play a key role in the disease progress. Here, we present experimental data based on hybrid analysis of two-photon-microscopy, solution small-angle X-ray scattering and circular dichroism data. Data show in real time changes in liposome …

Circular dichroismAmyloidPolymers and PlasticsAmyloidLipid BilayersBioengineeringProtein Structure SecondaryBiomaterialsCell membraneMaterials ChemistrymedicineScattering RadiationLipid bilayerSpectroscopyLiposomeLaurdanAdvanced MicroscopyChemistryCircular DichroismX-RaysNeurodegenerationCell MembraneLipid bilayer fusionProteinsmedicine.diseaseamyloid-membrane interactionco-aggregatemedicine.anatomical_structureMembraneBiophysicsalpha-SynucleinLewy BodiesBiomacromolecules
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Early impairment of epigenetic pattern in neurodegeneration: Additional mechanisms behind pyrethroid toxicity

2019

Abstract Permethrin is a synthetic pyrethroid extensively used as anti-woodworm agent and for indoor and outdoor pest control. The main route of human exposure is through fruit, vegetable and milk intake. Low dosage exposure to permethrin during neonatal brain development (from postnatal day 6 to postnatal day 21) leads to dopamine decrease in rat striatum nucleus, oxidative stress and behavioural changes linked to the development of Parkinson's like neurodegeneration later in life. The aim of this study was to evaluate the expression of genes involved in the dopaminergic pathway and epigenetic regulatory mechanisms in adolescent rats treated with permethrin during neonatal brain developmen…

Male0301 basic medicineAgingDopamineStriatumPharmacologyBiologyBiochemistryEpigenesis GeneticMECP203 medical and health sciences0302 clinical medicineEndocrinologyDopamineNuclear Receptor Subfamily 4 Group A Member 2parasitic diseasesGeneticsmedicineAnimalsEpigeneticsRats WistarPromoter Regions GeneticDNA Modification MethylasesMolecular BiologyPermethrinOrphan receptorDopaminergicNeurodegenerationNeurodegenerative DiseasesCell BiologyDNA Methylationmedicine.diseaseCorpus StriatumRatsMolecular Docking Simulation030104 developmental biologyAnimals Newbornalpha-SynucleinProtein Multimerization030217 neurology & neurosurgeryPermethrinmedicine.drugExperimental Gerontology
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Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system

2000

alpha-Synuclein (alpha-Syn) is a 14 kDa protein of unknown function that has been implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that alpha-Syn-/- mice are viable and fertile, exhibit intact brain architecture, and possess a normal complement of dopaminergic cell bodies, fibers, and synapses. Nigrostriatal terminals of alpha-Syn-/- mice display a standard pattern of dopamine (DA) discharge and reuptake in response to simple electrical stimulation. However, they exhibit an increased release with paired stimuli that can be mimicked by elevated Ca2+. Concurrent with the altered DA release, alpha-Syn-/- mice display a reduction in striatal DA and an attenuation of …

MaleCalbindinsNeuroscience(all)DopamineDopamine AgentsLong-Term PotentiationPresynaptic TerminalsSynucleinsGene ExpressionGlutamic AcidSubstantia nigraNerve Tissue ProteinsNeurotransmissionMotor ActivityHippocampusSynaptic TransmissionReuptakechemistry.chemical_compoundMiceS100 Calcium Binding Protein GDopamineDopaminergic CellmedicineAnimalsAutoreceptorsAlpha-synucleinMice KnockoutNeuronsGeneral NeuroscienceRab3A GTP-Binding ProteinCorpus Striatumrab3A GTP-Binding Proteinnervous system diseasesMice Inbred C57BLSubstantia NigraAmphetaminechemistrynervous systemalpha-SynucleinCalciumFemaleBeta-synucleinNeuroscienceLocomotionmedicine.drug
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