Search results for "Nerve Tissue"

showing 10 items of 352 documents

Identification of potential therapeutic compounds for Parkinson's disease using Drosophila and human cell models.

2017

Abstract Parkinson's disease (PD) is the second most common neurodegenerative disorder after Alzheimer's disease. It is caused by a loss of dopaminergic neurons in the substantia nigra pars compacta, leading to a decrease in dopamine levels in the striatum and thus producing movement impairment. Major physiological causes of neurodegeneration in PD are oxidative stress (OS) and mitochondrial dysfunction; these pathophysiological changes can be caused by both genetic and environmental factors. Although most PD cases are sporadic, it has been shown that 5–10% of them are familial forms caused by mutations in certain genes. One of these genes is the DJ-1 oncogene, which is involved in an early…

0301 basic medicineParkinson's diseaseProtein Deglycase DJ-1Drug Evaluation PreclinicalSubstantia nigraNerve Tissue ProteinsBiologymedicine.disease_causeBiochemistryAnimals Genetically Modified03 medical and health sciences0302 clinical medicineDopaminePhysiology (medical)Cell Line TumorDrug DiscoverymedicineAnimalsDrosophila ProteinsHumansGeneticsMutationPars compactaNeurodegenerationDopaminergicParkinson Diseasemedicine.diseaseDisease Models AnimalOxidative Stress030104 developmental biologyGene Knockdown TechniquesMutationCancer researchDrosophila030217 neurology & neurosurgeryOxidative stressLocomotionmedicine.drugFree radical biologymedicine
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Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease

2016

International audience; Mutations in leucine-rich repeat kinase 2 (LRRK2) cause late-onset, autosomal dominant familial Parkinsons disease (PD) and variation at the LRRK2 locus contributes to the risk for idiopathic PD. LRRK2 can function as a protein kinase and mutations lead to increased kinase activity. To elucidate the pathophysiological mechanism of the R1441C mutation in the GTPase domain of LRRK2, we expressed human wild-type or R1441C LRRK2 in dopaminergic neurons of Drosophila and observe reduced locomotor activity, impaired survival and an age-dependent degeneration of dopaminergic neurons thereby creating a new PD-like model. To explore the function of LRRK2 variants in vivo, we …

0301 basic medicineProteomerab3 GTP-Binding Proteinsalpha-synucleindomainSyntaxin 1Interactomedopaminergic-neuronsAnimals Genetically Modifiedchemistry.chemical_compound0302 clinical medicinemicrotubule stabilityDrosophila ProteinsProtein Interaction MapsGenetics (clinical)LRRK2 GeneKinasephosphorylationBrainParkinson DiseaseArticlesGeneral Medicineautosomal-dominant parkinsonismLRRK2Drosophila melanogasterSynaptotagmin IProteomePhosphorylationSynaptic VesiclesNerve Tissue ProteinsBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-203 medical and health sciencesGeneticsAnimalsHumansKinase activitygeneMolecular BiologyAlpha-synucleingtp-bindingDopaminergic Neuronsrepeat kinase 2Molecular biologyPhosphoric Monoester Hydrolasesnervous system diseasesDisease Models Animal030104 developmental biologyGene Expression Regulationchemistrymutation030217 neurology & neurosurgery[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Endogenous β-neurexins on axons and within synapses show regulated dynamic behavior

2021

Summary: Neurexins are key organizer molecules that regulate synaptic function and are implicated in autism and schizophrenia. β-neurexins interact with numerous cell adhesion and receptor molecules, but their neuronal localization remains elusive. Using single-molecule tracking and high-resolution microscopy to detect neurexin1β and neurexin3β in primary hippocampal neurons from knockin mice, we demonstrate that endogenous β-neurexins are present in fewer than half of excitatory and inhibitory synapses. Moreover, we observe a large extrasynaptic pool of β-neurexins on axons and show that axonal β-neurexins diffuse with higher surface mobility than those transiently confined within synapses…

0301 basic medicineQH301-705.5Green Fluorescent ProteinsNerve Tissue ProteinsEndogenyHippocampal formationNeurotransmissionGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineProtein DomainsAnimalsPremovement neuronal activityneurotransmissionBiology (General)synaptic functionCell adhesionelectron microscopyintegumentary systemChemistryCell MembranefungiGlutamate receptorcell adhesionproteaseAxonsCell biologyMice Inbred C57BL030104 developmental biologyEctodomainProteolysisSynapsesExcitatory postsynaptic potentialsingle-particle tracking030217 neurology & neurosurgeryCell Reports
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Small Rab GTPases in Intracellular Vesicle Trafficking: The Case of Rab3A/Raphillin-3A Complex in the Kidney

2021

Small Rab GTPases, the largest group of small monomeric GTPases, regulate vesicle trafficking in cells, which are integral to many cellular processes. Their role in neurological diseases, such as cancer and inflammation have been extensively studied, but their implication in kidney disease has not been researched in depth. Rab3a and its effector Rabphillin-3A (Rph3A) expression have been demonstrated to be present in the podocytes of normal kidneys of mice rats and humans, around vesicles contained in the foot processes, and they are overexpressed in diseases with proteinuria. In addition, the Rab3A knockout mice model induced profound cytoskeletal changes in podocytes of high glucose fed a…

0301 basic medicineQH301-705.5Kidney Glomerulus030232 urology & nephrologyVesicular Transport ProteinsNerve Tissue ProteinsGTPaseReviewBiologyKidneyRabphilin-3ACatalysisInorganic Chemistry03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansPhysical and Theoretical ChemistryBiology (General)CytoskeletonMolecular BiologyQD1-999SpectroscopyAdaptor Proteins Signal TransducingKidneyEffectorPodocytesVesicleOrganic ChemistryRab3AIntracellular vesicleEpithelial CellsGeneral Medicinerab3A GTP-Binding ProteinComputer Science ApplicationsCell biologyChemistry030104 developmental biologymedicine.anatomical_structurerab GTP-Binding ProteinsRab proteinsKnockout mouseRabInternational Journal of Molecular Sciences
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Nucleocytoplasmic transport of the RNA-binding protein CELF2 regulates neural stem cell fates.

2020

The development of the cerebral cortex requires balanced expansion and differentiation of neural stem/progenitor cells (NPCs), which rely on precise regulation of gene expression. Because NPCs often exhibit transcriptional priming of cell-fate-determination genes, the ultimate output of these genes for fate decisions must be carefully controlled in a timely fashion at the post-transcriptional level, but how that is achieved is poorly understood. Here, we report that de novo missense variants in an RNA-binding protein CELF2 cause human cortical malformations and perturb NPC fate decisions in mice by disrupting CELF2 nucleocytoplasmic transport. In self-renewing NPCs, CELF2 resides in the cyt…

0301 basic medicineRegulation of gene expressionNeurogenesisRNA-Binding ProteinsTranslation (biology)RNA-binding proteinCell DifferentiationNerve Tissue ProteinsBiologyCell fate determinationGeneral Biochemistry Genetics and Molecular BiologyNeural stem cellCell biology03 medical and health sciences030104 developmental biology0302 clinical medicineNeural Stem CellsNucleocytoplasmic TransportCELF ProteinsHumansProgenitor cell030217 neurology & neurosurgeryCell reports
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Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
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2-methoxyestradiol impacts on amino acids-mediated metabolic reprogramming in osteosarcoma cells by interaction with NMDA receptor

2017

Deregulation of serine and glycine metabolism, have been identified to function as metabolic regulators in supporting tumor cell growth. The role of serine and glycine in regulation of cancer cell proliferation is complicated, dependent on concentrations of amino acids and tissue-specific. D-serine and glycine are coagonists of N-methyl-D-aspartate receptor subunit GRIN1. Importantly, NMDA receptors are widely expressed in cancer cells and play an important role in regulation of cell death, proliferation and metabolism of numerous malignancies. The aim of the present work was to associate the metabolism of glycine and D-serine with the anticancer activity of 2-methoxyestradiol. 2-methoxyest…

0301 basic medicineTime Factors2-methoxyestradiol neuronal nitric oxide synthase D-serine glycine osteosarcomaPhysiologyClinical BiochemistryNitric Oxide Synthase Type ISerine0302 clinical medicineCell MovementSerinechemistry.chemical_classificationMembrane Potential MitochondrialOsteosarcomaEstradiolTubulin ModulatorsAmino acidMolecular Docking Simulation030220 oncology & carcinogenesisMCF-7 CellsNMDA receptorOsteosarcomaFemalemedicine.drugProtein BindingSignal TransductionProgrammed cell deathGlycineAntineoplastic AgentsBone NeoplasmsBreast NeoplasmsNerve Tissue ProteinsBiologyMolecular Dynamics SimulationReceptors N-Methyl-D-Aspartate03 medical and health sciencesStructure-Activity RelationshipProtein DomainsmedicineHumans2-MethoxyestradiolCell ProliferationBinding SitesDose-Response Relationship DrugCell BiologyMetabolismmedicine.disease2-Methoxyestradiol030104 developmental biologychemistryCancer cellCancer researchEnergy Metabolism
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Impact of the Usher syndrome on olfaction

2015

Usher syndrome is a genetically and clinically heterogeneous disease in humans, characterized by sensorineural hearing loss, retinitis pigmentosa and vestibular dysfunction. This disease is caused by mutations in genes encoding proteins that form complex networks in different cellular compartments. Currently, it remains unclear whether the Usher proteins also form networks within the olfactory epithelium (OE). Here, we describe Usher gene expression at the mRNA and protein level in the OE of mice and showed interactions between these proteins and olfactory signaling proteins. Additionally, we analyzed the odor sensitivity of different Usher syndrome mouse models using electro-olfactogram re…

0301 basic medicineUsher syndromeCell Cycle ProteinsMice TransgenicNerve Tissue ProteinsOlfactionMyosinsBiologyCell LineMice03 medical and health sciencesOlfactory MucosaGene expressionRetinitis pigmentosaotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansCiliaMolecular BiologyGeneGenetics (clinical)GeneticsExtracellular Matrix ProteinsMessenger RNAGene Expression ProfilingEpithelial CellsGeneral MedicineCadherinsmedicine.diseaseeye diseasesSmellCytoskeletal ProteinsDisease Models Animal030104 developmental biologymedicine.anatomical_structureGene Expression RegulationMyosin VIIaMutationOdorantsSignal transductionCarrier ProteinsUsher SyndromesOlfactory epitheliumSignal TransductionHuman Molecular Genetics
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Histidine tracts in human transcription factors: insight into metal ion coordination ability

2017

Consecutive histidine repeats are chosen both by nature and by molecular biologists due to their high affinity towards metal ions. Screening of the human genome showed that transcription factors are extremely rich in His tracts. In this work, we examine two of such His-rich regions from forkhead box and MAFA proteins—MB3 (contains 18 His) and MB6 (with 21 His residues), focusing on the affinity and binding modes of Cu2+ and Zn2+ towards the two His-rich regions. In the case of Zn2+ species, the availability of imidazole nitrogen donors enhances metal complex stability. Interestingly, an opposite tendency is observed for Cu2+ complexes at above physiological pH, in which amide nitrogens part…

0301 basic medicineinorganic chemicalsMaf Transcription Factors LargeStereochemistryMetal ions in aqueous solutionPeptideNerve Tissue Proteins010402 general chemistry01 natural sciencesBiochemistryInorganic ChemistryMetal03 medical and health scienceschemistry.chemical_compoundCoordination ComplexesAmideImidazoleHomeostasisHumansHistidineAmino Acid SequenceTranscription factorHistidineLigand bindingchemistry.chemical_classificationOriginal PaperMass spectrometryForkhead Transcription FactorsHydrogen-Ion ConcentrationPeptide Fragments0104 chemical sciencesZinc030104 developmental biologyBinding affinitychemistryvisual_artPeptidevisual_art.visual_art_mediumThermodynamicsHuman genomeCopperProtein BindingJournal of Biological Inorganic Chemistry
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Dynamics of a Protein Interaction Network Associated to the Aggregation of polyQ-Expanded Ataxin-1

2020

Background: Several experimental models of polyglutamine (polyQ) diseases have been previously developed that are useful for studying disease progression in the primarily affected central nervous system. However, there is a missing link between cellular and animal models that would indicate the molecular defects occurring in neurons and are responsible for the disease phenotype in vivo. Methods: Here, we used a computational approach to identify dysregulated pathways shared by an in vitro and an in vivo model of ATXN1(Q82) protein aggregation, the mutant protein that causes the neurodegenerative polyQ disease spinocerebellar ataxia type-1 (SCA1). Results: A set of common dysregulated pathwa…

0301 basic medicinelcsh:QH426-470Ataxin 1Mice TransgenicNerve Tissue ProteinsProtein aggregationBlood–brain barrierblood-brain-barrierArticledrugspolyQ03 medical and health sciences0302 clinical medicineataxin-1Interaction networkIn vivoMutant proteinCerebellumGeneticsmedicineAnimalsGene Regulatory NetworksProtein Interaction MapsGenetics (clinical)NeuronsbiologypathwayGene Expression Profilingmedicine.diseaselcsh:Genetics030104 developmental biologymedicine.anatomical_structureGene Expression Regulationnetworkbiology.proteinSpinocerebellar ataxiaPeptidesNeuroscience030217 neurology & neurosurgeryFunction (biology)Genes
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