Search results for "Myelin sheath"

showing 10 items of 55 documents

Changes of the ratio between myelin thickness and axon diameter in the human developing sural nerve

1978

Axon caliber and myelin sheath thickness of individual nerve fibers were evaluated in the developing human sural nerve using three different methods of measurement: 1. ocular micrometer evaluation of large fibers, 2. photographic enlargements for evaluating large numbers of nerve fibers of all sizes, and 3. electron microscopic enlargements for more precise measurements in selected nerves. The average axonal diameter doubles from 5 months gestation to about 5 years of age. Large fiber group axons increase, during the same period, by a factor of 3--3.5 with a slight decrease thereafter. The myelin thickness increases more slowly, but continuously, between 5 months gestation until the age of …

MaleAdolescentSural nervePathology and Forensic MedicineCellular and Molecular NeuroscienceMyelinSural NervemedicineHumansAxonChildElectron microscopicMyelin SheathOcular micrometerChemistryMyelin sheathsInfant NewbornInfantAnatomyAxonsMicroscopy ElectronSpinal Nervesmedicine.anatomical_structurenervous systemCaliberChild PreschoolMyelin sheathFemaleNeurology (clinical)MathematicsActa Neuropathologica
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Giant axonal neuropathy and leukodystrophy

1991

Abstract An 11-year-old Persian boy, born to consanguineous parents, manifested a progressive gait abnormality beginning at 5 years of age. A severe cerebellar disorder developed with associated dysfunction of the peripheral nervous system, but no sign of mental impairment. The sensory and motor nerve conduction velocities were greatly reduced, especially in the lower extremities. Cerebrospinal fluid protein was normal. Computed tomography and magnetic resonance imaging revealed leukoencephalopathy, especially in the cerebellum, but also in periventricular areas. The diagnosis of giant axonal neuropathy was established by biopsy of the sural nerve. The few previous histologic examinations h…

MaleIntermediate FilamentsMotor nerveGenes RecessiveSural nerveCerebral VentriclesLeukoencephalopathyConsanguinityDevelopmental NeuroscienceCerebellummedicineHumansCerebellar disorderGliosisPeripheral NervesChildMyelin SheathSpinocerebellar DegenerationsGiant axonal neuropathybusiness.industryLeukodystrophyAnatomymedicine.diseaseMagnetic Resonance ImagingAxonsMicroscopy Electronmedicine.anatomical_structurenervous systemNeurologyPeripheral nervous systemPediatrics Perinatology and Child HealthGait abnormalityNeurology (clinical)medicine.symptomHereditary Sensory and Motor NeuropathybusinessPediatric Neurology
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Transport of the major myelin proteolipid protein is directed by VAMP3 and VAMP7.

2011

CNS myelination by oligodendrocytes requires directed transport of myelin membrane components and a timely and spatially controlled membrane expansion. In this study, we show the functional involvement of the R-solubleN-ethylmaleimide-sensitive factor attachment protein receptor (R-SNARE) proteins VAMP3/cellubrevin and VAMP7/TI-VAMP in myelin membrane trafficking. VAMP3 and VAMP7 colocalize with the major myelin proteolipid protein (PLP) in recycling endosomes and late endosomes/lysosomes, respectively. Interference with VAMP3 or VAMP7 function using small interfering RNA-mediated silencing and exogenous expression of dominant-negative proteins diminished transport of PLP to the oligodendro…

MaleProteolipid protein 1Vesicle-Associated Membrane Protein 3MESH: Myelin SheathMESH: R-SNARE Proteins[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyR-SNARE ProteinsMiceMyelin0302 clinical medicineMESH: Microscopy ImmunoelectronMESH: Genetic VectorsImage Processing Computer-AssistedMESH: AnimalsMicroscopy ImmunoelectronMESH: Myelin Proteolipid ProteinCells CulturedMyelin SheathMESH: Vesicle-Associated Membrane Protein 3VAMP30303 health sciencesMESH: ExocytosisGeneral NeuroscienceMESH: Enzyme-Linked Immunosorbent AssayArticlesImmunohistochemistryMESH: Image Processing Computer-AssistedMyelin proteolipid proteinCell biologymedicine.anatomical_structureElectrophoresis Polyacrylamide GelFemaleRNA InterferenceMESH: Cells CulturedEndosomeGenetic VectorsMESH: RNA InterferenceBiological Transport ActiveEnzyme-Linked Immunosorbent AssayEndosomesBiologyTransfectionExocytosisExocytosis03 medical and health sciencesMESH: Mice Inbred C57BLmedicineAnimalsSecretionMyelin Proteolipid ProteinMESH: MiceSecretory pathway030304 developmental biologyMESH: TransfectionCell MembraneMESH: ImmunohistochemistryMESH: MaleMice Inbred C57BLnervous systemMESH: EndosomesMESH: Biological Transport ActiveLysosomesMESH: Female030217 neurology & neurosurgeryMESH: LysosomesMESH: Cell MembraneMESH: Electrophoresis Polyacrylamide Gel
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Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci

2011

Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia–axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relat…

MaleProteomicsCandidate geneProteomePrions10208 Institute of Neuropathology610 Medicine & healthHereditary neuralgic amyotrophyTetraspanin 24BiologySeptinTranscriptomeMice03 medical and health sciencesMyelin0302 clinical medicinemedicineAnimalsElectrophoresis Gel Two-DimensionalRNA MessengerMyelin Sheath030304 developmental biologyMice KnockoutGenetics0303 health sciencesGeneral NeuroscienceComputational BiologyMembrane Proteins2800 General NeuroscienceArticlesmedicine.diseaseSciatic NerveCell biologyMyelin basic proteinMice Inbred C57BLMolecular Weightmedicine.anatomical_structureAnimals Newbornnervous systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomebiology.protein570 Life sciences; biologyChemokinesMyelin ProteinsSeptins030217 neurology & neurosurgeryBiogenesisDemyelinating Diseases
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Biallelic mutations in neurofascin cause neurodevelopmental impairment and peripheral demyelination

2019

See Karakaya and Wirth (doi:10.1093/brain/awz273) for a scientific commentary on this article. Neurofascin (NFASC) isoforms are immunoglobulin cell adhesion molecules involved in node of Ranvier assembly. Efthymiou et al. identify biallelic NFASC variants in ten unrelated patients with a neurodevelopmental disorder characterized by variable degrees of central and peripheral involvement. Abnormal expression of Nfasc155 is accompanied by severe loss of myelinated fibres.

Male[SDV]Life Sciences [q-bio][SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyNerve Fibers MyelinatedGene FrequencyNeurodevelopmental Disorder[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]Nerve Growth FactorProtein IsoformsChildComputingMilieux_MISCELLANEOUSMyelin Sheathneurofascin; neurodevelopment; peripheral demyelinationAlleleneurodevelopmentDemyelinating DiseaseGenomicsneurodevelopment neurofascin peripheral demyelinationSettore MED/39 - Neuropsichiatria InfantilePedigree[SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunologyChild PreschoolPeripheral Nerve[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Femaleneurodevelopment; neurofascin; peripheral demyelinationNeurogliaHumanAdultAdolescentNervous System MalformationsGuillain-Barre SyndromeAxonNervous System MalformationneurofascinRanvier's NodesHumansNerve Growth FactorsPeripheral NervesAllelesAutoantibodiesperipheral demyelinationInfantProtein IsoformOriginal ArticlesAxonsnervous systemNeurodevelopmental DisordersCell Adhesion MoleculeMutationCell Adhesion MoleculesDemyelinating Diseases
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Nano-structured myelin: new nanovesicles for targeted delivery to white matter and microglia, from brain-to-brain

2021

Neurodegenerative diseases affect millions of people worldwide and the presence of various physiological barriers limits the accessibility to the brain and reduces the efficacy of various therapies. Moreover, new carriers having targeting properties to specific brain regions and cells are needed in order to improve therapies for the brain disorder treatment. In this study, for the first time, Myelin nanoVesicles (hereafter defined MyVes) from brain-extracted myelin were produced. The MyVes have an average diameter of 100–150 ​nm, negative zeta potential, spheroidal morphology, and contain lipids and the key proteins of the myelin sheath. Furthermore, they exhibit good cytocompatibility. The…

Medicine (General)QH301-705.5nanovesiclesbrain deliveryBiomedical EngineeringBioengineeringmicroglia cellsBiomaterialsWhite matterMyelinR5-920Full Length Articlemedicinewithe matterBiology (General)nanovesicles myelin nanovesicles brain delivery withe matter microglia cellsMolecular BiologyMicrogliaAverage diameterChemistryCell Biologymyelin nanovesiclesmedicine.anatomical_structureSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoMyelin sheathNeuroscienceBiotechnologyMaterials Today Bio
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Unraveling the T-B tangle in anti-CD20 multiple sclerosis therapy.

2019

Significance Multiple sclerosis (MS) is an inflammatory demyelinating disease of the central nervous system. CD8+ T cells have been strongly implicated in MS pathogenesis, but it is unclear whether myelin is a CD8+ T cell autoantigenic target in MS. This study demonstrated that while myelin-specific CD8+ T cells are present at similar frequencies in untreated MS patients and healthy subjects, the proportion of memory and CD20-expressing myelin-specific CD8+ T cells was increased in MS patients, suggesting prior antigen encounter. This activated phenotype was reversible as the memory and CD20-expressing populations of certain myelin-specific CD8+ T cells were reduced following anti-CD20 trea…

Multiple SclerosisCentral nervous systemAxonal lossDiseaseCD8-Positive T-LymphocytesCD8+ T cellsanti-CD20 therapy03 medical and health sciences0302 clinical medicineImmune systemImmunology and InflammationAntigenmedicineHumansMyelin SheathMultidisciplinarybusiness.industryMultiple sclerosisExperimental autoimmune encephalomyelitisBiological Sciencesmedicine.diseaseAntigens CD20medicine.anatomical_structureImmunizationImmunologybusinessmyelin antigen030217 neurology & neurosurgery030215 immunologyProceedings of the National Academy of Sciences of the United States of America
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Myelin Basic Protein synthesis is regulated by small non‐coding RNA 715

2012

Oligodendroglial Myelin Basic Protein (MBP) synthesis is essential for myelin formation in the central nervous system. During oligodendrocyte differentiation, MBP mRNA is kept in a translationally silenced state while intracellularly transported, until neuron-derived signals initiate localized MBP translation. Here we identify the small non-coding RNA 715 (sncRNA715) as an inhibitor of MBP translation. SncRNA715 localizes to cytoplasmic granular structures and associates with MBP mRNA transport granule components. We also detect increased levels of sncRNA715 in demyelinated chronic human multiple sclerosis lesions, which contain MBP mRNA but lack MBP protein.

Multiple SclerosisCytoplasmic GranulesBiochemistryCell LineMiceGeneticsmedicineProtein biosynthesisAnimalsHumansMRNA transportRNA MessengerMolecular BiologyMyelin SheathMessenger RNAbiologyScientific ReportsOligodendrocyte differentiationBrainRNAMyelin Basic ProteinNon-coding RNAMolecular biologyOligodendrocyteRatsMyelin basic proteinOligodendrogliamedicine.anatomical_structureGene Expression RegulationProtein Biosynthesisbiology.proteinRNA Small UntranslatedEMBO reports
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Remyelinating strategies in multiple sclerosis.

2014

Multiple sclerosis (MS) is the most common chronic inflammatory demyelinating disorder of the CNS characterized by infiltration of immune cells and progressive damage to myelin sheaths and neurons. In recent years, the importance of the neuronal compartment in the early pathology of multiple sclerosis has become increasingly clear. Direct axonal damage within the early stages of inflammation as well as neuronal injury as a result of chronic demyelination are essential factors for the development of long-term disability in patients. Viewing MS as both inflammatory and neurodegenerative has significant implications for treatment, with remyelination of denuded axons to protect neurons from dam…

Multiple SclerosisInflammationBiologyNeuroprotectionImmune systemmedicineHumansPharmacology (medical)RemyelinationDemyelinating DisorderMyelin SheathNeuronsGeneral NeuroscienceMultiple sclerosisNeurodegenerationmedicine.diseaseAxonsPathology of multiple sclerosisOligodendrogliamedicine.anatomical_structurenervous systemImmunologyNeurology (clinical)medicine.symptomNeuroscienceImmunosuppressive AgentsDemyelinating DiseasesExpert review of neurotherapeutics
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A Novel CCT5 Missense Variant Associated with Early Onset Motor Neuropathy

2020

Diseases associated with acquired or genetic defects in members of the chaperoning system (CS) are increasingly found and have been collectively termed chaperonopathies. Illustrative instances of genetic chaperonopathies involve the genes for chaperonins of Groups I (e.g., Heat shock protein 60, Hsp60) and II (e.g., Chaperonin Containing T-Complex polypeptide 1, CCT). Examples of the former are hypomyelinating leukodystrophy 4 (HLD4 or MitCHAP60) and hereditary spastic paraplegia (SPG13). A distal sensory mutilating neuropathy has been linked to a mutation [p.(His147Arg)] in subunit 5 of the CCT5 gene. Here, we describe a new possibly pathogenic variant [p.(Leu224Val)] of the same subunit b…

Mutation.Hereditary spastic paraplegiaProtein subunitchaperoning systemMutation MissenseBiologyMolecular Dynamics Simulationmedicine.disease_causeCatalysisArticleChaperoninInorganic Chemistrylcsh:ChemistryHeat shock proteinmedicineMissense mutationHumansPhysical and Theoretical Chemistrymotor neuropathyAge of OnsetGenetic variantMolecular BiologyGenelcsh:QH301-705.5SpectroscopyExome sequencingMyelin SheathGenetic chaperonopathieGeneticsMutationgenetic variantsOrganic ChemistryInfant NewbornGeneral Medicinemedicine.diseasePhenotypeComputer Science ApplicationsCCT5; chaperoning system; chaperonins; genetic chaperonopathies; genetic variants; motor neuropathy; mutationPhenotypelcsh:Biology (General)lcsh:QD1-999chaperoninsFemaleCCT5mutationHereditary Sensory and Motor Neuropathygenetic chaperonopathiesChaperonin Containing TCP-1International Journal of Molecular Sciences
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