Search results for "Myelin proteolipid protein"

showing 8 items of 8 documents

A critical role for the cholesterol-associated proteolipids PLP and M6B in myelination of the central nervous system.

2012

The formation of central nervous system myelin by oligodendrocytes requires sterol synthesis and is associated with a significant enrichment of cholesterol in the myelin membrane. However, it is unknown how oligodendrocytes concentrate cholesterol above the level found in nonmyelin membranes. Here, we demonstrate a critical role for proteolipids in cholesterol accumulation. Mice lacking the most abundant myelin protein, proteolipid protein (PLP), are fully myelinated, but PLP-deficient myelin exhibits a reduced cholesterol content. We therefore hypothesized that "high cholesterol" is not essential in the myelin sheath itself but is required for an earlier step of myelin biogenesis that is f…

Central Nervous SystemProteolipid protein 1Nerve Tissue ProteinsBiologyCell Line03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compoundMyelinMice0302 clinical medicineimmune system diseasesmedicineEvoked Potentials Auditory Brain StemAnimalsMyelin Proteolipid ProteinMyelin Sheath030304 developmental biology0303 health sciencesMembrane GlycoproteinsCholesterolProteolipidsLeukodystrophyPelizaeus–Merzbacher diseasemedicine.diseaseOligodendrocytenervous system diseasesMyelin proteolipid proteinmedicine.anatomical_structureCholesterolnervous systemNeurologychemistryBiochemistryEvoked Potentials Visuallipids (amino acids peptides and proteins)Vomeronasal Organ030217 neurology & neurosurgeryGlia
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Reversible neural stem cell niche dysfunction in a model of multiple sclerosis

2011

Objective The subventricular zone (SVZ) of the brain constitutes a niche for neural stem and progenitor cells that can initiate repair after central nervous system (CNS) injury. In a relapsing-remitting model of experimental autoimmune encephalomyelitis (EAE), the neural stem cells (NSCs) become activated and initiate regeneration during acute disease, but lose this ability during the chronic phases of disease. We hypothesized that chronic microglia activation contributes to the failure of the NSC repair potential in the SVZ. Methods Using bromodeoxyuridine injections at different time points during EAE, we quantified the number of proliferating and differentiating progenitors, and evaluate…

Encephalomyelitis Autoimmune ExperimentalMultiple SclerosisTime FactorsSubventricular zoneCell CountMinocyclineBiologyArticleMiceSOX2Microscopy Electron TransmissionNeural Stem CellsCell MovementmedicineSecondary PreventionAnimalsProgenitor cellStem Cell NicheMyelin Proteolipid ProteinCell ProliferationMicrogliaExperimental autoimmune encephalomyelitismedicine.diseaseNeural stem cellOligodendrocytePeptide FragmentsAnti-Bacterial Agentsnervous system diseasesDisease Models AnimalOligodendrogliamedicine.anatomical_structureNeurologyBromodeoxyuridinenervous systemNeurology (clinical)MicrogliaStem cellNeuroscience
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L-Selectin-deficient SJL and C57BL/6 mice are not resistant to experimental autoimmune encephalomyelitis

2008

L-selectin has been suggested to play a role in the pathogenesis of experimental autoimmune encephalomyelitis (EAE), an animal model of multiple sclerosis. Here we demonstrate that L-selectin(-/-) SJL mice are susceptible to proteolipid protein (PLP)-induced EAE because the compromised antigen-specific T cell proliferation in peripheral lymph nodes is fully compensated by the T cell response raised in their spleen. Transfer of PLP-specific T cells into syngeneic recipients induced EAE independent of the presence or absence of L-selectin on PLP-specific T cells or in the recipient. Leukocyte infiltration into the central nervous system parenchyma was detectable independent of the mode of dis…

Encephalomyelitis Autoimmune ExperimentalProteolipid protein 1OvalbuminT cellImmunologySpleenPathogenesisMice03 medical and health sciencesMyelin0302 clinical medicineCell Movementimmune system diseasesmedicineAnimalsImmunology and AllergyL-SelectinMyelin Proteolipid Protein030304 developmental biologyInflammation0303 health sciencesbiologyExperimental autoimmune encephalomyelitismedicine.diseaseAdoptive TransferOligodendrocytenervous system diseases3. Good healthMice Inbred C57BLmedicine.anatomical_structureImmunologybiology.proteinFemaleL-selectinSpleen030215 immunologyEuropean Journal of Immunology
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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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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling.

2008

The central nervous system myelin sheath is a multilayered specialized membrane with compacted and non-compacted domains of defined protein composition. How oligodendrocytes regulate myelin membrane trafficking and establish membrane domains during myelination is largely unknown. Oligodendroglial cells respond to neuronal signals by adjusting the relative levels of endocytosis and exocytosis of the major myelin protein, proteolipid protein (PLP). We investigated whether endocytic trafficking is common to myelin proteins and analyzed the endocytic fates of proteins with distinct myelin subdomain localization. Interestingly, we found that PLP, myelin-associated glycoprotein (MAG) and myelin-o…

Proteolipid protein 1Endocytic cycleCell MembraneEndocytic recyclingCell BiologyBiologyEndocytosisExocytosisEndocytosisCell biologyMyelin oligodendrocyte glycoproteinMyelinMiceMyelin-Associated GlycoproteinOligodendrogliamedicine.anatomical_structurenervous systemimmune system diseasesCompact myelinmedicinebiology.proteinAnimalsMyelin-Oligodendrocyte GlycoproteinMyelin Proteolipid ProteinMyelin ProteinsJournal of cell science
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Oligodendrocytes secrete exosomes containing major myelin and stress-protective proteins: Trophic support for axons?

2007

Oligodendrocytes synthesize the CNS myelin sheath by enwrapping axonal segments with elongations of their plasma membrane. Spatial and temporal control of membrane traffic is a prerequisite for proper myelin formation. The major myelin proteolipid protein (PLP) accumulates in late endosomal storage compartments and multivesicular bodies (MVBs). Fusion of MVBs with the plasma membrane results in the release of the intralumenal vesicles, termed exosomes, into the extracellular space. Here, we show that cultured oligodendrocytes secrete exosomes carrying major amounts of PLP and 2'3'-cyclic-nucleotide-phosphodiesterase (CNP). These exosomes migrated at the characteristic density of 1.10-1.14 g…

Proteolipid protein 1EndosomeClinical BiochemistryBiologyExosomeMicrovesiclesMyelin proteolipid proteinCell biologyMyelin oligodendrocyte glycoproteinMyelin basic proteinMyelinmedicine.anatomical_structurenervous systemBiochemistrybiology.proteinmedicineProteomics. Clinical applications
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Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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