2019
Limiting Neuronal Nogo Receptor 1 Signaling during Experimental Autoimmune Encephalomyelitis Preserves Axonal Transport and Abrogates Inflammatory Demyelination
Lee JY, Kim MJ, Thomas S, Oorschot V, Ramm G, Aui PM, Sekine Y, Deliyanti D, Wilkinson-Berka J, Niego B, Harvey AR, Theotokis P, McLean C, Strittmatter SM, Petratos S. Limiting Neuronal Nogo Receptor 1 Signaling during Experimental Autoimmune Encephalomyelitis Preserves Axonal Transport and Abrogates Inflammatory Demyelination. Journal Of Neuroscience 2019, 39: 5562-5580. PMID: 31061088, PMCID: PMC6616297, DOI: 10.1523/jneurosci.1760-18.2019.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAged, 80 and overAnimalsAxonal TransportAxonsCells, CulturedEncephalomyelitis, Autoimmune, ExperimentalFemaleHumansIntercellular Signaling Peptides and ProteinsKinesinsMaleMiceMice, Inbred C57BLMiddle AgedMyelin SheathNerve Tissue ProteinsNogo Receptor 1Retinal Ganglion CellsSignal TransductionConceptsExperimental autoimmune encephalomyelitisCollapsin response mediator protein 2Optic nerveAxonal degenerationMultiple sclerosisAxonal vesicular transportAutoimmune encephalomyelitisInflammatory demyelinationAxonal integritySeverity of EAECre deletionAxonal transportRetinal ganglion cell axonsAxonal motor proteinsEAE-induced miceImmune-mediated destructionProgressive multiple sclerosisNeuron-specific deletionNogo receptor 1Ganglion cell axonsAnterograde transportFlx/Response mediator protein 2Adeno-associated virus serotype 2Phosphorylation of CRMP2Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma
Sekine Y, Algarate PT, Cafferty WBJ, Strittmatter SM. Plexina2 and CRMP2 Signaling Complex Is Activated by Nogo-A-Liganded Ngr1 to Restrict Corticospinal Axon Sprouting after Trauma. Journal Of Neuroscience 2019, 39: 3204-3216. PMID: 30804090, PMCID: PMC6788813, DOI: 10.1523/jneurosci.2996-18.2019.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsChlorocebus aethiopsCOS CellsIntercellular Signaling Peptides and ProteinsMiceMice, KnockoutMotor ActivityNerve RegenerationNerve Tissue ProteinsNeuronsNogo ProteinsNogo Receptor 1Pyramidal TractsReceptors, Cell SurfaceRecovery of FunctionSpinal Cord InjuriesConceptsCNS traumaNeural repairMouse cervical spinal cordSpinal cord traumaCervical spinal cordNon-neuronal cellsInteraction of NogoAxon growth inhibitionAxonal guidance mechanismsNeurological recoveryAxonal sproutingCNS pathwaysCord traumaFunctional recoveryAxon sproutingSpinal cordNgR1 functionUnilateral pyramidotomyAxon regenerationAdult traumaNgR1TraumaAxon growthNogoCytoplasmic mediators
2017
Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice
Klein ZA, Takahashi H, Ma M, Stagi M, Zhou M, Lam TT, Strittmatter SM. Loss of TMEM106B Ameliorates Lysosomal and Frontotemporal Dementia-Related Phenotypes in Progranulin-Deficient Mice. Neuron 2017, 95: 281-296.e6. PMID: 28728022, PMCID: PMC5558861, DOI: 10.1016/j.neuron.2017.06.026.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCells, CulturedFrontotemporal DementiaGranulinsIntercellular Signaling Peptides and ProteinsLysosomesMice, KnockoutMutationNeuronsPhenotypePolymorphism, Single NucleotideProgranulinsProteomicsConceptsLysosomal protein levelsFrontotemporal lobar degenerationProtein levelsMultiple lysosomal enzymesLysosomal enzymesV0 subunitsTMEM106B geneProteomic analysisProgranulin-deficient miceExtent of neurodegenerationCommon neurodegenerative disorderLysosomal acidificationLysosomal enzyme levelsProtein 1Microglial accumulationRisk modificationFTLD riskBehavioral abnormalitiesRetinal degenerationNeurodegenerative disordersFrontotemporal dementiaGRNTMEM106BFunctional relationshipEnzyme levelsOpposing effects of progranulin deficiency on amyloid and tau pathologies via microglial TYROBP network
Takahashi H, Klein ZA, Bhagat SM, Kaufman AC, Kostylev MA, Ikezu T, Strittmatter SM, For the Alzheimer’s Disease Neuroimaging Initiative. Opposing effects of progranulin deficiency on amyloid and tau pathologies via microglial TYROBP network. Acta Neuropathologica 2017, 133: 785-807. PMID: 28070672, PMCID: PMC5391267, DOI: 10.1007/s00401-017-1668-z.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloidogenic ProteinsAmyloidosisAnimalsDisease Models, AnimalFrontotemporal Lobar DegenerationGranulinsHumansIntercellular Signaling Peptides and ProteinsMiceMice, TransgenicMicrogliaPlaque, AmyloidProgranulinsTau ProteinsConceptsAPP/PS1 micePS1 micePGRN deficiencyAlzheimer's diseaseAD risk variantsCerebrospinal fluid Aβ levelsLoss of progranulinMicroglial Aβ phagocytosisCSF tau levelsFrontotemporal lobar degenerationRisk variantsAPPswe/Aβ phagocytosisNeuronal injuryAβ levelsAβ pathologyCerebral amyloidosisAxonal dystrophyTau pathologyTau levelsComplement depositionPGRN levelsAD pathophysiologyAmyloid imagingProgranulin deficiency
2014
Progressive retinal degeneration and accumulation of autofluorescent lipopigments in Progranulin deficient mice
Hafler BP, Klein ZA, Zhou Z, Strittmatter SM. Progressive retinal degeneration and accumulation of autofluorescent lipopigments in Progranulin deficient mice. Brain Research 2014, 1588: 168-174. PMID: 25234724, PMCID: PMC4254024, DOI: 10.1016/j.brainres.2014.09.023.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedElectroretinographyGranulinsImmunohistochemistryIntercellular Signaling Peptides and ProteinsMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalNeuronal Ceroid-LipofuscinosesOptical ImagingPhotoreceptor Cells, VertebrateProgranulinsRetinal DegenerationRetinal Ganglion CellsConceptsProgranulin-deficient miceNeuronal ceroid lipofuscinosisAdult-onset neuronal ceroid lipofuscinosisDeficient miceRetinal degenerationCeroid lipofuscinosisRetinal ganglion cellsCentral nervous systemAutofluorescent storage materialMotor dysfunctionNeuropathological analysisGanglion cellsVision lossOptic atrophyEarly deathAutofluorescent lipopigmentsClinical observationsNervous systemDegenerative pathologyMiceDegenerationHomozygous mutationAutofluorescent materialPatientsNeurons
2012
Limiting multiple sclerosis related axonopathy by blocking Nogo receptor and CRMP-2 phosphorylation
Petratos S, Ozturk E, Azari MF, Kenny R, Lee JY, Magee KA, Harvey AR, McDonald C, Taghian K, Moussa L, Aui P, Siatskas C, Litwak S, Fehlings MG, Strittmatter SM, Bernard CC. Limiting multiple sclerosis related axonopathy by blocking Nogo receptor and CRMP-2 phosphorylation. Brain 2012, 135: 1794-1818. PMID: 22544872, PMCID: PMC3589918, DOI: 10.1093/brain/aws100.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnalysis of VarianceAnimalsAntibodiesAxonsCD3 ComplexCell Line, TumorDemyelinating DiseasesDisease Models, AnimalEncephalomyelitis, Autoimmune, ExperimentalFemaleGene Expression RegulationGlycoproteinsGPI-Linked ProteinsGreen Fluorescent ProteinsHumansImmunoprecipitationIntercellular Signaling Peptides and ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutMiddle AgedMultiple SclerosisMutationMyelin ProteinsMyelin-Oligodendrocyte GlycoproteinNerve DegenerationNerve Tissue ProteinsNeuroblastomaNeurofilament ProteinsNogo Receptor 1Optic NervePeptide FragmentsPhosphorylationReceptors, Cell SurfaceRetinal Ganglion CellsSeverity of Illness IndexSilver StainingSpinal CordTau ProteinsTime FactorsTransduction, GeneticTubulinConceptsExperimental autoimmune encephalomyelitisAutoimmune encephalomyelitisMyelin oligodendrocyte glycoproteinMultiple sclerosisAxonal degenerationSpinal cordChronic active multiple sclerosis lesionsOptic nerve axonal degenerationNogo-66 receptor 1CRMP-2Axonal growth inhibitorsCollapsin response mediator protein 2Improved clinical outcomesSpinal cord neuronsRetinal ganglion cellsResponse mediator protein 2Central nervous systemViable therapeutic targetAdeno-associated viral vectorMultiple sclerosis lesionsClinical outcomesOptic nerveCord neuronsOligodendrocyte glycoproteinGanglion cells
2010
Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin
Hu F, Padukkavidana T, Vægter CB, Brady OA, Zheng Y, Mackenzie IR, Feldman HH, Nykjaer A, Strittmatter SM. Sortilin-Mediated Endocytosis Determines Levels of the Frontotemporal Dementia Protein, Progranulin. Neuron 2010, 68: 654-667. PMID: 21092856, PMCID: PMC2990962, DOI: 10.1016/j.neuron.2010.09.034.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAnimalsCells, CulturedChlorocebus aethiopsCOS CellsEndocytosisFrontotemporal DementiaGranulinsHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMice, KnockoutProgranulinsProtein BindingRatsConceptsFrontotemporal lobar degenerationSerum PGRN levelsFTLD-TDP casesFTLD-TDPMicroglial cellsPGRN levelsCortical neuronsGRN haploinsufficiencyProgranulin mutationsTDP-43Causative rolePGRNUbiquitin aggregatesNeuronsSortilinMiceCell surfaceDetermine levelsPathophysiologyInjuryProgranulinCNSCentral roleDegenerationBrain
2001
Semaphorin-mediated axonal guidance via Rho-related G proteins
Liu B, Strittmatter S. Semaphorin-mediated axonal guidance via Rho-related G proteins. Current Opinion In Cell Biology 2001, 13: 619-626. PMID: 11544032, DOI: 10.1016/s0955-0674(00)00260-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsCarrier ProteinsGrowth ConesGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntercellular Signaling Peptides and ProteinsModels, NeurologicalNerve Tissue ProteinsNeuronsNeuropilin-1Receptors, Cell SurfaceRho GTP-Binding Proteins
2000
Molecular basis of semaphorin‐mediated axon guidance
Nakamura F, Kalb R, Strittmatter S. Molecular basis of semaphorin‐mediated axon guidance. Developmental Neurobiology 2000, 44: 219-229. PMID: 10934324, DOI: 10.1002/1097-4695(200008)44:2<219::aid-neu11>3.0.co;2-w.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsCell Adhesion MoleculesGene ExpressionGrowth ConesIntercellular Signaling Peptides and ProteinsNerve Tissue ProteinsNeuropilin-1Semaphorin-3AConceptsGrowth cone collapseSemaphorin guidance cuesMonomeric G proteinsSignal transduction cascadeGuidance cuesAxon guidance eventsCone collapseGrowth cone motilityCaenorhabditis elegansActin cytoskeletonTransmembrane proteinFilopodial tipsNeuropilin-1Transduction cascadeMolecular basisComplex interactsIntracellular domainPrototypic memberGrowth cone turningRac1 activityAxon guidanceG proteinsRepulsive guidance cuesNeuronal proteinsAxonal guidance
1997
Brain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase
Wang L, Strittmatter S. Brain CRMP Forms Heterotetramers Similar to Liver Dihydropyrimidinase. Journal Of Neurochemistry 1997, 69: 2261-2269. PMID: 9375656, DOI: 10.1046/j.1471-4159.1997.69062261.x.Peer-Reviewed Original ResearchMeSH KeywordsAmidohydrolasesAnimalsBrainCattleHumansIntercellular Signaling Peptides and ProteinsLiverMiceNerve Tissue ProteinsPolymersRatsSemaphorin-3AA novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse
Goshima Y, Kawakami T, Hori H, Sugiyama Y, Takasawa S, Hashimoto Y, Kagoshima‐Maezono M, Takenaka T, Misu Y, Strittmatter S. A novel action of collapsin: Collapsin‐1 increases antero‐ and retrograde axoplasmic transport independently of growth cone collapse. Developmental Neurobiology 1997, 33: 316-328. PMID: 9298768, DOI: 10.1002/(sici)1097-4695(199709)33:3<316::aid-neu9>3.0.co;2-4.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonal TransportCells, CulturedDose-Response Relationship, DrugGanglia, SpinalGlycoproteinsGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMyelin ProteinsNerve Growth FactorsNeuritesOrganellesPeptidesPertussis ToxinSemaphorin-3AVirulence Factors, BordetellaWasp Venoms
1996
A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System
Wang LH, Strittmatter SM. A Family of Rat CRMP Genes Is Differentially Expressed in the Nervous System. Journal Of Neuroscience 1996, 16: 6197-6207. PMID: 8815901, PMCID: PMC6579169, DOI: 10.1523/jneurosci.16-19-06197.1996.Peer-Reviewed Original ResearchMeSH KeywordsAgingAmino Acid SequenceAnimalsAnimals, NewbornEmbryonic and Fetal DevelopmentGanglia, SensoryGanglia, SympatheticGene ExpressionHumansIntercellular Signaling Peptides and ProteinsIsomerismMolecular Sequence DataMultigene FamilyNerve Tissue ProteinsNervous System Physiological PhenomenaProsencephalonRatsSemaphorin-3ASpinal Cord
1995
Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33
Goshima Y, Nakamura F, Strittmatter P, Strittmatter S. Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. Nature 1995, 376: 509-514. PMID: 7637782, DOI: 10.1038/376509a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCaenorhabditis elegans ProteinsCell LineCell MembraneChick EmbryoGanglia, SpinalGlycoproteinsGTP-Binding ProteinsHelminth ProteinsIntercellular Signaling Peptides and ProteinsMolecular Sequence DataNerve Growth FactorsNerve Tissue ProteinsNeuritesNeuronsOocytesRecombinant Fusion ProteinsSemaphorin-3ASignal TransductionVirulence Factors, BordetellaXenopus laevisConceptsGrowth cone collapseDorsal root ganglion neuronsCollapsin response mediator proteinsCone collapseXenopus laevis oocyte expression systemChick nervous systemGanglion neuronsNervous systemOocyte expression systemUNC-33Inward currentsNeuronal proteinsAxonal pathfindingNeural developmentX. laevis oocytesGrowth conesLaevis oocytesIntracellular proteinsHeterotrimeric GTPMediator proteinsProteinIntracellular componentsNeurons
1994
Activated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell
Strittmatter S, Fishman M, Zhu X. Activated mutants of the alpha subunit of G(o) promote an increased number of neurites per cell. Journal Of Neuroscience 1994, 14: 2327-2338. PMID: 8158271, PMCID: PMC6577129, DOI: 10.1523/jneurosci.14-04-02327.1994.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCell LineChlorocebus aethiopsDNA PrimersDose-Response Relationship, DrugGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedNeuritesNeuroblastomaPC12 CellsPeptidesPertussis ToxinPoint MutationTransfectionTumor Cells, CulturedVirulence Factors, BordetellaWasp VenomsConceptsAlpha oNumber of neuritesPertussis toxin-sensitive G proteinToxin-sensitive G proteinGrowth conesAlpha subunitG proteinsNeurite outgrowthTotal neurite lengthN1E-115 cellsAlpha i2Activated alpha subunitNeuroblastoma cellsNeurite numberNeurite lengthNeuronal growth conesAlpha sOncogenic mutationsActivation stateO mutantsActivationNeuritesCellsPoint mutationsSubunits
1993
Mediation by G Proteins of Signals That Cause Collapse of Growth Cones
Igarashi M, Strittmatter S, Vartanian T, Fishman M. Mediation by G Proteins of Signals That Cause Collapse of Growth Cones. Science 1993, 259: 77-79. PMID: 8418498, DOI: 10.1126/science.8418498.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCell MembraneChick EmbryoGanglia, SpinalGTP-Binding ProteinsIntercellular Signaling Peptides and ProteinsMyelin ProteinsNeuronsOrgan Culture TechniquesPeptidesPertussis ToxinSignal TransductionVirulence Factors, BordetellaWasp Venoms