2023
Amino-terminal proteolytic fragment of the axon growth inhibitor Nogo-A (Rtn4A) is upregulated by injury and promotes axon regeneration
Sekine Y, Wang X, Kikkawa K, Honda S, Strittmatter S. Amino-terminal proteolytic fragment of the axon growth inhibitor Nogo-A (Rtn4A) is upregulated by injury and promotes axon regeneration. Journal Of Biological Chemistry 2023, 299: 105232. PMID: 37690690, PMCID: PMC10622843, DOI: 10.1016/j.jbc.2023.105232.Peer-Reviewed Original ResearchConceptsAxon regenerationCentral nervous system injuryPersistent neurological deficitsCerebral cortical neuronsNervous system injuryNeurological deficitsSystem injuryCNS injuryCortical neuronsAmino-terminal fragmentInjuryExtracellular actionPhysiological productionNogoInhibitory proteinMiceNeuronsInhibitory domainOverexpression increasesVaried resultsProteolytic fragmentsAxotomyExpressionNogoAGene targeting
2016
Axonal branching in lateral olfactory tract is promoted by Nogo signaling
Iketani M, Yokoyama T, Kurihara Y, Strittmatter SM, Goshima Y, Kawahara N, Takei K. Axonal branching in lateral olfactory tract is promoted by Nogo signaling. Scientific Reports 2016, 6: 39586. PMID: 28000762, PMCID: PMC5175167, DOI: 10.1038/srep39586.Peer-Reviewed Original ResearchConceptsLateral olfactory tractCultured OB neuronsOB neuronsCollateral branchesAxonal branchingOlfactory bulbOlfactory tractAxonal bundlesMajor projection neuronsReceptor 1 antagonistKnockdown of NogoCollateral formationProjection neuronsPrimary axonsNogo signalingMitral cellsMiceNeuronsExpression levelsAbnormal increaseTractNogoAntagonistAxonsInhibiting poly(ADP-ribosylation) improves axon regeneration
Byrne AB, McWhirter RD, Sekine Y, Strittmatter SM, Miller DM, Hammarlund M. Inhibiting poly(ADP-ribosylation) improves axon regeneration. ELife 2016, 5: e12734. PMID: 27697151, PMCID: PMC5050021, DOI: 10.7554/elife.12734.Peer-Reviewed Original ResearchConceptsNovel intrinsic regulatorAxon regenerationDLK functionChemical inhibitionIntrinsic regulatorRegeneration pathwayPARG expressionIntrinsic regenerative potentialDLK signalingCritical functionsPARGRegenerative potentialPARP inhibitorsProteinPARPMammalian cortical neuronsRegenerationMotor neuronsGABA neuronsPolymeraseCortical neuronsSignalingRegulatorSpeciesNeurons
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 materialPatientsNeuronsThe Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus
Konopka-Anstadt JL, Mainou BA, Sutherland DM, Sekine Y, Strittmatter SM, Dermody TS. The Nogo Receptor NgR1 Mediates Infection by Mammalian Reovirus. Cell Host & Microbe 2014, 15: 681-691. PMID: 24922571, PMCID: PMC4100558, DOI: 10.1016/j.chom.2014.05.010.Peer-Reviewed Original ResearchConceptsCentral nervous systemReceptor NgR1Reovirus infectionExpression of NgR1Primary cortical neuronsDistinct cell surface moleculesJunctional adhesion molecule ASoluble NgR1Cell surface moleculesNeurotropic virusesCortical neuronsMammalian reovirusesNonsusceptible cellsNervous systemNgR1Null miceSystemic spreadInfectionIndependent receptorsMultiple receptorsReovirus replicationInitial siteReovirus virionsNeuronsReceptors
2012
Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
Um JW, Nygaard HB, Heiss JK, Kostylev MA, Stagi M, Vortmeyer A, Wisniewski T, Gunther EC, Strittmatter SM. Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons. Nature Neuroscience 2012, 15: 1227-1235. PMID: 22820466, PMCID: PMC3431439, DOI: 10.1038/nn.3178.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesAnimalsBlotting, WesternCalcium SignalingCell LineDendritic SpinesElectroencephalographyEnzyme ActivationHumansMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicNeuronsPhosphorylationProtein BindingProto-Oncogene Proteins c-fynPrPC ProteinsRatsReceptors, N-Methyl-D-AspartateSeizuresSynapses
2011
Membrane-type Matrix Metalloproteinase-3 Regulates Neuronal Responsiveness to Myelin through Nogo-66 Receptor 1 Cleavage*
Ferraro GB, Morrison CJ, Overall CM, Strittmatter SM, Fournier AE. Membrane-type Matrix Metalloproteinase-3 Regulates Neuronal Responsiveness to Myelin through Nogo-66 Receptor 1 Cleavage*. Journal Of Biological Chemistry 2011, 286: 31418-31424. PMID: 21768085, PMCID: PMC3173120, DOI: 10.1074/jbc.m111.249169.Peer-Reviewed Original ResearchConceptsMatrix metalloproteinase-3Primary neuronsMetalloproteinase-3Neuronal responsesSH-SY5Y neuroblastoma cellsMetalloproteinase-dependent mannerNeuronal responsivenessAxonal regrowthCortical neuronsNeuronal knockdownNgR1Receptor 1Neuroblastoma cellsNeuronsCell surfaceMT3-MMPMyelinSpecific metalloproteinasesGlycosylphosphatidylinositol-anchored receptorInhibitorsPhysiological consequencesCleavage fragmentsCleavage-resistant formMetalloproteinasesReceptorsA Multi-domain Fragment of Nogo-A Protein Is a Potent Inhibitor of Cortical Axon Regeneration via Nogo Receptor 1*
Huebner EA, Kim BG, Duffy PJ, Brown RH, Strittmatter SM. A Multi-domain Fragment of Nogo-A Protein Is a Potent Inhibitor of Cortical Axon Regeneration via Nogo Receptor 1*. Journal Of Biological Chemistry 2011, 286: 18026-18036. PMID: 21454605, PMCID: PMC3093876, DOI: 10.1074/jbc.m110.208108.Peer-Reviewed Original ResearchConceptsMature cortical neuronsCortical neuronsNogo-66Axon regenerationReceptor 1Central nervous system injuryDorsal root ganglion neuronsNogo-66 receptor 1Expression of PirBMature cortical culturesNogo receptor 1Nervous system injuryNogo-A proteinImmunoglobulin-like receptorsChick dorsal root ganglion neuronsFunctional recoverySystem injuryGanglion neuronsCortical culturesPredominant receptorNgR1Genetic deletionPirBCell surface receptorsNeurons
2010
Lynx for Braking Plasticity
Higley MJ, Strittmatter SM. Lynx for Braking Plasticity. Science 2010, 330: 1189-1190. PMID: 21109660, PMCID: PMC3244692, DOI: 10.1126/science.1198983.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAgingAmblyopiaAnimalsChondroitin Sulfate ProteoglycansDominance, OcularMembrane GlycoproteinsMiceMice, KnockoutNeuronal PlasticityNeuropeptidesNicotinic AntagonistsReceptors, ImmunologicReceptors, NicotinicSensory DeprivationSignal TransductionVision, OcularVisual CortexVisual PathwaysConceptsVisual cortex plasticityVisual cortex neuronsNicotinic acetylcholine receptorsJuvenile plasticityNeurological performanceCortex neuronsJuvenile brainOcular dominanceAdult miceAcetylcholine receptorsVisual cortexAdult animalsSensory inputAdultsYoung mammalsMiceMedical implicationsEyesSuch plasticityPlasticityCortexNeuronsBrainReceptorsSortilin-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 ResearchConceptsFrontotemporal lobar degenerationSerum PGRN levelsFTLD-TDP casesFTLD-TDPMicroglial cellsPGRN levelsCortical neuronsGRN haploinsufficiencyProgranulin mutationsTDP-43Causative rolePGRNUbiquitin aggregatesNeuronsSortilinMiceCell surfaceDetermine levelsPathophysiologyInjuryProgranulinCNSCentral roleDegenerationBrain
2009
Inosine Alters Gene Expression and Axonal Projections in Neurons Contralateral to a Cortical Infarct and Improves Skilled Use of the Impaired Limb
Zai L, Ferrari C, Subbaiah S, Havton LA, Coppola G, Strittmatter S, Irwin N, Geschwind D, Benowitz LI. Inosine Alters Gene Expression and Axonal Projections in Neurons Contralateral to a Cortical Infarct and Improves Skilled Use of the Impaired Limb. Journal Of Neuroscience 2009, 29: 8187-8197. PMID: 19553458, PMCID: PMC2856695, DOI: 10.1523/jneurosci.0414-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBrain InfarctionCerebral CortexComplement C1qComplement C3Disease Models, AnimalExtremitiesFunctional LateralityGene Expression RegulationHeat-Shock ProteinsImmunohistochemistryInjections, IntraventricularInosineNeuronsOligonucleotide Array Sequence AnalysisProteasome Endopeptidase ComplexRatsRats, Sprague-DawleyRecovery of FunctionRNA, MessengerTreatment OutcomeUbiquitinationConceptsUndamaged neuronsSpinal cordSynaptic bouton-like structuresImpaired limbAlters gene expressionCorticospinal tract axonsSpecific cortical areasBouton-like structuresCortical infarctsCorticospinal neuronsDenervated sideUnaffected hemisphereAxon collateralsSensorimotor cortexBrain damageBrain injuryInjury modelLaser capture microdissectionAxonal projectionsGene expressionCortical areasDenervated halfComplement cascadeNeuronsAxon growth
2006
Axonal Regeneration and Recovery From Chronic Central Nervous System Injury
Strittmatter S. Axonal Regeneration and Recovery From Chronic Central Nervous System Injury. 2006, 1165-1172. DOI: 10.1007/978-1-59259-963-9_122.Peer-Reviewed Original ResearchAxonal regenerationChronic central nervous system injuryCentral nervous system injuryNervous system injuryChronic neurological dysfunctionRecovery of functionTreatment of dysfunctionSystem injuryPersistent dysfunctionNeurological dysfunctionSpinal cordNeurological conditionsAdult brainTrophic factorsNeuronal connectivityDysfunctionNeuronsRecent scientific advancesStem cellsCellsTransplantationCordInjuryBrainRecovery
2002
Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact
Wang X, Chun SJ, Treloar H, Vartanian T, Greer CA, Strittmatter SM. Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact. Journal Of Neuroscience 2002, 22: 5505-5515. PMID: 12097502, PMCID: PMC6758202, DOI: 10.1523/jneurosci.22-13-05505.2002.Peer-Reviewed Original ResearchConceptsAdult CNSLimited axonal regenerationSpinal cord injuryNogo-66 receptorInteraction of NogoAxonal plasticityCord injurySynaptic contactsAxonal regenerationNgR proteinMyelinated fibersPostnatal neuronsLocalization of NogoMyelinated axonsAxonal growthOligodendrocyte surfacePhysiologic roleAxonsNogoProtein expressionNeuronsReceptorsInhibitory proteinInjuryCNSSmall Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth
Bonilla IE, Tanabe K, Strittmatter SM. Small Proline-Rich Repeat Protein 1A Is Expressed by Axotomized Neurons and Promotes Axonal Outgrowth. Journal Of Neuroscience 2002, 22: 1303-1315. PMID: 11850458, PMCID: PMC6757578, DOI: 10.1523/jneurosci.22-04-01303.2002.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAxonsAxotomyCell DifferentiationCell Surface ExtensionsCornified Envelope Proline-Rich ProteinsCOS CellsGanglia, SpinalMaleMembrane ProteinsMiceMice, Inbred C57BLNerve CrushNerve RegenerationNeuronsOligonucleotide Array Sequence AnalysisProtein BiosynthesisProteinsRNA, MessengerS100 ProteinsSciatic NerveSciatic NeuropathySpinal Cord InjuriesTransfectionConceptsSmall proline-rich repeat protein 1AProtein 1AAxonal outgrowthMembrane rufflesP21/WAFDifferentiation genesCDNA microarrayNerve regenerationF-actinEpithelial differentiation genesPeripheral axonal damageSciatic nerve regenerationSuccessful nerve regenerationAbility of neuronsSPRR1AGenesUninjured neuronsAxotomized neuronsRange of substratesAxonal damageSensory neuronsOutgrowthNeuronsRufflesAxonsChapter 25 Nogo and the Nogo-66 receptor
Fournier AE, GrandPré T, Gould G, Wang X, Strittmatter SM. Chapter 25 Nogo and the Nogo-66 receptor. Progress In Brain Research 2002, 137: 361-369. PMID: 12440378, DOI: 10.1016/s0079-6123(02)37027-4.Peer-Reviewed Original ResearchConceptsNogo-66 receptorAxonal regenerationNogo-66Oligodendrocyte myelin glycoproteinAxonal inhibitionAdult vertebrate CNSUnresponsive neuronsChondroitin sulfate proteoglycanCentral nervous system myelinCNS injuryReceptor expressionAxon regenerationMyelin inhibitionMyelin glycoproteinReceptor componentsNogoReceptorsSystem myelinAxonal surfaceSulfate proteoglycanNeuronsInhibitionMyelinVertebrate CNSHigh affinity
2001
Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration
Fournier A, GrandPre T, Strittmatter S. Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration. Nature 2001, 409: 341-346. PMID: 11201742, DOI: 10.1038/35053072.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAxonsBinding SitesCell DivisionCell LineChickensCloning, MolecularCOS CellsDNA, ComplementaryGene ExpressionGPI-Linked ProteinsGrowth ConesHumansMiceMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsNogo Receptor 1Protein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsConceptsNogo-66Axonal regenerationHuman CNS injuryNogo-66 receptorAxonal inhibitionAdult vertebrate CNSUnresponsive neuronsCentral nervous system myelinCNS injuryReceptor expressionAxon regenerationEnhanced recoveryGlycophosphatidylinositol-linked proteinAxonal extensionNogoNeuronsReceptorsSystem myelinAxonal surfaceInhibitionCell typesVertebrate CNSExtracellular domainHigh affinityCell morphology
2000
Dendrites go up, axons go down
Strittmatter S. Dendrites go up, axons go down. Nature 2000, 404: 557-559. PMID: 10766224, DOI: 10.1038/35007181.Peer-Reviewed Original ResearchBrain‐Derived Neurotrophic Factor Induces Excitotoxic Sensitivity in Cultured Embryonic Rat Spinal Motor Neurons Through Activation of the Phosphatidylinositol 3‐Kinase Pathway
Fryer H, Wolf D, Knox R, Strittmatter S, Pennica D, O'Leary R, Russell D, Kalb R. Brain‐Derived Neurotrophic Factor Induces Excitotoxic Sensitivity in Cultured Embryonic Rat Spinal Motor Neurons Through Activation of the Phosphatidylinositol 3‐Kinase Pathway. Journal Of Neurochemistry 2000, 74: 582-595. PMID: 10646509, DOI: 10.1046/j.1471-4159.2000.740582.x.Peer-Reviewed Original ResearchConceptsHerpes simplex virusBrain-derived neurotrophic factorNeurotrophic factorMotor neuronsGlial-derived neurotrophic factorRat spinal motor neuronsEffects of BDNFRat motor neuronsSpinal motor neuronsActivation of TrkBPI3K pathwayExcitotoxic deathNeurotrophin-3Receptor p75NTRBDNFSimplex virusIntracellular Ca2Cardiotrophin-1NeuronsReceptor-mediated cell deathK pathwayPI3KDominant negative p85 subunitTrkBCell death
1998
Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors
Takahashi T, Nakamura F, Jin Z, Kalb R, Strittmatter S. Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors. Nature Neuroscience 1998, 1: 487-493. PMID: 10196546, DOI: 10.1038/2203.Peer-Reviewed Original Research
1997
Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites
Takahashi T, Nakamura F, Strittmatter S. Neuronal and Non-Neuronal Collapsin-1 Binding Sites in Developing Chick Are Distinct from Other Semaphorin Binding Sites. Journal Of Neuroscience 1997, 17: 9183-9193. PMID: 9364065, PMCID: PMC6573609, DOI: 10.1523/jneurosci.17-23-09183.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAvian ProteinsAxonsBinding SitesCells, CulturedCentral Nervous SystemChick EmbryoDNA, ComplementaryFetal ProteinsGanglia, SpinalGlycoproteinsLungMembrane ProteinsMesodermMiceMotor NeuronsMultigene FamilyNerve Growth FactorsNerve Tissue ProteinsNeuronsNeurotrophin 3Organ SpecificityRatsRats, Sprague-DawleyReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3AConceptsFusion proteinBinding sitesGrowth conesDRG neuronsNon-neuronal tissuesExtracellular proteinsF fusion proteinSemaphorin familyDRG growth conesProteinLow nanomolar affinityMajor blood vesselsLigand familyBrainstem neuronsSympathetic neuronsNanomolar affinityNervous systemAxonal pathsBiological activityBlood vesselsNeuronsFamilySitesMesenchymeSemaphorins