2009
Ibuprofen Enhances Recovery from Spinal Cord Injury by Limiting Tissue Loss and Stimulating Axonal Growth
Wang X, Budel S, Baughman K, Gould G, Song KH, Strittmatter SM. Ibuprofen Enhances Recovery from Spinal Cord Injury by Limiting Tissue Loss and Stimulating Axonal Growth. Journal Of Neurotrauma 2009, 26: 81-95. PMID: 19125588, PMCID: PMC2913782, DOI: 10.1089/neu.2007.0464.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory Agents, Non-SteroidalAxotomyChick EmbryoDisease Models, AnimalEfferent PathwaysFemaleGrowth ConesGrowth InhibitorsIbuprofenMiceNerve RegenerationNIH 3T3 CellsPyramidal TractsRaphe NucleiRatsRats, Sprague-DawleyRhoA GTP-Binding ProteinSpinal CordSpinal Cord InjuriesConceptsSpinal cord injuryAxonal sproutingCord injuryAxonal regenerationAxon regenerationNonsteroidal anti-inflammatory drugsComplete spinal cord transectionWeight-bearing statusSpinal cord contusionRecovery of ratsSpinal cord traumaTreatment of miceAdministration of ibuprofenSpinal cord transectionAnti-inflammatory drugsCorticospinal axon regenerationAction of ibuprofenRaphespinal axonsSpinal contusionCord contusionCord traumaMicroglial reactionChondroitin sulfate proteoglycanCord transectionCorticospinal fibers
2008
Genetic Variants of Nogo-66 Receptor with Possible Association to Schizophrenia Block Myelin Inhibition of Axon Growth
Budel S, Padukkavidana T, Liu BP, Feng Z, Hu F, Johnson S, Lauren J, Park JH, McGee AW, Liao J, Stillman A, Kim JE, Yang BZ, Sodi S, Gelernter J, Zhao H, Hisama F, Arnsten AF, Strittmatter SM. Genetic Variants of Nogo-66 Receptor with Possible Association to Schizophrenia Block Myelin Inhibition of Axon Growth. Journal Of Neuroscience 2008, 28: 13161-13172. PMID: 19052207, PMCID: PMC2892845, DOI: 10.1523/jneurosci.3828-08.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainChick EmbryoChlorocebus aethiopsChromosome MappingCodonCOS CellsFemaleGenetic Predisposition to DiseaseGPI-Linked ProteinsGrowth ConesGrowth InhibitorsHumansMaleMiceMice, KnockoutMutationMyelin ProteinsNerve Fibers, MyelinatedNeurogenesisNeuronal PlasticityNogo Receptor 1Organ Culture TechniquesRatsReceptors, Cell SurfaceSchizophreniaConceptsMyelin inhibitionNogo-66 receptorCase-control analysisMyelin-specific genesAxonal sproutingMyelin signalGenetic predispositionAxon inhibitionNeuronal culturesPossible associationReceptor 1Disease riskAxon growthSchizophreniaAxonal proteinsPotential endophenotypeMemory functionGenetic variantsDysfunctional proteinsInhibitionSchizophrenia susceptibilityDominant negativeProtein exhibitCandidate genesChromosome 22q11Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein
Schmidt EF, Shim SO, Strittmatter SM. Release of MICAL Autoinhibition by Semaphorin-Plexin Signaling Promotes Interaction with Collapsin Response Mediator Protein. Journal Of Neuroscience 2008, 28: 2287-2297. PMID: 18305261, PMCID: PMC2846290, DOI: 10.1523/jneurosci.5646-07.2008.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell Line, TransformedChick EmbryoCytoskeletal ProteinsFlavin-Adenine DinucleotideGanglia, SpinalGenetic VectorsHIVHumansImmunoprecipitationIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMembrane GlycoproteinsMicrofilament ProteinsMixed Function OxygenasesMutationNerve Tissue ProteinsNeuritesNeuronsPeptide FragmentsProtein BindingSemaphorin-3ASemaphorinsSignal TransductionTransfectionConceptsCollapsin response mediator proteinsMediator proteinsCytoplasmic proteinsEnzymatic domainsCatalytic domainPlexin functionPlexin receptorsTerminal domainMICALPromotes interactionAxon guidanceNeuronal developmentAxonal guidanceEnzymatic activityProteinAutoinhibitionDomainPlexinsSignalingSemaphorinsActivatorAssociatesInteractionActivityActivationThe N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism
Hu F, Strittmatter SM. The N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism. Journal Of Neuroscience 2008, 28: 1262-1269. PMID: 18234903, PMCID: PMC2856844, DOI: 10.1523/jneurosci.1068-07.2008.Peer-Reviewed Original ResearchConceptsCell adhesionFocal adhesion kinase activationN-terminal domainAxonal outgrowthInhibits cell adhesionAxonal growth conesCNS axon regenerationKinase activationCertain integrinsIntegrin activatorIntegrin beta1Widespread expressionExtracellular matrixSecond domainAlpha5 integrinUnknown mechanismIntegrinsGrowth conesNogo-A proteinCell linesAlpha6 integrinNogo-66 receptorAxonal growthAdult brainOutgrowth
2007
Toll-Like Receptor 3 Is a Potent Negative Regulator of Axonal Growth in Mammals
Cameron JS, Alexopoulou L, Sloane JA, DiBernardo AB, Ma Y, Kosaras B, Flavell R, Strittmatter SM, Volpe J, Sidman R, Vartanian T. Toll-Like Receptor 3 Is a Potent Negative Regulator of Axonal Growth in Mammals. Journal Of Neuroscience 2007, 27: 13033-13041. PMID: 18032677, PMCID: PMC4313565, DOI: 10.1523/jneurosci.4290-06.2007.Peer-Reviewed Original ResearchConceptsToll-like receptor 3Functional toll-like receptor 3Poly IActivation of TLR3Nervous systemInnate immunityReceptor 3Pattern recognition receptor functionAxonal growthDorsal root gangliaFunction of TLRsToll-like receptorsPeripheral nervous systemMammalian Toll-like receptorsPattern recognition receptorsViral double-stranded RNAClasses of receptorsNuclear factor kappaB.Sensorimotor deficitsRoot gangliaNeonatal miceNeurodegenerative effectsGrowth cone collapseCNS regenerationRecognition receptors
2006
RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors
Togashi H, Schmidt EF, Strittmatter SM. RanBPM Contributes to Semaphorin3A Signaling through Plexin-A Receptors. Journal Of Neuroscience 2006, 26: 4961-4969. PMID: 16672672, PMCID: PMC2846289, DOI: 10.1523/jneurosci.0704-06.2006.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell Adhesion MoleculesCell DeathCell SizeCells, CulturedChick EmbryoCloning, MolecularCricetinaeCricetulusCytoskeletal ProteinsDose-Response Relationship, DrugDrug InteractionsEnzyme InhibitorsGanglia, SpinalGene ExpressionGreen Fluorescent ProteinsHumansImmunoprecipitationIn Situ Nick-End LabelingNerve Tissue ProteinsNeuritesNeuronsNeuropilin-1Nuclear ProteinsRan GTP-Binding ProteinSemaphorin-3ASignal TransductionTranscription Factor AP-1TransfectionTwo-Hybrid System TechniquesConceptsPlexin-A1Collapsin response mediator proteinsNervous system developmentReceptor complex consistingSignal transductionRanBPMMediator proteinsMicrotubule functionCell spreadingComplex consistingAxonal guidanceNeuronal cellsAxonal guidance cuesProteinGuidance cuesPlexinsAxonal outgrowthExpressionSema3ATransductionReceptorsDomainOverexpressionNeuropilinsSystem development
2005
Effect of combined treatment with methylprednisolone and soluble Nogo‐66 receptor after rat spinal cord injury
Ji B, Li M, Budel S, Pepinsky RB, Walus L, Engber TM, Strittmatter SM, Relton JK. Effect of combined treatment with methylprednisolone and soluble Nogo‐66 receptor after rat spinal cord injury. European Journal Of Neuroscience 2005, 22: 587-594. PMID: 16101740, PMCID: PMC2846292, DOI: 10.1111/j.1460-9568.2005.04241.x.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsAxonsBehavior, AnimalBiotinCells, CulturedChick EmbryoDextransDisease Models, AnimalDose-Response Relationship, DrugDrug InteractionsDrug Therapy, CombinationExploratory BehaviorFemaleGanglia, SpinalGPI-Linked ProteinsImmunoglobulin GLaminectomyMethylprednisoloneMyelin ProteinsMyelin SheathNerve RegenerationNeuronsNogo Receptor 1Pyramidal TractsRatsRats, Long-EvansReceptors, Cell SurfaceReceptors, PeptideRecombinant ProteinsRecovery of FunctionSpinal Cord InjuriesConceptsSpinal cord injuryCord injuryRat spinal cord injuryMP treatmentAdult central nervous systemThoracic dorsal hemisectionNovel experimental therapiesCorticospinal tract axonsRecovery of functionNogo-66 receptorNumber of axonsCentral nervous systemGrowth inhibitory effectsDorsal hemisectionBBB scoresAxonal sproutingFunctional recoveryBresnahan (BBB) scoringAxonal regenerationMotor neuronsExperimental therapiesMethylprednisoloneSynthetic glucocorticoidNervous systemAxonal growthNogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist
Hu F, Liu BP, Budel S, Liao J, Chin J, Fournier A, Strittmatter SM. Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist. Journal Of Neuroscience 2005, 25: 5298-5304. PMID: 15930377, PMCID: PMC2855126, DOI: 10.1523/jneurosci.5235-04.2005.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAxonsBinding SitesCell LineChick EmbryoChlorocebus aethiopsGlutathione TransferaseGPI-Linked ProteinsHumansIn Vitro TechniquesLigandsMiceMyelin ProteinsNogo ProteinsNogo Receptor 1PeptidesProtein IsoformsProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion Proteins
2004
Neogenin mediates the action of repulsive guidance molecule
Rajagopalan S, Deitinghoff L, Davis D, Conrad S, Skutella T, Chedotal A, Mueller BK, Strittmatter SM. Neogenin mediates the action of repulsive guidance molecule. Nature Cell Biology 2004, 6: 756-762. PMID: 15258590, DOI: 10.1038/ncb1156.Peer-Reviewed Original ResearchConceptsRepulsive guidance moleculeRetinal ganglion cell axonsGuidance moleculesGanglion cell axonsDorsal root ganglion axonsTemporal retinal axonsVisual map formationReceptor mechanismsCell axonsNeogenin expressionRetinal axonsGanglion axonsAxonal responsivenessOptic tectumChick retinaNeogeninSub-nanomolar affinityAxonsAxonal guidanceNeogenin functionsResponsive stateNeural tubeMap formationExpressionRetinaRGM and its receptor neogenin regulate neuronal survival
Matsunaga E, Tauszig-Delamasure S, Monnier PP, Mueller BK, Strittmatter SM, Mehlen P, Chédotal A. RGM and its receptor neogenin regulate neuronal survival. Nature Cell Biology 2004, 6: 749-755. PMID: 15258591, DOI: 10.1038/ncb1157.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAvian ProteinsCaspasesCell SurvivalCells, CulturedChick EmbryoChickensDown-RegulationEnzyme ActivationGene Expression Regulation, DevelopmentalGreen Fluorescent ProteinsImmunohistochemistryIn Situ HybridizationLuminescent ProteinsMembrane ProteinsMutagenesis, Site-DirectedNeuronsRatsRNA, Small InterferingConceptsRepulsive guidance moleculeNeural tubePro-apoptotic activityAxon guidance proteinCytoplasmic domainImmortalized neuronal cellsGene transfer technologyDependence receptorsCell deathGuidance proteinsNeuronal cellsNeogenin receptorGuidance moleculesNeuronal survivalRetinal axonsChick embryosNeogeninReceptor neogeninExpressionCaspasesReceptorsTransfer technologyEmbryosProteinApoptosis
2003
Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling
Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling. The EMBO Journal 2003, 23: 9-22. PMID: 14685275, PMCID: PMC1271659, DOI: 10.1038/sj.emboj.7600021.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsCell Adhesion MoleculesCell LineChick EmbryoChlorocebus aethiopsCOS CellsCrystallography, X-RayGanglia, SpinalHumansHydrogen BondingImmunophilinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3ASequence Homology, Amino AcidSignal TransductionStructure-Activity RelationshipConceptsCollapsin response mediator proteinsStructure-based mutagenesisCOS-7 cellsSurface-exposed residuesTetrameric assemblyPhysical complexAxonal specificationMediator proteinsStructural basisFunctional domainsAlanine substitutionsActive proteinCytosolic phosphoproteinNeuronal differentiationAxonal repulsionAxonal guidanceReceptor componentsProteinStructural viewX-ray crystal structureCRMP1Sema3ACell contractionCellsNP1Rho Kinase Inhibition Enhances Axonal Regeneration in the Injured CNS
Fournier AE, Takizawa BT, Strittmatter SM. Rho Kinase Inhibition Enhances Axonal Regeneration in the Injured CNS. Journal Of Neuroscience 2003, 23: 1416-1423. PMID: 12598630, PMCID: PMC6742251, DOI: 10.1523/jneurosci.23-04-01416.2003.Peer-Reviewed Original ResearchMeSH KeywordsADP Ribose TransferasesAmidesAnimalsAxonsBotulinum ToxinsCells, CulturedChick EmbryoEnzyme InhibitorsFemaleGanglia, SpinalIntracellular Signaling Peptides and ProteinsMotor ActivityMyelin ProteinsNerve RegenerationNeuritesNogo ProteinsPC12 CellsProtein Serine-Threonine KinasesPyridinesRatsRats, Sprague-DawleyRho GTP-Binding ProteinsRho-Associated KinasesSpinal Cord InjuriesConceptsAxonal regenerationAdult ratsNeurite outgrowthCorticospinal tract lesionsNeurite outgrowth inhibitorChick DRG neuronsRho-kinase inhibitionCST fibersDRG neuronsCST lesionLocomotor recoveryTract lesionsSpinal cordOutgrowth inhibitorInhibits neurite outgrowthNogo-66Activity levelsMyelinKinase inhibitionLesionsActivation of RhoRatsC3 transferaseInhibition of p160ROCKInhibitors
2002
Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin
Fournier AE, Gould GC, Liu BP, Strittmatter SM. Truncated Soluble Nogo Receptor Binds Nogo-66 and Blocks Inhibition of Axon Growth by Myelin. Journal Of Neuroscience 2002, 22: 8876-8883. PMID: 12388594, PMCID: PMC6757674, DOI: 10.1523/jneurosci.22-20-08876.2002.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsCell LineChick EmbryoGPI-Linked ProteinsGrowth ConesHumansKidneyMiceMolecular Sequence DataMutagenesis, Site-DirectedMyelin ProteinsMyelin SheathNeuritesNogo ProteinsNogo Receptor 1Peptide FragmentsProtein BindingProtein Structure, TertiaryReceptors, Cell SurfaceRepetitive Sequences, Amino AcidRetinaSequence DeletionSignal TransductionSolubilityConceptsChick retinal ganglion cellsRetinal ganglion cellsOutgrowth inhibitionMechanism of NogoGanglion cellsNogo receptorOutgrowth inhibitorViral infectionMyelin inhibitionInhibitory signalingNogo-66Axon growthCNS myelinAxon outgrowthMyelinRegenerative growthNogoCOS-7 cellsInhibitionAlkaline phosphataseReceptorsNGRMyelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor
Liu BP, Fournier A, GrandPré T, Strittmatter SM. Myelin-Associated Glycoprotein as a Functional Ligand for the Nogo-66 Receptor. Science 2002, 297: 1190-1193. PMID: 12089450, DOI: 10.1126/science.1073031.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBinding SitesChick EmbryoCloning, MolecularCOS CellsGanglia, SpinalGene LibraryGPI-Linked ProteinsLigandsMiceMyelin ProteinsMyelin-Associated GlycoproteinNerve RegenerationNeuritesNeuronsNogo ProteinsNogo Receptor 1Peptide FragmentsPhosphatidylinositol Diacylglycerol-LyaseProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSialic AcidsTransfectionType C Phospholipases
2001
PlexinA1 Autoinhibition by the Plexin Sema Domain
Takahashi T, Strittmatter S. PlexinA1 Autoinhibition by the Plexin Sema Domain. Neuron 2001, 29: 429-439. PMID: 11239433, DOI: 10.1016/s0896-6273(01)00216-1.Peer-Reviewed Original Research
2000
Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse
Fournier A, Nakamura F, Kawamoto S, Goshima Y, Kalb R, Strittmatter S. Semaphorin3a Enhances Endocytosis at Sites of Receptor–F-Actin Colocalization during Growth Cone Collapse. Journal Of Cell Biology 2000, 149: 411-422. PMID: 10769032, PMCID: PMC2175148, DOI: 10.1083/jcb.149.2.411.Peer-Reviewed Original ResearchRho GTPases and axonal growth cone collapse
Fournier AE, Kalb RG, Strittmatter SM. Rho GTPases and axonal growth cone collapse. Methods In Enzymology 2000, 325: 473-482. PMID: 11036628, DOI: 10.1016/s0076-6879(00)25467-0.Peer-Reviewed Original ResearchIdentification of the Nogo inhibitor of axon regeneration as a Reticulon protein
GrandPré T, Nakamura F, Vartanian T, Strittmatter S. Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein. Nature 2000, 403: 439-444. PMID: 10667797, DOI: 10.1038/35000226.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsCattleCell DivisionCell LineCentral Nervous SystemChick EmbryoCloning, MolecularConsensus SequenceEscherichia coliGrowth InhibitorsHumansMembrane ProteinsMolecular Sequence DataMyelin ProteinsNerve RegenerationNogo ProteinsOligodendrogliaPC12 CellsRatsRecombinant ProteinsSequence Homology, Amino AcidConceptsCentral nervous systemPeripheral nervous systemCNS white matterAxonal regenerationAxon regenerationNervous systemWhite matterAdult central nervous systemMammalian axon regenerationIN-1 antibodiesReticulon 1Dorsal root ganglion growth conesFunctional recoverySpinal cordSchwann cellsCNS axonsExtracellular domainAxonal extensionNogoAxon extensionGrowth conesOligodendrocytesInhibitory activityReticulon 4Moderate degree
1999
Growth cone neuropilin‐1 mediates collapsin‐1/sema III facilitation of antero‐ and retrograde axoplasmic transport
Goshima Y, Hori H, Sasaki Y, Yang T, Maezono M, Li C, Takenaka T, Nakamura F, Takahashi T, Strittmatter S, Misu Y, Kawakami T. Growth cone neuropilin‐1 mediates collapsin‐1/sema III facilitation of antero‐ and retrograde axoplasmic transport. Developmental Neurobiology 1999, 39: 579-589. PMID: 10380079, DOI: 10.1002/(sici)1097-4695(19990615)39:4<579::aid-neu11>3.0.co;2-9.Peer-Reviewed Original Research
1998
Neuropilin-1 Extracellular Domains Mediate Semaphorin D/III-Induced Growth Cone Collapse
Nakamura F, Tanaka M, Takahashi T, Kalb R, Strittmatter S. Neuropilin-1 Extracellular Domains Mediate Semaphorin D/III-Induced Growth Cone Collapse. Neuron 1998, 21: 1093-1100. PMID: 9856464, DOI: 10.1016/s0896-6273(00)80626-1.Peer-Reviewed Original Research