2017
CNS Neurons Deposit Laminin α5 to Stabilize Synapses
Omar MH, Campbell M, Xiao X, Zhong Q, Brunken WJ, Miner JH, Greer CA, Koleske AJ. CNS Neurons Deposit Laminin α5 to Stabilize Synapses. Cell Reports 2017, 21: 1281-1292. PMID: 29091766, PMCID: PMC5776391, DOI: 10.1016/j.celrep.2017.10.028.Peer-Reviewed Original ResearchConceptsDendritic spine head sizeLaminin α5Larger postsynaptic densitiesDendritic spine densitySpine head sizeAge-dependent lossDendritic spine sizeEnhanced neurotransmissionSpine densityHippocampal neuronsDendritic spinesConditional deletionLaminin β2Postsynaptic densitySynapsesSpine sizeEarly adulthoodBehavioral defectsNeuronsBrainHead sizeMolecular mechanismsΑ5LamininNeurotransmission
2014
Erratum: CORRIGENDUM: Regeneration of Aplysia Bag Cell Neurons is Synergistically Enhanced by Substrate-Bound Hemolymph Proteins and Laminin
Hyland C, Dufresne E, Forscher P. Erratum: CORRIGENDUM: Regeneration of Aplysia Bag Cell Neurons is Synergistically Enhanced by Substrate-Bound Hemolymph Proteins and Laminin. Scientific Reports 2014, 4: 5582. PMCID: PMC4087918, DOI: 10.1038/srep05582.Peer-Reviewed Original ResearchBag cell neuronsHemolymph proteinsRespiratory protein hemocyaninAplysia bag cell neuronsProtein complexesFurther molecular characterizationAddition of hemolymphHigh molecular weight proteinsCell neuronsMolecular weight proteinsMolecular characterizationCellular targetsExtracellular matrixProteinNervous system repairNovel synergistic effectWeight proteinsLaminin substrateHumoral proteinsLamininPossible cooperationActive factorsMigration rateEndogenous factorsPotential relevanceRegeneration of Aplysia Bag Cell Neurons is Synergistically Enhanced by Substrate-Bound Hemolymph Proteins and Laminin
Hyland C, Dufresne ER, Forscher P. Regeneration of Aplysia Bag Cell Neurons is Synergistically Enhanced by Substrate-Bound Hemolymph Proteins and Laminin. Scientific Reports 2014, 4: 4617. PMID: 24722588, PMCID: PMC3983596, DOI: 10.1038/srep04617.Peer-Reviewed Original ResearchConceptsBag cell neuronsHemolymph proteinsRespiratory protein hemocyaninAplysia bag cell neuronsProtein complexesFurther molecular characterizationAddition of hemolymphHigh molecular weight proteinsCell neuronsMolecular weight proteinsMolecular characterizationCellular targetsExtracellular matrixProteinNervous system repairNovel synergistic effectWeight proteinsLaminin substrateHumoral proteinsLamininPossible cooperationActive factorsMigration rateEndogenous factorsPotential relevance
2013
An Inhibitory Antibody Blocks the First Step in the Dithiol/Disulfide Relay Mechanism of the Enzyme QSOX1
Grossman I, Alon A, Ilani T, Fass D. An Inhibitory Antibody Blocks the First Step in the Dithiol/Disulfide Relay Mechanism of the Enzyme QSOX1. Journal Of Molecular Biology 2013, 425: 4366-4378. PMID: 23867277, DOI: 10.1016/j.jmb.2013.07.011.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntibodies, BlockingAntibodies, MonoclonalBinding SitesCell AdhesionCell MovementDisulfidesHumansKineticsModels, MolecularMolecular Sequence DataMultiprotein ComplexesOxidoreductases Acting on Sulfur Group DonorsProtein BindingProtein ConformationProtein Interaction Domains and MotifsSingle-Chain AntibodiesTolueneConceptsQuiescin sulfhydryl oxidase 1Catalyst of disulfide bond formationIntegrin-mediated cell survivalExtracellular matrixSulfhydryl oxidase 1Single-chain variantDisulfide bond formationOxidase domainTumor cell adhesionTight-binding inhibitorProtein dissectionSulfhydryl oxidase activityExtracellular matrix compositionOver-producedCell migrationCell survivalLaminin isoformsRecombinant versionCell adhesionInhibitory antibodiesCultured fibroblastsPotential therapeutic applicationsOxidase activityEnzymeLamininA Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function
Ilani T, Alon A, Grossman I, Horowitz B, Kartvelishvily E, Cohen S, Fass D. A Secreted Disulfide Catalyst Controls Extracellular Matrix Composition and Function. Science 2013, 341: 74-76. PMID: 23704371, DOI: 10.1126/science.1238279.Peer-Reviewed Original ResearchConceptsQuiescin sulfhydryl oxidase 1Disulfide bond formationEndoplasmic reticulumExtracellular matrixCell-matrix adhesionSulfhydryl oxidase 1Extracellular catalysisGolgi apparatusEnzyme familyExtracellular matrix propertiesSecretory proteinsExtracellular matrix compositionInhibitory monoclonal antibodiesCysteine cross-linkingIncorporation of lamininCell migrationPhysiological functionsDisulfide catalystsMonoclonal antibodiesGolgiBond formationReticulumEnzymeProteinLaminin
2005
Expression of Structural Proteins and Angiogenic Factors in Normal Arterial and Unruptured and Ruptured Aneurysm Walls
Kılıc T, Sohrabifar M, Kurtkaya Ö, Yildirim Ö, Elmaci I, Günel M, Pamir MN. Expression of Structural Proteins and Angiogenic Factors in Normal Arterial and Unruptured and Ruptured Aneurysm Walls. Neurosurgery 2005, 57: 997-1007. PMID: 16284569, DOI: 10.1227/01.neu.0000180812.77621.6c.Peer-Reviewed Original ResearchConceptsStructural proteinsGrowth factorPattern of expressionCertain structural proteinsAngiogenic growth factorsLevel of expressionNormal vessel wallGrowth factor alpha expressionAngiogenic factorsProteinBiological mediatorsExpressionFibronectinVessel wallLamininNovel findingsIntracranial aneurysm formationPairs of specimensAneurysmal specimensTissue groupsFormationMediators
1993
Effect of transforming growth factor-β on extracellular matrix productionby cultured rat mesangial cells
ISHIMURA E, MORII H, STERZEL R, KASHGARIAN M. Effect of transforming growth factor-β on extracellular matrix productionby cultured rat mesangial cells. 日本腎臓学会誌 1993, 35: 311-320. PMID: 8341006, DOI: 10.14842/jpnjnephrol1959.35.311.Peer-Reviewed Original ResearchConceptsNorthern blottingCultured rat mesangial cellsRat mesangial cellsCollagen IExtracellular matrix constituentsMesangial cellsGrowth factorEnzyme-linked immunoadsorbent assayGene expressionProtein productionSingle growth factorECM constituentsProtein synthesisGenetic expressionMatrix componentsLamininExpressionGlomerular remodelingECM accumulationTGF-beta administrationBlottingMRNA expressionMatrix constituentsCellsGlomerular injury
1992
Independent modulation of enterocyte migration and proliferation by growth factors, matrix proteins, and pharmacologic agents in an in vitro model of mucosal healing.
Basson M, Modlin I, Flynn S, Jena B, Madri J. Independent modulation of enterocyte migration and proliferation by growth factors, matrix proteins, and pharmacologic agents in an in vitro model of mucosal healing. Surgery 1992, 112: 299-307; discussion 307-8. PMID: 1353641.Peer-Reviewed Original ResearchConceptsMucosal healingPharmacologic agentsGrowth factorEGF-stimulated proliferationCaco-2 enterocytesHuman Caco-2 enterocytesInhibited basalAlpha 2 integrin subunitMatrix proteinsEnterocyte migrationCollagen IInhibitor genisteinIntegrin subunitsHealingIndomethacinProliferationTyrosine kinaseEGFLamininBasalGenisteinAltered organizationIndependent modulationExtracellular matrix protein: gene expression and synthesis in cultured rat mesangial cells
ISHIMURA E, STERZEL R, MORII H, KASHGARIAN M. Extracellular matrix protein: gene expression and synthesis in cultured rat mesangial cells. 日本腎臓学会誌 1992, 34: 9-17. PMID: 1593802, DOI: 10.14842/jpnjnephrol1959.34.9.Peer-Reviewed Original ResearchConceptsGene expressionProtein synthesisExtracellular matrixNorthern blottingBasement membrane matrix componentsFetal calf serumCollagen IMesangial cellsMRNA expressionDNA amountSynthesis of ECMCellular confluenceECM productionCultured rat mesangial cellsMatrix componentsRat mesangial cellsExpressionLamininBlottingCellsCalf serumImmunocytochemical studyPrevious immunocytochemical studiesCIIIMRNA
1991
Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells.
Boll W, Partin JS, Katz AI, Caplan MJ, Jamieson JD. Distinct pathways for basolateral targeting of membrane and secretory proteins in polarized epithelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 8592-8596. PMID: 1656451, PMCID: PMC52555, DOI: 10.1073/pnas.88.19.8592.Peer-Reviewed Original ResearchConceptsCarrier vesiclesMembrane proteinsBasolateral domainSecretory proteinsMadin-Darby canine kidney II cell linePolarized epithelial cellsBasement membrane protein lamininEpithelial cellsBasolateral proteinsBasolateral targetingProtein lamininMicrotubule disruptionDistinct pathwaysMicrotubule depolymerizationProteinDistinct setsCell linesBinding sitesBasolateral secretionIntegrinsVesiclesLamininPathwayMembraneCells
1990
Spatiotemporal segregation of endothelial cell integrin and nonintegrin extracellular matrix-binding proteins during adhesion events.
Basson C, Knowles W, Bell L, Albelda S, Castronovo V, Liotta L, Madri J. Spatiotemporal segregation of endothelial cell integrin and nonintegrin extracellular matrix-binding proteins during adhesion events. Journal Of Cell Biology 1990, 110: 789-801. PMID: 2407741, PMCID: PMC2116027, DOI: 10.1083/jcb.110.3.789.Peer-Reviewed Original ResearchConceptsMatrix-binding proteinsBeta 1 integrinLow-affinity integrinsRGD-dependent receptorExtracellular matrix-binding proteinsIntegrin beta 1Integrin subclassesBeta 1Beta 3Endothelial cell integrinsPeptide inhibitionBAECFibrinogenBAEC migrationCell integrinsLamininPerinuclear vesiclesIntegrinsAlpha subunitMatrix proteinsAdhesive eventsFibronectinPeptides
1985
Immunolocalization of type IV collagen and laminin in nonbasement membrane structures of murine corneal stroma. A light and electron microscopic study.
Pratt B, Madri J. Immunolocalization of type IV collagen and laminin in nonbasement membrane structures of murine corneal stroma. A light and electron microscopic study. Laboratory Investigation 1985, 52: 650-6. PMID: 3892156.Peer-Reviewed Original ResearchConceptsElectron microscopic immunolocalizationMicrofibril bundlesInterstitial collagen types IType IV collagenPossible functionsExtracellular matrixImmunofluorescent localizationMembrane structureIV collagenCollagen type IType IType V collagenOxytalan microfibrilsImmunolocalizationCellular sourceMicrofibrilsLaminin
1980
Ultrastructural localization of fibronectin and laminin in the basement membranes of the murine kidney.
Madri J, Roll F, Furthmayr H, Foidart J. Ultrastructural localization of fibronectin and laminin in the basement membranes of the murine kidney. Journal Of Cell Biology 1980, 86: 682-687. PMID: 6995470, PMCID: PMC2111490, DOI: 10.1083/jcb.86.2.682.Peer-Reviewed Original ResearchConceptsTubular basement membraneMesangial areaBowman's capsuleMesangial matrixBasement membraneFrozen sectionsNormal murine kidneyMurine kidneyAffinity-purified rabbit antibodiesConventional frozen sectionsGlomerular basement membraneSheep anti-rabbit IgGLaminin labellingThick frozen sectionsImmunofluorescence stainingSpecific antibodiesRabbit antibodiesLamina rara internaMesangial cell processesKidneyUltrastructural levelCapsuleAntibodiesAnti-rabbit IgGLaminin
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