2004
Paracrine and Autocrine Functions of Brain-derived Neurotrophic Factor (BDNF) and Nerve Growth Factor (NGF) in Brain-derived Endothelial Cells*
Kim H, Li Q, Hempstead BL, Madri JA. Paracrine and Autocrine Functions of Brain-derived Neurotrophic Factor (BDNF) and Nerve Growth Factor (NGF) in Brain-derived Endothelial Cells*. Journal Of Biological Chemistry 2004, 279: 33538-33546. PMID: 15169782, DOI: 10.1074/jbc.m404115200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBlotting, WesternBrainBrain-Derived Neurotrophic FactorCaspase 3CaspasesCell Line, TransformedCerebral CortexEndothelial CellsEnzyme ActivationEnzyme InhibitorsFlow CytometryGene Expression RegulationHypoxiaImmunohistochemistryImmunosorbent TechniquesMAP Kinase Kinase KinasesMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNerve Growth FactorPhosphoinositide-3 Kinase InhibitorsPhosphorylationRatsReceptor, Nerve Growth FactorReceptor, trkBReceptors, Nerve Growth FactorRecombinant Fusion ProteinsRecombinant ProteinsTransfectionVascular Endothelial Growth Factor Receptor-2ConceptsBrain-derived neurotrophic factorEndogenous brain-derived neurotrophic factorBrain-derived endothelial cellsNerve growth factorEndothelial cellsNeurotrophic factorAutocrine functionExpression of BDNFCentral nervous system (CNS) endotheliumPro-nerve growth factorGrowth factorExpression of TrkBNormoxic conditionsCentral nervous systemBDNF levelsBDNF expressionBDNF responseTrkB phosphorylationNervous systemTrkBSurvival/apoptosisCell survival/apoptosisRobust angiogenesisAkt pathwayInhibitor of phosphatidylinositol
2003
Elevated glucose inhibits VEGF-A–mediated endocardial cushion formation
Enciso JM, Gratzinger D, Camenisch TD, Canosa S, Pinter E, Madri JA. Elevated glucose inhibits VEGF-A–mediated endocardial cushion formation. Journal Of Cell Biology 2003, 160: 605-615. PMID: 12591918, PMCID: PMC2173755, DOI: 10.1083/jcb.200209014.Peer-Reviewed Original ResearchMeSH KeywordsAngiogenesis Inducing AgentsAnimalsCell MovementCell SizeCells, CulturedCulture TechniquesDipeptidesEmbryo, MammalianEndocardial Cushion DefectsFemaleGlucoseHeartMaleMatrix Metalloproteinase 2MiceMorphogenesisMyocardiumPlatelet Endothelial Cell Adhesion Molecule-1Protease InhibitorsRecombinant Fusion ProteinsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-1ConceptsEpithelial-mesenchymal transformationEndocardial cushion formationPlatelet endothelial cell adhesion molecule-1Cushion formationPECAM-1-positive endothelial cellsSingle cell motilityMMP-2 expressionMorphogenesis resultsHigh glucose-induced inhibitionCell motilityEndothelial cellsBlocks invasionMatrix metalloproteinase-2 expressionEndocardial cellsExtracellular matrixLack of invasionEndothelial cell adhesion molecule-1Mesenchymal cellsMyocardial VEGFMMP-2 inductionMetalloproteinase-2 expressionVEGF-A165ExpressionGrowth factorVascular endothelial growth factorPlatelet–endothelial cell adhesion molecule-1 modulates endothelial migration through its immunoreceptor tyrosine-based inhibitory motif
Gratzinger D, Barreuther M, Madri JA. Platelet–endothelial cell adhesion molecule-1 modulates endothelial migration through its immunoreceptor tyrosine-based inhibitory motif. Biochemical And Biophysical Research Communications 2003, 301: 243-249. PMID: 12535670, DOI: 10.1016/s0006-291x(02)02982-0.Peer-Reviewed Original ResearchMeSH KeywordsAdherens JunctionsAmino Acid MotifsAnimalsCattleCell MovementCells, CulturedEndothelium, VascularEnzyme ActivationIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein BindingProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine PhosphatasesRecombinant Fusion ProteinsTyrosineConceptsSHP-2Tyrosine phosphatase SHP-2Endothelial migrationFocal contact componentsPlatelet endothelial cell adhesion molecule-1Phosphatase SHP-2Cell-cell junctionsImmunoreceptor tyrosine-based inhibitory motifCell-substrate adhesionFocal adhesion kinaseTyrosine-based inhibitory motifPECAM-1Endothelial cellsPECAM-1 phosphorylationSelective dephosphorylationAdhesion kinaseTyrosine phosphorylationAdhesion proteinsRecombinant proteinsCytoskeletal fractionCell adhesion molecule-1Coordinated migrationInhibitory motifPhosphorylationAdhesion molecule-1
2000
Platelet-Endothelial Cell Adhesion Molecule-1 (CD31), a Scaffolding Molecule for Selected Catenin Family Members Whose Binding Is Mediated by Different Tyrosine and Serine/Threonine Phosphorylation*
Ilan N, Cheung L, Pinter E, Madri J. Platelet-Endothelial Cell Adhesion Molecule-1 (CD31), a Scaffolding Molecule for Selected Catenin Family Members Whose Binding Is Mediated by Different Tyrosine and Serine/Threonine Phosphorylation*. Journal Of Biological Chemistry 2000, 275: 21435-21443. PMID: 10801826, DOI: 10.1074/jbc.m001857200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBinding SitesCadherinsCell Adhesion MoleculesCell LineCells, CulturedCytoskeletal ProteinsCytoskeletonDesmoplakinsEmbryo, MammalianEndothelium, VascularGamma CateninHumansMicePhosphorylationPhosphoserinePhosphothreoninePhosphotyrosinePlatelet Endothelial Cell Adhesion Molecule-1Protein Kinase CRecombinant Fusion ProteinsSignal TransductionTrans-ActivatorsUmbilical VeinsYolk SacConceptsSerine/threonine phosphorylationThreonine phosphorylationCell-cell junctionsSpecific tyrosine residuesSignal transduction pathwaysPECAM-1 functionsTyrosine phosphorylation levelsInsoluble cytoskeletal fractionPECAM-1Beta-catenin localizationCytoskeleton interactionsPKC enzymeTransduction pathwaysCell adhesion moleculeCytoskeletal fractionTyrosine residuesMolecular mechanismsDifferent tyrosinePlatelet endothelial cell adhesion molecule-1Phosphorylation levelsITAM domainSW480 cellsEndothelium-specific markersPhosphorylationPlatelet endothelial cell adhesion molecule
1993
Characterization of distinct functional domains of transforming growth factor beta.
Burmester J, Qian S, Roberts A, Huang A, Amatayakul-Chantler S, Suardet L, Odartchenko N, Madri J, Sporn M. Characterization of distinct functional domains of transforming growth factor beta. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 8628-8632. PMID: 7690965, PMCID: PMC47411, DOI: 10.1073/pnas.90.18.8628.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAlpha-MacroglobulinsAmino Acid SequenceAnimalsCattleCHO CellsCricetinaeDose-Response Relationship, DrugEndothelium, VascularHeartHumansKineticsMiceMolecular Sequence DataReceptors, Cell SurfaceReceptors, Transforming Growth Factor betaRecombinant Fusion ProteinsRecombinant ProteinsTransforming Growth Factor betaUmbilical VeinsConceptsGrowth factor betaFactor betaHuman colorectal cancer cell linesColorectal cancer cell linesLS513 cellsCancer cell linesTGF-beta moleculesCell linesAlphaBiological potencyBetaCellsCertain cellsAmino acidsPotencyDistinct functional domainsAdditional amino acidsDifferent isoformsIsoformsDistinct isoformsFunctional domainsChimeric protein
1992
Acidic fibroblast growth factor-Pseudomonas exotoxin chimeric protein elicits antiangiogenic effects on endothelial cells.
Merwin J, Lynch M, Madri J, Pastan I, Siegall C. Acidic fibroblast growth factor-Pseudomonas exotoxin chimeric protein elicits antiangiogenic effects on endothelial cells. Cancer Research 1992, 52: 4995-5001. PMID: 1381275.Peer-Reviewed Original ResearchMeSH KeywordsADP Ribose TransferasesAmino Acid SequenceAnimalsBacterial ToxinsCell MovementCell SurvivalCells, CulturedEndothelium, VascularExotoxinsFibroblast Growth Factor 1In Vitro TechniquesMolecular Sequence DataNeovascularization, PathologicRatsRats, Inbred StrainsReceptors, Cell SurfaceReceptors, Fibroblast Growth FactorRecombinant Fusion ProteinsVirulence FactorsConceptsGrowth factor beta 1Endothelial cellsChimeric toxinBeta 1Inhibitory effectDose-dependent toxic effectAnti-angiogenic agentsMicrovascular endothelial cellsAcidic fibroblast growth factorFibroblast growth factorSignificant inhibitory effectMicrovascular endotheliumAntiangiogenic effectsPseudomonas exotoxinTumor cell linesAntimigratory effectsGrowth factorAngiogenic responseProtein synthesisCell linesFGF receptorsToxic effectsCell deathEndotheliumCell viability analysisIdentification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells.
Qian S, Burmester J, Merwin J, Madri J, Sporn M, Roberts A. Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6290-6294. PMID: 1631120, PMCID: PMC49486, DOI: 10.1073/pnas.89.14.6290.Peer-Reviewed Original ResearchConceptsEndothelial cellsFetal bovine heart endothelial cellsMicrovascular endothelial cellsGrowth factor betaHeart endothelial cellsAortic endothelial cellsBovine aortic endothelial cellsFactor betaType 1Amino acids 40Beta moleculesInhibition of growthAmino acids 1Biological potencyCellsGreater activity