2017
NOD Mice Having a Lyn Tyrosine Kinase Mutation Exhibit Abnormal Neutrophil Chemotaxis
Wu Y, Hannigan M, Zhan L, Madri JA, Huang C. NOD Mice Having a Lyn Tyrosine Kinase Mutation Exhibit Abnormal Neutrophil Chemotaxis. Journal Of Cellular Physiology 2017, 232: 1689-1695. PMID: 27591397, DOI: 10.1002/jcp.25583.Peer-Reviewed Original ResearchAs human lung microvascular endothelia achieve confluence, src family kinases are activated, and tyrosine-phosphorylated p120 catenin physically couples NEU1 sialidase to CD31
Hyun SW, Liu A, Liu Z, Lillehoj EP, Madri JA, Reynolds AB, Goldblum SE. As human lung microvascular endothelia achieve confluence, src family kinases are activated, and tyrosine-phosphorylated p120 catenin physically couples NEU1 sialidase to CD31. Cellular Signalling 2017, 35: 1-15. PMID: 28343945, DOI: 10.1016/j.cellsig.2017.03.014.Peer-Reviewed Original ResearchMeSH KeywordsCateninsCell LineCell-Free SystemDelta CateninEndothelial CellsHumansLungMicrovesselsN-Acetylneuraminic AcidNeovascularization, PhysiologicNeuraminidasePhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein BindingProtein Interaction MapsProto-Oncogene Proteins c-fynProto-Oncogene Proteins c-yesSignal TransductionSrc-Family Kinases
2011
Laminar shear, but not orbital shear, has a synergistic effect with thrombin stimulation on tissue factor expression in human umbilical vein endothelial cells
Rochier A, Nixon A, Yamashita N, Abe R, Abe R, Madri JA, Sumpio BE. Laminar shear, but not orbital shear, has a synergistic effect with thrombin stimulation on tissue factor expression in human umbilical vein endothelial cells. Journal Of Vascular Surgery 2011, 54: 480-488. PMID: 21367569, DOI: 10.1016/j.jvs.2011.01.002.Peer-Reviewed Original ResearchAnalysis of VarianceBlotting, WesternCell Culture TechniquesCells, CulturedEndothelial CellsEnzyme ActivationHumansMechanotransduction, CellularMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3P38 Mitogen-Activated Protein KinasesPhosphorylationProtein Kinase InhibitorsRNA, MessengerStress, MechanicalThrombinThromboplastinTime FactorsUp-RegulationGSK-3β: a signaling pathway node modulating neural stem cell and endothelial cell interactions
Li Q, Michaud M, Canosa S, Kuo A, Madri JA. GSK-3β: a signaling pathway node modulating neural stem cell and endothelial cell interactions. Angiogenesis 2011, 14: 173-185. PMID: 21253820, DOI: 10.1007/s10456-011-9201-9.Peer-Reviewed Original ResearchMeSH KeywordsAminophenolsAnimalsBasic Helix-Loop-Helix Transcription FactorsBeta CateninBrainCell CommunicationCell DifferentiationCell MovementCell ProliferationEndothelial CellsEnzyme ActivationGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHypoxia-Inducible Factor 1, alpha SubunitIntercellular Signaling Peptides and ProteinsMaleMaleimidesMiceMice, Inbred C57BLNeovascularization, PhysiologicNeural Stem CellsNeurogenesisPhosphorylationPhosphoserineReceptor Cross-TalkSignal TransductionSolubilitySpecies SpecificityConceptsNeural stem cellsNotch-1 expressionHIF-1αGSK-3βSDF-1III-tubulinStem cellsPremature infant populationMicrovascular endothelial cellsGSK-3β activationCD1 levelsEndothelial cell interactionsNeurogenic areasVascular proliferationInfant populationGSK-3β inhibitorTherapeutic potentialSVZ tissueGreater angiogenesisHIF-2αMouse strainsΒ-catenin participatesEndothelial cellsReciprocal modulation
2009
Bone Marrow Monocyte PECAM-1 Deficiency Elicits Increased Osteoclastogenesis Resulting in Trabecular Bone Loss
Wu Y, Tworkoski K, Michaud M, Madri JA. Bone Marrow Monocyte PECAM-1 Deficiency Elicits Increased Osteoclastogenesis Resulting in Trabecular Bone Loss. The Journal Of Immunology 2009, 182: 2672-2679. PMID: 19234161, DOI: 10.4049/jimmunol.0802398.Peer-Reviewed Original ResearchMeSH KeywordsAgingAnimalsBone Marrow CellsBone ResorptionCell DifferentiationCells, CulturedDown-RegulationFemaleIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutMonocytesOsteoclastsOsteogenesisPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein-Tyrosine KinasesSyk KinaseZAP-70 Protein-Tyrosine KinaseConceptsOsteoclast-like cellsKO miceBone marrowPECAM-1-null miceTrabecular bone lossPECAM-1Trabecular bone volumeSize of osteoclastsNF-kappaB ligandOsteoclast precursor culturesSHP-1 interactionsNumber of trabeculaeWT miceBM monocytesBone lossBone resorptionReceptor activatorBone volumeSHP-1Precursor culturesNull miceMiceLong bonesSyk kinaseFurther studies
2008
Differential Effects of Shear Stress and Cyclic Strain on Sp1 Phosphorylation by Protein Kinase Cζ Modulates Membrane Type 1–Matrix Metalloproteinase in Endothelial Cells
Kim JI, Cordova AC, Hirayama Y, Madri JA, Sumpio BE. Differential Effects of Shear Stress and Cyclic Strain on Sp1 Phosphorylation by Protein Kinase Cζ Modulates Membrane Type 1–Matrix Metalloproteinase in Endothelial Cells. Endothelium 2008, 15: 33-42. PMID: 18568943, PMCID: PMC2644408, DOI: 10.1080/10623320802092260.Peer-Reviewed Original ResearchConceptsSp1 phosphorylationMT1-MMP expressionPromoter sitesPKCzeta inhibitorProtein kinase CzetaAffinity of Sp1Egr-1 bindingProtein kinase CζExtracellular matrix remodelingEndothelial cell migrationSp1Cell migrationPhosphorylationMatrix remodelingProtein expressionCyclic strainExpressionMembrane typeEndothelial cellsKey roleCzetaInhibitorsCζMetalloproteinaseAffinity
2007
MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil polarization
Wu Y, Zhan L, Ai Y, Hannigan M, Gaestel M, Huang CK, Madri JA. MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil polarization. Biochemical And Biophysical Research Communications 2007, 358: 170-175. PMID: 17481585, DOI: 10.1016/j.bbrc.2007.04.104.Peer-Reviewed Original ResearchAnimalsCarrier ProteinsCell PolarityChemotaxis, LeukocyteHumansImidazolesIn Vitro TechniquesIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutMicrofilament ProteinsNeutrophil ActivationNeutrophilsN-Formylmethionine Leucyl-PhenylalanineP38 Mitogen-Activated Protein KinasesPhosphorylationProtein Serine-Threonine KinasesPseudopodiaPyridines
2006
PECAM-1 Affects GSK-3β-Mediated β-Catenin Phosphorylation and Degradation
Biswas P, Canosa S, Schoenfeld D, Schoenfeld J, Li P, Cheas LC, Zhang J, Cordova A, Sumpio B, Madri JA. PECAM-1 Affects GSK-3β-Mediated β-Catenin Phosphorylation and Degradation. American Journal Of Pathology 2006, 169: 314-324. PMID: 16816383, PMCID: PMC1698776, DOI: 10.2353/ajpath.2006.051112.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBlotting, WesternCapillary PermeabilityCells, CulturedEndothelial CellsFluorescent Antibody TechniqueGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHistamineHistamine AgentsHumansMiceModels, BiologicalPhosphatidylinositol 3-KinasesPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Proto-Oncogene Proteins c-aktReceptors, HistamineSignal TransductionConceptsAdherens junctionsSerine phosphorylationSrc homology 2 domainBeta-catenin expression levelsAdherens junction componentsSerine phosphorylation levelEndothelial cellsΒ-catenin phosphorylationPECAM-1Cell biological responsesCytoplasmic domainSHP-2Proteosomal degradationGSK-3betaDynamic regulatorJunction componentsPhosphorylation levelsPhosphorylationEndothelial cell adhesion molecule-1Expression levelsGSK-3βBiological responsesEndothelial barrier permeabilityMice exhibitCell adhesion molecule-1
2005
MAPKs (ERK½, p38) and AKT Can Be Phosphorylated by Shear Stress Independently of Platelet Endothelial Cell Adhesion Molecule-1 (CD31) in Vascular Endothelial Cells*
Sumpio BE, Yun S, Cordova AC, Haga M, Zhang J, Koh Y, Madri JA. MAPKs (ERK½, p38) and AKT Can Be Phosphorylated by Shear Stress Independently of Platelet Endothelial Cell Adhesion Molecule-1 (CD31) in Vascular Endothelial Cells*. Journal Of Biological Chemistry 2005, 280: 11185-11191. PMID: 15668248, DOI: 10.1074/jbc.m414631200.Peer-Reviewed Original ResearchAnimalsCattleCell CommunicationEndothelial CellsEnzyme ActivationHumansMechanoreceptorsMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3P38 Mitogen-Activated Protein KinasesPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktStress, MechanicalTyrosine
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
PECAM-1: old friend, new partners
Ilan N, Madri JA. PECAM-1: old friend, new partners. Current Opinion In Cell Biology 2003, 15: 515-524. PMID: 14519385, DOI: 10.1016/s0955-0674(03)00100-5.Peer-Reviewed Original ResearchMeSH KeywordsAdherens JunctionsAlpha CateninAnimalsApoptosisBeta CateninCapillary PermeabilityCell Adhesion MoleculesCytoskeletal ProteinsDNA-Binding ProteinsHumansIntermediate FilamentsMilk ProteinsModels, MolecularPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein Structure, TertiarySignal TransductionSTAT5 Transcription FactorTrans-ActivatorsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Expression, β-Catenin Tyrosine Phosphorylation, and Endothelial Proliferative Behavior: A Pathway for Transformation?
Ilan N, Tucker A, Madri JA. Vascular Endothelial Growth Factor Expression, β-Catenin Tyrosine Phosphorylation, and Endothelial Proliferative Behavior: A Pathway for Transformation? Laboratory Investigation 2003, 83: 1105-1115. PMID: 12920240, DOI: 10.1097/01.lab.0000083531.84403.8b.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, BlockingAntigens, CD1Beta CateninCell DivisionCell Transformation, NeoplasticCytoskeletal ProteinsEndothelial Growth FactorsEndothelium, VascularExtracellular Matrix ProteinsHemangioendotheliomaHumansIntercellular Signaling Peptides and ProteinsLymphokinesPhosphorylationTrans-ActivatorsTumor Cells, CulturedTyrosineUmbilical VeinsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth FactorsConceptsVascular endothelial growth factorEOMA cellsCD1 levelsFlk-1Vascular endothelial growth factor (VEGF) expressionExogenous vascular endothelial growth factorEndogenous vascular endothelial growth factorEndothelial cell tumorsGrowth factor expressionEndothelial growth factorTyrosine phosphorylationNuclear beta-catenin localizationNuclear localizationProliferative behaviorΒ-catenin tyrosine phosphorylationHuman endothelial cellsComponent expression levelsCD1 expressionCell tumorsCommon tumorsImmune complex kinase assayEndothelial cell transformationMitogen-activated protein kinase activationPrimary human endothelial cellsAutocrine loopPlatelet–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
2002
Transcription Factor Sp1 Phosphorylation Induced by Shear Stress Inhibits Membrane Type 1-Matrix Metalloproteinase Expression in Endothelium*
Yun S, Dardik A, Haga M, Yamashita A, Yamaguchi S, Koh Y, Madri JA, Sumpio BE. Transcription Factor Sp1 Phosphorylation Induced by Shear Stress Inhibits Membrane Type 1-Matrix Metalloproteinase Expression in Endothelium*. Journal Of Biological Chemistry 2002, 277: 34808-34814. PMID: 12093818, DOI: 10.1074/jbc.m205417200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCells, CulturedDNADNA-Binding ProteinsEarly Growth Response Protein 1Electrophoretic Mobility Shift AssayEndothelium, VascularImmediate-Early ProteinsMatrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesNogalamycinPhosphorylationPromoter Regions, GeneticRatsRats, Sprague-DawleyRNA, MessengerSp1 Transcription FactorStress, PhysiologicalTranscription FactorsConceptsMT1-MMP expressionEgr-1MRNA transcriptionMT1-MMP promoterPost-translational modificationsCalf intestinal phosphataseDistinct environmental stimuliTranscription factor expressionSp1 phosphorylationEgr-1 expressionSp1 DNAEndothelial cell migrationSerine phosphorylationPromoter sitesSp1Cell migrationEnvironmental stimuliMatrix remodelingIntestinal phosphataseProtein levelsTranscriptionTime-dependent fashionPhosphorylationMechanical forcesExpressionParacrine and Autocrine Functions of Neuronal Vascular Endothelial Growth Factor (VEGF) in the Central Nervous System*
Ogunshola OO, Antic A, Donoghue MJ, Fan SY, Kim H, Stewart WB, Madri JA, Ment LR. Paracrine and Autocrine Functions of Neuronal Vascular Endothelial Growth Factor (VEGF) in the Central Nervous System*. Journal Of Biological Chemistry 2002, 277: 11410-11415. PMID: 11777931, DOI: 10.1074/jbc.m111085200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCerebral CortexEndothelial Growth FactorsImmunohistochemistryLymphokinesMAP Kinase Kinase Kinase 1MiceNeuronsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationProtein Serine-Threonine KinasesRatsReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, Vascular Endothelial Growth FactorSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsVascular endothelial growth factorNeuronal vascular endothelial growth factorExtracellular signal-regulated protein kinaseSignal-regulated protein kinaseCentral nervous systemFlk-1Inhibition of phosphatidylinositolPost-mitotic neuronsTyrosine phosphorylation levelsInhibition of MEKEndothelial growth factorAutocrine functionGrowth factorEmbryonic mouse forebrainNervous systemMaintenance of neuronsProtein kinaseTyrosine phosphorylationNovel functionNeuronal culturesPhosphorylation levelsSpecific inhibitorExpression of VEGFExogenous additionEmbryonic cortical neurons
2001
Astrocyte-derived VEGF mediates survival and tube stabilization of hypoxic brain microvascular endothelial cells in vitro
Chow J, Ogunshola O, Fan S, Li Y, Ment L, Madri J. Astrocyte-derived VEGF mediates survival and tube stabilization of hypoxic brain microvascular endothelial cells in vitro. Brain Research 2001, 130: 123-132. PMID: 11557101, DOI: 10.1016/s0165-3806(01)00220-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornApoptosisAstrocytesCell CommunicationCell Culture TechniquesCell DivisionCell HypoxiaCell SurvivalCoculture TechniquesCollagenEndothelial Growth FactorsEndothelium, VascularGelsHypoxia, BrainLymphokinesMitogen-Activated Protein KinasesPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRatsVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsBrain microvascular endothelial cellsChronic sublethal hypoxiaVascular endothelial growth factorHypoxic conditionsNewborn rat astrocytesMicrovascular endothelial cellsEndothelial growth factorDose-dependent mannerEffects of hypoxiaVEGF receptor 1Mild hypoxic conditionsImportance of VEGFRBE4 cellsRat astrocytesAmount of VEGFSublethal hypoxiaReceptor 1MAPK tyrosine phosphorylationEndothelial cellsGrowth factorRobust inductionVEGFTube formationTube stabilizationExogenous VEGFHyperglycemia-Induced Vasculopathy in the Murine Conceptus Is Mediated via Reductions of VEGF-A Expression and VEGF Receptor Activation
Pinter E, Haigh J, Nagy A, Madri J. Hyperglycemia-Induced Vasculopathy in the Murine Conceptus Is Mediated via Reductions of VEGF-A Expression and VEGF Receptor Activation. American Journal Of Pathology 2001, 158: 1199-1206. PMID: 11290536, PMCID: PMC1891927, DOI: 10.1016/s0002-9440(10)64069-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood VesselsEndothelial Growth FactorsFetal DiseasesFetusHyperglycemiaLymphokinesMicePhosphorylationReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, Vascular Endothelial Growth FactorTime FactorsVascular DiseasesVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsVEGF receptorsMajor congenital malformationsCongenital cardiovascular abnormalitiesVEGF/VEGF receptorVitelline circulationNovel therapeutic approachesLevels of VEGFReduction of VEGFCause of mortalityDiabetic mothersInsult resultsVEGF levelsCardiovascular abnormalitiesHyperglycemic insultGlucose levelsTherapeutic approachesCongenital malformationsResultant abnormalitiesReceptor activationVEGF receptor activationCardiovascular systemTeratogenic agentsVasculopathyDiabetesConceptusPECAM-1 Is a Modulator of STAT Family Member Phosphorylation and Localization: Lessons from a Transgenic Mouse
Ilan N, Cheung L, Miller S, Mohsenin A, Tucker A, Madri J. PECAM-1 Is a Modulator of STAT Family Member Phosphorylation and Localization: Lessons from a Transgenic Mouse. Developmental Biology 2001, 232: 219-232. PMID: 11254359, DOI: 10.1006/dbio.2001.0186.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DivisionCell NucleusCells, CulturedDNA-Binding ProteinsEndothelium, VascularFemaleHumansMammary Glands, AnimalMiceMice, TransgenicMilk ProteinsMorphogenesisPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Pulmonary AlveoliSTAT5 Transcription FactorTrans-ActivatorsTumor Suppressor ProteinsConceptsImmunoreceptor tyrosine activation motifMilk protein gene expressionPhosphorylation levelsSignal transduction pathwaysProtein gene expressionTyrosine activation motifTyrosine phosphorylation levelsPECAM-1Cell cycle progressionMammary gland developmentInduction of p21Cytoplasmic tailBranching morphogenesisTransduction pathwaysTransgenic miceActivation motifCell adhesion moleculeDuctal epithelial cell proliferationGene expressionCycle progressionGland developmentEpithelial cell proliferationDuctal branching morphogenesisCell proliferationVascular cellsFocal Adhesion Kinase Activates Stat1 in Integrin-mediated Cell Migration and Adhesion*
Xie B, Zhao J, Kitagawa M, Durbin J, Madri J, Guan J, Fu X. Focal Adhesion Kinase Activates Stat1 in Integrin-mediated Cell Migration and Adhesion*. Journal Of Biological Chemistry 2001, 276: 19512-19523. PMID: 11278462, DOI: 10.1074/jbc.m009063200.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCell AdhesionCell LineCell MovementDNA-Binding ProteinsDose-Response Relationship, DrugEnzyme ActivationFibroblastsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene DeletionGlutathione TransferaseHumansIntegrinsMicroscopy, FluorescenceMutagenesis, Site-DirectedMutationPhosphorylationPlasmidsPrecipitin TestsProtein BindingProtein Structure, TertiaryProtein-Tyrosine KinasesSignal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorTime FactorsTrans-ActivatorsTransfectionConceptsFocal adhesion kinaseCell adhesionCell migrationFAK-deficient cellsIntegrin/focal adhesion kinaseC-terminal deletionsAdhesion kinaseTerminal domainFAK localizationTranscription pathwayFocal contactsSignal transducerSTAT1PathwayRecent studiesAdhesionMigrationCellsKinaseIntegrinsSTAT3DeletionActivatorFirst timeActivation
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