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
2003
Vascular 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
Paracrine 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
1999
PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin
Ilan N, Mahooti S, Rimm D, Madri J. PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated β-catenin. Journal Of Cell Science 1999, 112: 3005-3014. PMID: 10462517, DOI: 10.1242/jcs.112.18.3005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninCattleCells, CulturedCytoskeletal ProteinsEndothelial Growth FactorsEndothelium, VascularGene ExpressionHumansIn Vitro TechniquesLymphokinesModels, BiologicalNeovascularization, PhysiologicPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein-Tyrosine KinasesTrans-ActivatorsTransfectionTyrosineVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsTyrosine phosphorylationBeta-catenin tyrosine phosphorylationBeta-catenin nuclear translocationAdherens junction formationProtein tyrosine kinasesPECAM-1 functionsTyrosine phosphorylation levelsCell-cell contactSW480 colon carcinoma cellsEndothelial cell-cell contactsCatenin functionVascular endothelial growth factorCell adhesion moleculeTranscriptional factorsPECAM-1Colon carcinoma cellsTyrosine kinaseGamma cateninMajor substrateJunctional proteinsCytoplasmic levelsPhosphorylation levelsNuclear translocationΒ-cateninCateninHyperglycemia-Induced Vasculopathy in the Murine Vitelline Vasculature Correlation with PECAM-1/CD31 Tyrosine Phosphorylation State
Pinter E, Mahooti S, Wang Y, Imhof B, Madri J. Hyperglycemia-Induced Vasculopathy in the Murine Vitelline Vasculature Correlation with PECAM-1/CD31 Tyrosine Phosphorylation State. American Journal Of Pathology 1999, 154: 1367-1379. PMID: 10329590, PMCID: PMC1866605, DOI: 10.1016/s0002-9440(10)65391-6.Peer-Reviewed Original ResearchConceptsPECAM-1 tyrosine phosphorylationTyrosine phosphorylation stateMurine conceptusYolk sacCell-extracellular matrixFirst organ systemCell-factor interactionsTyrosine dephosphorylationEndothelial cell migrationEmbryonic angioblastsEmbryonic developmentMesodermal cellsVasculogenesis/angiogenesisTyrosine phosphorylationPhosphorylation statePerinatal lethalityNormal organogenesisVascular systemCell migrationHematopoietic cellsDiabetic pregnant miceComplex vascular systemVasculogenesisPECAM-1 expressionOffspring
1997
Platelet-endothelial cell adhesion molecule-1 (PECAM-1/CD31) tyrosine phosphorylation state changes during vasculogenesis in the murine conceptus.
Pinter E, Barreuther M, Lu T, Imhof B, Madri J. Platelet-endothelial cell adhesion molecule-1 (PECAM-1/CD31) tyrosine phosphorylation state changes during vasculogenesis in the murine conceptus. American Journal Of Pathology 1997, 150: 1523-30. PMID: 9137078, PMCID: PMC1858227.Peer-Reviewed Original ResearchConceptsBlood islandsSrc homology 2 domain-containing proteinsDomain-containing proteinsPhosphorylation state changesPlatelet endothelial cell adhesion molecule-1PECAM-1 cytoplasmic domainMurine conceptusParticular tyrosine residueCell-extracellular matrixDifferential tyrosine phosphorylationCell-cell interactionsEndothelial cell migrationCytoplasmic domainEmbryonic angioblastsMesodermal cellsTyrosine phosphorylationTyrosine residuesCellular localizationCell migrationAngioblastsPhosphorylationGrowth factorVasculogenesisCell adhesion molecule-1Morphogens
1995
Modulation of cell spreading and migration by pp125FAK phosphorylation.
Sankar S, Mahooti-Brooks N, Hu G, Madri J. Modulation of cell spreading and migration by pp125FAK phosphorylation. American Journal Of Pathology 1995, 147: 601-8. PMID: 7677174, PMCID: PMC1870973.Peer-Reviewed Original ResearchConceptsPp125FAK tyrosine phosphorylationTyrosine phosphorylationCell migrationCell spreadingIntegrin-mediated signalingFocal adhesion kinaseKinase-negative mutantPp125FAK phosphorylationAdhesion kinaseMigration ratePhosphorylationCascade pathwayFaster migration rateControl cellsSlower migration rateType I collagenEnhanced levelsCellsI collagenFibronectinMigrationPp125FAKMutantsKinaseSignaling