2017
Increased Oxidative Stress and Hypoxia Inducible Factor-1 Expression during Arteriovenous Fistula Maturation
Sadaghianloo N, Yamamoto K, Bai H, Tsuneki M, Protack CD, Hall MR, Declemy S, Hassen-Khodja R, Madri J, Dardik A. Increased Oxidative Stress and Hypoxia Inducible Factor-1 Expression during Arteriovenous Fistula Maturation. Annals Of Vascular Surgery 2017, 41: 225-234. PMID: 28163173, PMCID: PMC5411319, DOI: 10.1016/j.avsg.2016.09.014.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaArteriovenous Shunt, SurgicalGene Expression RegulationHeme Oxygenase-1Hydrogen PeroxideHyperplasiaHypoxia-Inducible Factor 1, alpha SubunitMaleMembrane ProteinsMice, Inbred C57BLNADPH Oxidase 2NeointimaOxidative StressReactive Oxygen SpeciesSignal TransductionTime FactorsTyrosineVascular Endothelial Growth Factor AVascular PatencyVena Cava, InferiorConceptsHeme oxygenase-1Arteriovenous fistulaAVF maturationNOX-2HIF-1αOxidative stressHypoxia-inducible factor 1 (HIF-1) expressionSham-operated micePoor clinical resultsHIF-1α immunoreactivityInferior vena cavaArteriovenous fistula maturationVascular endothelial growth factorHypoxia-inducible factor-1 (HIF-1) pathwayFactor-1 expressionEndothelial growth factorHIF-1 pathwayHuman AVF maturationQuantitative polymerase chain reactionOxidative stress increasesAortocaval fistulaFistula maturationVena cavaClinical resultsPolymerase chain reaction
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
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
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 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*
Lu T, Barreuther M, Davis S, Madri J. Platelet Endothelial Cell Adhesion Molecule-1 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*. Journal Of Biological Chemistry 1997, 272: 14442-14446. PMID: 9162084, DOI: 10.1074/jbc.272.22.14442.Peer-Reviewed Original ResearchConceptsSrc homology 2C-SrcGST-SrcCytoplasmic tailImmunoreceptor tyrosineCytoplasmic domain sequencesEndothelial cell adhesion molecule-1Src SH2 domainCell-cell bordersPECAM-1 functionsPECAM-1PECAM-1 phosphorylationUnidentified phosphoproteinsProtein associatesHomology 2Kinase assaysSignal transductionGlutathione S-transferaseSheet migrationConfluent endothelial cellsActivation motifConsensus sequenceDomain sequencesDomain interactionsEndothelial cellsPlatelet-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
1996
Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1.
Lu T, Yan L, Madri J. Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 11808-11813. PMID: 8876219, PMCID: PMC38140, DOI: 10.1073/pnas.93.21.11808.Peer-Reviewed Original Research3T3 CellsAnimalsCell AdhesionCell Adhesion MoleculesCell MovementCells, CulturedEndothelium, VascularFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansMaleMiceMutagenesis, Site-DirectedPhosphorylationPhosphotyrosinePlatelet Endothelial Cell Adhesion Molecule-1Protein Tyrosine PhosphatasesProtein-Tyrosine KinasesRatsRecombinant ProteinsTransfectionTyrosineUmbilical Veins
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