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 loopPECAM-1 promotes β-catenin accumulation and stimulates endothelial cell proliferation
Biswas P, Canosa S, Schoenfeld J, Schoenfeld D, Tucker A, Madri JA. PECAM-1 promotes β-catenin accumulation and stimulates endothelial cell proliferation. Biochemical And Biophysical Research Communications 2003, 303: 212-218. PMID: 12646189, DOI: 10.1016/s0006-291x(03)00313-9.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBeta CateninBlotting, WesternCell AdhesionCell DivisionCytoplasmCytoskeletal ProteinsEndotheliumFlow CytometryHumansLungMiceMice, KnockoutMicroscopy, FluorescencePlatelet Endothelial Cell Adhesion Molecule-1Precipitin TestsSignal TransductionTrans-ActivatorsTranscription, GeneticTransfectionConceptsPECAM-1-positive endothelial cellsBeta-catenin proteinCell proliferationEndothelial cellsPECAM-1Beta-catenin localizationCytoplasmic domainΒ-catenin accumulationFull-length PECAM-1Functional consequencesEndothelial cell proliferationCell membraneKnockout animalsAdhesion moleculesLess accumulationCellsAccumulationProliferative rateProliferationMembraneProteinBinds
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 VEGFpp60c-src Modulates Microvascular Endothelial Phenotype and in Vitro Angiogenesis
Marx M, Warren S, Madri J. pp60c-src Modulates Microvascular Endothelial Phenotype and in Vitro Angiogenesis. Experimental And Molecular Pathology 2001, 70: 201-213. PMID: 11417999, DOI: 10.1006/exmp.2001.2358.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsBecaplerminCell DivisionEndothelium, VascularGenes, srcGenetic VectorsMaleMicrocirculationMoloney murine leukemia virusNeovascularization, PhysiologicPlatelet-Derived Growth FactorProto-Oncogene Proteins c-sisProto-Oncogene Proteins pp60(c-src)RatsRecombinant ProteinsSignal TransductionTransfectionConceptsC-Src mutantC-SrcTwo-dimensional cultureThree-dimensional cultureWild-type c-SrcC-Src kinase activityC-Src tyrosine kinaseC-Src associatesC-src proteinPlatelet-derived growth factor receptorV-SrcPDGF signalCytoskeletal organizationGrowth factor receptorKinase activityCell shapeTyrosine kinaseVitro AngiogenesisTube-like structuresCell morphologyFactor receptorTube formationMutantsRegulatory effectsOverexpressionPECAM-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 cellsPECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics
ILAN N, MOHSENIN A, CHEUNG L, MADRI J. PECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics. The FASEB Journal 2001, 15: 362-372. PMID: 11156952, DOI: 10.1096/fj.00-0372com.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAnimalsAntigens, CDApoptosisBlood PlateletsCaspasesCattleCell DivisionCell LineCell MembraneCells, CulturedColonic NeoplasmsCulture MediaDipeptidesEndothelium, VascularEnzyme InhibitorsHumansPlatelet Endothelial Cell Adhesion Molecule-1Sequence DeletionSignal TransductionTransfectionTumor Cells, CulturedUmbilical VeinsConceptsFull-length PECAM-1Signal transduction cascadeSignal transduction eventsCaspase-8 cleavageCell proliferationPECAM-1SW480 colon carcinoma cellsCaspase substratesSHP-2Transduction cascadeTransduction eventsGrowth factor receptorCell adhesion moleculeGene constructsCell surface moleculesColon carcinoma cellsSoluble proteinStable expressionCell deathCulture mediumMatrix metalloproteinaseCell surfaceJNK phosphorylationUnique functionFactor receptor
2000
Matrix metalloproteinase activity is required for activity-induced angiogenesis in rat skeletal muscle
Haas T, Milkiewicz M, Davis S, Zhou A, Egginton S, Brown M, Madri J, Hudlicka O. Matrix metalloproteinase activity is required for activity-induced angiogenesis in rat skeletal muscle. AJP Heart And Circulatory Physiology 2000, 279: h1540-h1547. PMID: 11009439, DOI: 10.1152/ajpheart.2000.279.4.h1540.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCapillariesCell DivisionDipeptidesElectric StimulationImmunohistochemistryMatrix Metalloproteinase 2Matrix Metalloproteinase InhibitorsMatrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesMicroscopy, ElectronMotor ActivityMuscle, SkeletalNeovascularization, PhysiologicProtease InhibitorsRatsRNA, MessengerConceptsMembrane proteinsBasement membrane proteinsEndothelial cell sprout formationRat skeletal muscleSkeletal muscleMatrix metalloproteinasesMembrane type 1Inflammation-mediated angiogenesisPhysiological angiogenesisBasement membraneCell proliferationMMP proteolysisProtein levelsProteolysisSprout formationMajor classesCritical roleProteinMatrix metalloproteinase activityMetalloproteinase activityProliferationAngiogenesisNew capillariesMembraneMMP inhibition
1998
The synergistic activity of αvβ3 integrin and pdgf receptor increases cell migration
Woodard A, García-Cardeña G, Leong M, Madri J, Sessa W, Languino L. The synergistic activity of αvβ3 integrin and pdgf receptor increases cell migration. Journal Of Cell Science 1998, 111: 469-478. PMID: 9443896, DOI: 10.1242/jcs.111.4.469.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsAntigens, CDBecaplerminCell AdhesionCell DivisionCell MovementCells, CulturedEndothelium, VascularHumansIntegrin alphaVLamininMiceOligopeptidesPlatelet-Derived Growth FactorProto-Oncogene Proteins c-sisRatsReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorReceptors, VitronectinVitronectinConceptsMicrovascular endothelial cellsGrowth factor receptorGrowth factorEndothelial cellsFactor receptorCell migrationSynergistic activityPlatelet-derived growth factor receptorRat microvascular endothelial cellsAlphavbeta3 integrinGrowth factor-BBNIH 3T3 cellsTissue infiltrationFactor-BBNeovessel formationDifferent antibodiesPlateletsΑvβ3 integrinReceptorsAlphavbeta3Beta1 integrinCell's abilityIntegrinsCellsNovel pathway
1997
Nitric oxide production contributes to the angiogenic properties of vascular endothelial growth factor in human endothelial cells.
Papapetropoulos A, García-Cardeña G, Madri JA, Sessa WC. Nitric oxide production contributes to the angiogenic properties of vascular endothelial growth factor in human endothelial cells. Journal Of Clinical Investigation 1997, 100: 3131-3139. PMID: 9399960, PMCID: PMC508526, DOI: 10.1172/jci119868.Peer-Reviewed Original ResearchConceptsHuman umbilical vein endothelial cellsVascular endothelial growth factorPhosphoinositide-3 kinase inhibitorDimensional collagen gelsRegulator of vasculogenesisKinase inhibitorsGrowth of HUVECsGrowth factorExposure of cellsUmbilical vein endothelial cellsEndothelial cellsTyrosine kinaseHuman endothelial cellsVEGF stimulationSynthase proteinK kinaseEndothelial growth factorVein endothelial cellsProtein levelsEC proliferationKinaseHuman ECsDependent formationNO-dependent mannerShort-term stimulationVascular endothelial growth factor mediates reactive angiogenesis in the postnatal developing brain
Ment L, Stewart W, Fronc R, Seashore C, Mahooti S, Scaramuzzino D, Madri J. Vascular endothelial growth factor mediates reactive angiogenesis in the postnatal developing brain. Brain Research 1997, 100: 52-61. PMID: 9174246, DOI: 10.1016/s0165-3806(97)00012-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornAstrocytesCell DivisionCell HypoxiaCells, CulturedCerebral CortexCoculture TechniquesEndothelial Growth FactorsEndothelium, VascularHypoxia, BrainLymphokinesMicrocirculationNeovascularization, PathologicNeovascularization, PhysiologicRatsRats, Sprague-DawleyRNA, MessengerTranscription, GeneticVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsVascular endothelial growth factorEndothelial growth factorVEGF protein levelsExperimental ratsSublethal hypoxiaBrain microvascular endothelial cellsEndothelial cellsGrowth factorChronic sublethal hypoxiaProtein levelsAge-matched controlsMicrovascular endothelial cellsHypoxic pupsHRP studyCortical vesselsImmunohistochemical studyVascular densityAddition of VEGFBeagle pupsNewborn ratsReactive angiogenesisAstrocyte culturesThree-dimensional cocultureRat forebrainVEGF proteinNitric oxide synthase inhibitors attenuate transforming-growth-factor-beta 1-stimulated capillary organization in vitro.
Papapetropoulos A, Desai KM, Rudic RD, Mayer B, Zhang R, Ruiz-Torres MP, García-Cardeña G, Madri JA, Sessa WC. Nitric oxide synthase inhibitors attenuate transforming-growth-factor-beta 1-stimulated capillary organization in vitro. American Journal Of Pathology 1997, 150: 1835-44. PMID: 9137106, PMCID: PMC1858220.Peer-Reviewed Original ResearchConceptsNitric oxideL-NAMETube formationNOS isoformsNitric oxide synthase inhibitorL-nitro-arginine methylesterOxide synthase inhibitorNO donor sodium nitroprussideRole of NOTranscriptase-polymerase chain reactionExcess L-arginineDonor sodium nitroprussideSoluble guanylate cyclaseWestern blot analysisEndothelial cell proliferationNOS blockadeCapillary tube formationEndothelial NOSSodium nitroprussideSynthase inhibitorL-arginineMicrovascular ECsAutocrine productionGuanylate cyclaseCapillary organization
1996
Regulation of human colonic cell line proliferation and phenotype by sodium butyrate
Basson M, Turowski G, Rashid Z, Hong F, Madri J. Regulation of human colonic cell line proliferation and phenotype by sodium butyrate. Digestive Diseases And Sciences 1996, 41: 1986-1993. PMID: 8888712, DOI: 10.1007/bf02093601.Peer-Reviewed Original ResearchConceptsBrush border enzyme activitiesSerial cell countsCell line proliferationHuman colonic cellsColonic butyrateApparent protective actionColon carcinogenesisMalignant behaviorCell countButyrate effectMucosal differentiationColonic cellsProtective actionSodium butyrateCaco-2Surface expressionCollagen ICollagen IVDietary fiberProliferationRelevant concentrationsCarcinogenesisCultured cellsMotilityMatrix proteinsLaminin promotes differentiation of NB4 promyelocytic leukemia cells with all-trans retinoic acid.
Becker P, Li Z, Potselueva T, Madri J, Newburger P, Berliner N. Laminin promotes differentiation of NB4 promyelocytic leukemia cells with all-trans retinoic acid. Blood 1996, 88: 261-7. PMID: 8704182, DOI: 10.1182/blood.v88.1.261.bloodjournal881261.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CDBase SequenceCalciumCell Culture TechniquesCell DifferentiationCell DivisionCollagenDrug SynergismFibronectinsGene Expression Regulation, LeukemicHumansIntegrin alpha6Integrin beta1IonomycinIonophoresLamininLeukemia, Promyelocytic, AcuteMolecular Sequence DataNeoplasm ProteinsNeoplastic Stem CellsOxidation-ReductionPolymerase Chain ReactionReceptors, LamininTretinoinTumor Cells, CulturedConceptsAlpha 6 integrinTrans retinoic acidNB4 promyelocytic leukemia cellsPromyelocytic leukemia cellsMorphologic maturationLeukemia cellsRetinoic acidReverse transcription-polymerase chain reactionTranscription-polymerase chain reactionSecondary granule proteinsPresence of ionomycinPromyelocytic leukemia cell lineHistologic appearanceHours of exposureLeukemia cell linesMinimal maturationFlow cytometryHigh-level surface expressionDifferentiation agentsCollagen type INB4 cellsLaminin receptorATRAExtracellular matrix componentsCell proliferationModulation of transforming growth factor beta receptor levels on microvascular endothelial cells during in vitro angiogenesis.
Sankar S, Mahooti-Brooks N, Bensen L, McCarthy T, Centrella M, Madri J. Modulation of transforming growth factor beta receptor levels on microvascular endothelial cells during in vitro angiogenesis. Journal Of Clinical Investigation 1996, 97: 1436-1446. PMID: 8617876, PMCID: PMC507203, DOI: 10.1172/jci118565.Peer-Reviewed Original Research
1994
Glutamine modulates phenotype and stimulates proliferation in human colon cancer cell lines.
Turowski G, Rashid Z, Hong F, Madri J, Basson M. Glutamine modulates phenotype and stimulates proliferation in human colon cancer cell lines. Cancer Research 1994, 54: 5974-80. PMID: 7954430.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBeta-GalactosidaseCathepsin CCell AdhesionCell DifferentiationCell DivisionColonic NeoplasmsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDose-Response Relationship, DrugExtracellular Matrix ProteinsGlutamineHumansIntegrinsLactaseOligo-1,6-GlucosidasePhenotypeTumor Cells, CulturedConceptsMatrix proteinsHuman colon carcinoma cell lineColon carcinoma cell lineCell linesCarcinoma cell linesSurface expressionDigestive enzyme expressionGlutamine-free mediumCell-matrix interactionsColon cancer cell linesHuman colon cancer cell linesCaco-2 proliferationSerial cell countsIntegrin surface expressionSW620 cellsCancer cell linesDigestive enzymesProteinEnzyme expressionGlutamineSynthetic substratesAdherent cellsCathepsin CExpressionIntegrin expressionEffect of tyrosine kinase inhibition on basal and epidermal growth factor‐stimulated human Caco‐2 enterocyte sheet migration and proliferation
Basson M, Turowski G, Zarif A, Modlin I, Beidler D, Jena B, Madri J. Effect of tyrosine kinase inhibition on basal and epidermal growth factor‐stimulated human Caco‐2 enterocyte sheet migration and proliferation. Journal Of Cellular Physiology 1994, 160: 491-501. PMID: 8077287, DOI: 10.1002/jcp.1041600312.Peer-Reviewed Original ResearchConceptsEpidermal growth factorTyrosine kinaseTyrosine kinase regulationEGF-stimulated migrationProtein-linked DNA breaksSubstrate-binding siteTyrosine kinase inhibitor genisteinCell-matrix interactionsDNA topoisomerase activityKinase inhibitor genisteinKinase regulationATP bindingMonolayer expansionEGF stimulationSheet migrationSubunit organizationDNA breaksTopoisomerase activityEGF receptorInhibitor genisteinCell migrationCell proliferationKinase inhibitionTyrosine kinase inhibitionKinaseModulation of platelet-derived growth factor receptor expression in microvascular endothelial cells during in vitro angiogenesis.
Marx M, Perlmutter R, Madri J. Modulation of platelet-derived growth factor receptor expression in microvascular endothelial cells during in vitro angiogenesis. Journal Of Clinical Investigation 1994, 93: 131-139. PMID: 7506710, PMCID: PMC293745, DOI: 10.1172/jci116936.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsCell DivisionCells, CulturedElectrophoresis, Polyacrylamide GelEndothelium, VascularEpididymisImmunoblottingKineticsMaleMicrocirculationMolecular WeightNeovascularization, PathologicPlatelet-Derived Growth FactorRatsReceptors, Platelet-Derived Growth FactorRecombinant ProteinsTime FactorsConceptsMicrovascular endothelial cellsEndothelial cellsPDGF receptorReceptor expressionPlatelet-derived growth factor receptor expressionGrowth factor receptor expressionPDGF receptor expressionFactor receptor expressionPDGF receptor alphaReceptor surface expressionEndothelial cell growthNovel therapeutic applicationsCell growthSuramin treatmentProliferative responseEndothelial cell phenotypeReceptor alphaPDGF isoformsPDGF-AAInhibited proliferationReceptor regulationPDGF-BBPDGF-ABAngiogenesisCell proliferation
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 modulationIdentification 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
1991
Vascular cell responses to a hybrid Transforming Growth Factor-Beta molecule
Merwin J, Tucker A, Madisen L, Purchio A, Madri J. Vascular cell responses to a hybrid Transforming Growth Factor-Beta molecule. Biochemical And Biophysical Research Communications 1991, 175: 589-595. PMID: 1708238, DOI: 10.1016/0006-291x(91)91606-d.Peer-Reviewed Original Research