2017
As 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
2005
Identification of the regions of PECAM-1 involved in β- and γ-catenin associations
Biswas P, Zhang J, Schoenfeld JD, Schoenfeld D, Gratzinger D, Canosa S, Madri JA. Identification of the regions of PECAM-1 involved in β- and γ-catenin associations. Biochemical And Biophysical Research Communications 2005, 329: 1225-1233. PMID: 15766557, DOI: 10.1016/j.bbrc.2005.02.095.Peer-Reviewed Original Research
2001
Focal 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 timeActivationPECAM‐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
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
1998
Distinct signal transduction pathways are utilized during the tube formation and survival phases of in vitro angiogenesis
Ilan N, Mahooti S, Madri J. Distinct signal transduction pathways are utilized during the tube formation and survival phases of in vitro angiogenesis. Journal Of Cell Science 1998, 111: 3621-3631. PMID: 9819353, DOI: 10.1242/jcs.111.24.3621.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCalcium-Calmodulin-Dependent Protein KinasesCapillariesCell Culture TechniquesCell LineCell SurvivalCollagenEndothelial Growth FactorsEndothelium, VascularExtracellular MatrixHumansLymphokinesNeovascularization, PhysiologicPhosphatidylinositol 3-KinasesPhosphorylationProtein Kinase CProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionTetradecanoylphorbol AcetateVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsHuman umbilical vein endothelial cellsAkt/PKB pathwayTube formationDistinct signal transduction pathwaysAkt/PKBSignal transduction pathwaysDifferent ECM proteinsCollagen gelsExtracellular matrix componentsPeptide growth factorsPKB pathwayProtein kinaseTransduction pathwaysMAP kinaseUmbilical vein endothelial cellsECM proteinsVein endothelial cellsNew blood vesselsPre-existing onesKinaseMajor groupsVivo angiogenesisRapid inductionMatrix componentsSurvival phase
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 proteins
1994
Effect 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 inhibitionKinaseThe induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent.
Romanic A, Madri J. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. Journal Of Cell Biology 1994, 125: 1165-1178. PMID: 7515069, PMCID: PMC2120055, DOI: 10.1083/jcb.125.5.1165.Peer-Reviewed Original ResearchConceptsVascular cell adhesion molecule-1Recombinant VCAM-1T cellsT cell transmigrationEndothelial cellsNegative endothelial cellsCell transmigrationCell adhesion molecule-1Transmigrated T cellsExperimental autoimmune encephalomyelitisT cell extravasationAdhesion molecule-1Late antigen-4VCAM-1 positive cellsMyelin basic proteinAutoimmune encephalomyelitisEndothelial cell monolayersAntigen-4Brain parenchymaNormal miceEndothelial cell layerPositive cellsMolecule-1Perivascular tissueT cell adhesion
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 modulation
1989
Modulation of actin mRNAs in cultured vascular cells by matrix components and TGF-β1
Kocher O, Madri J. Modulation of actin mRNAs in cultured vascular cells by matrix components and TGF-β1. In Vitro Cellular & Developmental Biology 1989, 25: 424-434. PMID: 2659578, DOI: 10.1007/bf02624627.Peer-Reviewed Original ResearchConceptsTwo-dimensional cultureActin mRNAEndothelial cell populationSmooth muscle cellsIndividual extracellular matrix proteinsSmooth muscle cell differentiationCell typesRat capillary endothelial cellsMuscle cell differentiationActin mRNA expressionThree-dimensional type ISkeletal muscle cellsMatrix componentsExtracellular matrix proteinsCell populationsCytoplasmic actin mRNAsMuscle actin mRNAEndothelial cellsMuscle cellsSmooth muscle cell markersExtracellular matrix componentsCultured vascular cellsΑ-SM actinBovine aortic endothelial cellsMuscle cell markers
1988
Extracellular matrix specificity for the differentiation of capillary endothelial cells
Carley W, Milici A, Madri J. Extracellular matrix specificity for the differentiation of capillary endothelial cells. Experimental Cell Research 1988, 178: 426-434. PMID: 3049122, DOI: 10.1016/0014-4827(88)90411-9.Peer-Reviewed Original ResearchConceptsExtracellular matrixCapillary endothelial cellsEndothelial cellsSpecific extracellular matrixEndothelial cell migrationVivo phenotypeDifferentiated phenotypeCell migrationCell typesCell growthCell dedifferentiationEndothelial cell growthMatrix componentsMembrane structurePhenotypeCellsExpressionCulture methodCytoplasmProteinGrowthMadinDifferentiationDedifferentiationGreater number
1983
Ultrastructural morphology and domain structure of a unique collagenous component of basement membranes.
Madri J, Foellmer H, Furthmayr H. Ultrastructural morphology and domain structure of a unique collagenous component of basement membranes. Biochemistry 1983, 22: 2797-804. PMID: 6409144, DOI: 10.1021/bi00281a005.Peer-Reviewed Original Research
1982
Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment.
Rao C, Margulies I, Tralka T, Terranova V, Madri J, Liotta L. Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment. Journal Of Biological Chemistry 1982, 257: 9740-9744. PMID: 7107589, DOI: 10.1016/s0021-9258(18)34135-8.Peer-Reviewed Original ResearchConceptsElectron microscopySubunits of lamininGlobular end regionsBeta subunitLaminin short armsTumor cellsWhole laminin moleculeAlpha subunitSquamous carcinoma cellsHuman squamous carcinoma cellsMicroscopyCell attachmentLaminin moleculeAttachment propertiesCarcinoma cellsTumor cell attachmentBasement membraneLong armAlpha-thrombin