2014
Adhesion Molecule-Mediated Hippo Pathway Modulates Hemangioendothelioma Cell Behavior
Tsuneki M, Madri JA. Adhesion Molecule-Mediated Hippo Pathway Modulates Hemangioendothelioma Cell Behavior. Molecular And Cellular Biology 2014, 34: 4485-4499. PMID: 25266662, PMCID: PMC4248725, DOI: 10.1128/mcb.00671-14.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDApoptosisBrainCadherinsCaspase 3Cell Line, TumorCell ProliferationHemangioendotheliomaHippo Signaling PathwayImidazolesInhibitor of Apoptosis ProteinsLIM Domain ProteinsMiceMice, Inbred C57BLNaphthoquinonesPlatelet Endothelial Cell Adhesion Molecule-1Protein Serine-Threonine KinasesRepressor ProteinsRNA, Small InterferingSignal TransductionSurvivinConceptsHippo pathwayCell adhesion moleculeAjuba expressionCell proliferationAdhesion moleculesSmall interference RNA transfectionEffector caspase-3Murine hemangioendothelioma cellsPromoter interactionsApoptotic mechanismsMolecule modulationCell behaviorContact inhibitionEndothelial cell proliferationRNA transfectionVE-cadherinCaspase-3Microvascular endothelial cell proliferationApoptosisHemangioendothelioma cellsPathwayCell culturesProliferationEndothelial cell adhesion moleculesExpressionNEU1 Sialidase Regulates the Sialylation State of CD31 and Disrupts CD31-driven Capillary-like Tube Formation in Human Lung Microvascular Endothelia*
Lee C, Liu A, Miranda-Ribera A, Hyun SW, Lillehoj EP, Cross AS, Passaniti A, Grimm PR, Kim BY, Welling PA, Madri JA, DeLisser HM, Goldblum SE. NEU1 Sialidase Regulates the Sialylation State of CD31 and Disrupts CD31-driven Capillary-like Tube Formation in Human Lung Microvascular Endothelia*. Journal Of Biological Chemistry 2014, 289: 9121-9135. PMID: 24550400, PMCID: PMC3979388, DOI: 10.1074/jbc.m114.555888.Peer-Reviewed Original ResearchConceptsHuman pulmonary microvascular ECsCapillary-like tube formationEC tube formationTube formationCell adhesion molecule-1Pulmonary microvascular ECsHuman Lung Microvascular EndotheliaNeu1 sialidaseLung microvascular endotheliumAdhesion molecule-1Endothelial cell adhesion molecule-1Platelet endothelial cell adhesion molecule-1Endothelial cell expressionMultiplicity of infectionMicrovascular endotheliumMolecule-1Microvascular ECsCell expressionCD31Matrigel substrateSialylation statePeanut agglutinin lectinAdhesion moleculesInhibitory effectAngiogenic phenotypeCD44 Regulation of Endothelial Cell Proliferation and Apoptosis via Modulation of CD31 and VE-cadherin Expression*
Tsuneki M, Madri JA. CD44 Regulation of Endothelial Cell Proliferation and Apoptosis via Modulation of CD31 and VE-cadherin Expression*. Journal Of Biological Chemistry 2014, 289: 5357-5370. PMID: 24425872, PMCID: PMC3937614, DOI: 10.1074/jbc.m113.529313.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDApoptosisCadherinsCell AdhesionCell ProliferationCells, CulturedEndothelial CellsGene Expression RegulationHippo Signaling PathwayHyaluronan ReceptorsInhibitor of Apoptosis ProteinsMiceMice, KnockoutPlatelet Endothelial Cell Adhesion Molecule-1Protein Serine-Threonine KinasesProtein Structure, TertiaryRepressor ProteinsSurvivinConceptsVE-cadherin expressionHippo pathwayYAP nuclear localizationCortical membrane proteinsAdhesion protein expressionInitiator caspasesMembrane proteinsNuclear localizationCaspase cascadeEndothelial cellsHigh cell densityCritical regulatorCD44 regulationJunctional integrityKey roleCell behaviorEndothelial cell proliferationCell growthDiverse arrayCell proliferationVascular barrier integrityProtein expressionRole of CD44Pathway activationMurine CD44
2001
PECAM‐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
Distinct roles for matrix metalloproteinase-2 and α4 integrin in autoimmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis
Graesser D, Mahooti S, Madri J. Distinct roles for matrix metalloproteinase-2 and α4 integrin in autoimmune T cell extravasation and residency in brain parenchyma during experimental autoimmune encephalomyelitis. Journal Of Neuroimmunology 2000, 109: 121-131. PMID: 10996214, DOI: 10.1016/s0165-5728(00)00275-7.Peer-Reviewed Original ResearchConceptsMatrix metalloproteinase-2Auto-reactive T cellsExpression of alpha4T cellsMetalloproteinase-2Human multiple sclerosisExperimental autoimmune encephalomyelitisT cell extravasationMMP-2 inductionCentral nervous systemAutoimmune encephalomyelitisMultiple sclerosisAutoimmune diseasesBrain parenchymaNervous systemΑ4 integrinAlpha4 integrinsCell extravasationIndependent roleEAEAlpha4Basement membrane matrixInductionDistinct rolesIntegrins
1998
The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis.
Graesser D, Mahooti S, Haas T, Davis S, Clark R, Madri J. The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis. Laboratory Investigation 1998, 78: 1445-58. PMID: 9840619.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDCell AdhesionCell MembraneCell MovementCells, CulturedClone CellsEncephalomyelitis, Autoimmune, ExperimentalEndothelium, VascularGelatinasesIntegrin alpha4Matrix Metalloproteinase 14Matrix Metalloproteinase 2Matrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesMiceMice, Inbred StrainsProtease InhibitorsT-LymphocytesTissue Inhibitor of Metalloproteinase-2TransfectionConceptsExperimental autoimmune encephalomyelitisT cell clonesRecombinant vascular cell adhesion molecule-1Autoreactive T cell clonesAlpha4 integrinsMMP-2EAE inductionAutoimmune encephalomyelitisMyelin basic protein-reactive T cell clonesDisease processMatrix metalloproteinaseVascular cell adhesion molecule-1Cell adhesion molecule-1Human multiple sclerosisSusceptible mouse strainsAdhesion molecule-1T cell transmigrationMatrix metalloproteinase-2Microvascular endothelial cellsAlpha4 integrin expressionExpression of alpha4Adoptive transferMultiple sclerosisMouse modelEndothelial cell layerThe 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
1996
Laminin 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 proliferation
1994
Expression of a functional human complement inhibitor in a transgenic pig as a model for the prevention of xenogeneic hyperacute organ rejection.
Fodor W, Williams B, Matis L, Madri J, Rollins S, Knight J, Velander W, Squinto S. Expression of a functional human complement inhibitor in a transgenic pig as a model for the prevention of xenogeneic hyperacute organ rejection. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 11153-11157. PMID: 7526391, PMCID: PMC45185, DOI: 10.1073/pnas.91.23.11153.Peer-Reviewed Original ResearchConceptsHuman complement inhibitorsHyperacute rejectionComplement inhibitorsAnti-porcine antibodiesTerminal complement inhibitorTransgenic pigsXenogeneic transplantation modelPorcine cell typesHigh-level cell surface expressionVariety of murineXenogeneic complementsXenogeneic organ transplantationGraft failureOrgan rejectionVessel occlusionCell surface expressionHyperacute organ rejectionTransplantation modelOrgan transplantationXenogeneic organsVascular endotheliumTransgenic miceSerum complementAutologous complementTransplantation