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
2003
Transcriptional Up-regulation of Endothelial Cell Matrix Metalloproteinase-2 in Response to Extracellular Cues Involves GATA-2*
Han X, Boyd PJ, Colgan S, Madri JA, Haas TL. Transcriptional Up-regulation of Endothelial Cell Matrix Metalloproteinase-2 in Response to Extracellular Cues Involves GATA-2*. Journal Of Biological Chemistry 2003, 278: 47785-47791. PMID: 14512418, DOI: 10.1074/jbc.m309482200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBlotting, NorthernBlotting, WesternCell NucleusCells, CulturedCollagenCOS CellsDNA-Binding ProteinsEndothelial CellsExtracellular MatrixGATA2 Transcription FactorGelatinGenes, ReporterLuciferasesMatrix Metalloproteinase 2MicrocirculationMolecular Sequence DataNeovascularization, PhysiologicPhenotypePromoter Regions, GeneticProtein BindingRatsTranscription FactorsTranscription, GeneticTranscriptional ActivationTransfectionUp-RegulationPlatelet–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
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 timeActivation
1999
Egr-1 Mediates Extracellular Matrix-driven Transcription of Membrane Type 1 Matrix Metalloproteinase in Endothelium*
Haas T, Stitelman D, Davis S, Apte S, Madri J. Egr-1 Mediates Extracellular Matrix-driven Transcription of Membrane Type 1 Matrix Metalloproteinase in Endothelium*. Journal Of Biological Chemistry 1999, 274: 22679-22685. PMID: 10428849, DOI: 10.1074/jbc.274.32.22679.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCloning, MolecularDNA-Binding ProteinsEarly Growth Response Protein 1Endothelium, VascularExtracellular MatrixGene Expression Regulation, EnzymologicHalf-LifeImmediate-Early ProteinsMatrix Metalloproteinase 14Matrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesMiceMolecular Sequence DataNeovascularization, PhysiologicProtein BindingRatsRNA, MessengerSp1 Transcription FactorTranscription FactorsTranscription, GeneticUp-RegulationConceptsMembrane type 1 matrix metalloproteinaseEgr-1MT1-MMPTranscription factor Egr-1Number of proteinsExtracellular matrix environmentEnhanced transcriptional activityEndothelial cellsTranscriptional activityPromoter correlatesIncreased transcriptionCellular invasionInvasive phenotypeMatrix metalloproteinaseTranscriptionMatrix environmentMatrix metalloproteinase activityMetalloproteinase activityCellsMatrix metalloproteinasesInvasionIncrease productionAngiogenesisMetalloproteinaseProtein
1995
Expression of Transforming Growth Factor Type III Receptor in Vascular Endothelial Cells Increases Their Responsiveness to Transforming Growth Factor β2 ∗
Sankar S, Mahooti-Brooks N, Centrella M, McCarthy T, Madri J. Expression of Transforming Growth Factor Type III Receptor in Vascular Endothelial Cells Increases Their Responsiveness to Transforming Growth Factor β2 ∗. Journal Of Biological Chemistry 1995, 270: 13567-13572. PMID: 7768960, DOI: 10.1074/jbc.270.22.13567.Peer-Reviewed Original ResearchConceptsTGF beta 2Type II receptorBovine aortic endothelial cellsTGF beta 1Receptor proteinType III receptorII receptorsBeta 2TGF-beta type III receptorBeta 1Serine-threonine kinaseInhibitor-1 proteinPlasminogen activator inhibitor-1 proteinEndothelial cellsTGF beta sGrowth factor betaGrowth factor β2Inhibition of migrationVascular endothelial cellsSignaling capacityType IAortic endothelial cellsReceptor cDNAReceptor complexProtein