2009
Bone Marrow Monocyte PECAM-1 Deficiency Elicits Increased Osteoclastogenesis Resulting in Trabecular Bone Loss
Wu Y, Tworkoski K, Michaud M, Madri JA. Bone Marrow Monocyte PECAM-1 Deficiency Elicits Increased Osteoclastogenesis Resulting in Trabecular Bone Loss. The Journal Of Immunology 2009, 182: 2672-2679. PMID: 19234161, DOI: 10.4049/jimmunol.0802398.Peer-Reviewed Original ResearchMeSH KeywordsAgingAnimalsBone Marrow CellsBone ResorptionCell DifferentiationCells, CulturedDown-RegulationFemaleIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutMonocytesOsteoclastsOsteogenesisPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein-Tyrosine KinasesSyk KinaseZAP-70 Protein-Tyrosine KinaseConceptsOsteoclast-like cellsKO miceBone marrowPECAM-1-null miceTrabecular bone lossPECAM-1Trabecular bone volumeSize of osteoclastsNF-kappaB ligandOsteoclast precursor culturesSHP-1 interactionsNumber of trabeculaeWT miceBM monocytesBone lossBone resorptionReceptor activatorBone volumeSHP-1Precursor culturesNull miceMiceLong bonesSyk kinaseFurther studies
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
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-cateninCatenin
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
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 inhibitionKinase