2011
GSK-3β: a signaling pathway node modulating neural stem cell and endothelial cell interactions
Li Q, Michaud M, Canosa S, Kuo A, Madri JA. GSK-3β: a signaling pathway node modulating neural stem cell and endothelial cell interactions. Angiogenesis 2011, 14: 173-185. PMID: 21253820, DOI: 10.1007/s10456-011-9201-9.Peer-Reviewed Original ResearchMeSH KeywordsAminophenolsAnimalsBasic Helix-Loop-Helix Transcription FactorsBeta CateninBrainCell CommunicationCell DifferentiationCell MovementCell ProliferationEndothelial CellsEnzyme ActivationGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHypoxia-Inducible Factor 1, alpha SubunitIntercellular Signaling Peptides and ProteinsMaleMaleimidesMiceMice, Inbred C57BLNeovascularization, PhysiologicNeural Stem CellsNeurogenesisPhosphorylationPhosphoserineReceptor Cross-TalkSignal TransductionSolubilitySpecies SpecificityConceptsNeural stem cellsNotch-1 expressionHIF-1αGSK-3βSDF-1III-tubulinStem cellsPremature infant populationMicrovascular endothelial cellsGSK-3β activationCD1 levelsEndothelial cell interactionsNeurogenic areasVascular proliferationInfant populationGSK-3β inhibitorTherapeutic potentialSVZ tissueGreater angiogenesisHIF-2αMouse strainsΒ-catenin participatesEndothelial cellsReciprocal modulation
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
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