2002
Disrupted synaptic development in the hypoxic newborn brain
Curristin SM, Cao A, Stewart WB, Zhang H, Madri JA, Morrow JS, Ment LR. Disrupted synaptic development in the hypoxic newborn brain. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 15729-15734. PMID: 12438650, PMCID: PMC137784, DOI: 10.1073/pnas.232568799.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornApoptosisAtmosphere Exposure ChambersBrain Damage, ChronicCell DifferentiationCytoskeletonDisease Models, AnimalDNA, ComplementaryEndothelial Growth FactorsGene Expression ProfilingHypoxiaHypoxia, BrainHypoxia-Inducible Factor 1, alpha SubunitIntercellular Signaling Peptides and ProteinsLymphokinesMembrane ProteinsMiceMice, Inbred C57BLMicrotubulesNerve Tissue ProteinsOligodendrogliaOligonucleotide Array Sequence AnalysisStress, PhysiologicalSynapsesSynaptic TransmissionTranscription FactorsTranscription, GeneticVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsPostnatal hypoxiaCerebral maturationGlial maturationNewborn brainSynaptic maturationPresynaptic functionPostsynaptic functionSublethal hypoxiaSynaptic developmentHealth crisisHypoxiaCognitive disabilitiesBrainMaturation programMaturationDysynchronyNeuropathologyInfantsNeurotransmissionCohortProtein assaysMiceHypoxic
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
1986
Basement membrane as a spatial organizer of polarized epithelia. Exogenous basement membrane reorients pancreatic epithelial tumor cells in vitro.
Ingber DE, Madri JA, Jamieson JD. Basement membrane as a spatial organizer of polarized epithelia. Exogenous basement membrane reorients pancreatic epithelial tumor cells in vitro. American Journal Of Pathology 1986, 122: 129-39. PMID: 3942197, PMCID: PMC1888129.Peer-Reviewed Original ResearchConceptsDistinct membrane domainsEpithelial cell-cell interactionsCell shape changesCell-cell interactionsAcinar tumor cellsMembrane domainsTumor cellsBasement membranePolarized distributionSpatial organizersGolgi complexProtein synthesisIndividual cellsCell surfaceLipid dropletsIntracellular actinPancreatic acinar carcinomaJunctional complexesEpithelial tumor cellsCell contactCytoskeletal alterationsAmniotic basement membraneEpithelial orientationIntact basement membraneZymogen granules