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
1982
Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment.
Rao C, Margulies I, Tralka T, Terranova V, Madri J, Liotta L. Isolation of a subunit of laminin and its role in molecular structure and tumor cell attachment. Journal Of Biological Chemistry 1982, 257: 9740-9744. PMID: 7107589, DOI: 10.1016/s0021-9258(18)34135-8.Peer-Reviewed Original ResearchConceptsElectron microscopySubunits of lamininGlobular end regionsBeta subunitLaminin short armsTumor cellsWhole laminin moleculeAlpha subunitSquamous carcinoma cellsHuman squamous carcinoma cellsMicroscopyCell attachmentLaminin moleculeAttachment propertiesCarcinoma cellsTumor cell attachmentBasement membraneLong armAlpha-thrombin
1981
Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix
Engel J, Odermatt E, Engel A, Madri J, Furthmayr H, Rohde H, Timpl R. Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. Journal Of Molecular Biology 1981, 150: 97-120. PMID: 6795355, DOI: 10.1016/0022-2836(81)90326-0.Peer-Reviewed Original ResearchRole of basal lamina in neoplastic disorganization of tissue architecture.
Ingber D, Madri J, Jamieson J. Role of basal lamina in neoplastic disorganization of tissue architecture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1981, 78: 3901-3905. PMID: 7022458, PMCID: PMC319681, DOI: 10.1073/pnas.78.6.3901.Peer-Reviewed Original Research