2015
Cell–extracellular matrix interactions in oral tumorigenesis: Roles of podoplanin and CD44 and modulation of Hippo pathway
Tsuneki M, Madri J, Saku T. Cell–extracellular matrix interactions in oral tumorigenesis: Roles of podoplanin and CD44 and modulation of Hippo pathway. Journal Of Oral Biosciences 2015, 57: 45-53. DOI: 10.1016/j.job.2015.02.004.Peer-Reviewed Original ResearchCell-extracellular matrix interactionsHippo pathwayExtracellular matrixDynamic reciprocal interactionsMatrix interactionsCell surfaceHyaluronan-rich extracellular matrixMultifunctional transmembrane proteinBasolateral cell surfaceVascular endothelialEndothelial cell survivalAdhesion moleculesStromal cellsVascular endothelial cell survivalTransmembrane proteinMurine hemangioendothelioma cellsTumor cellsSquamous cell carcinoma cellsOral squamous cell carcinoma cellsCell survivalContact inhibitionVE-cadherinTissue architectureTumor survivalIntercellular spaces
2001
PECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics
ILAN N, MOHSENIN A, CHEUNG L, MADRI J. PECAM‐1 shedding during apoptosis generates a membrane‐anchored truncated molecule with unique signaling characteristics. The FASEB Journal 2001, 15: 362-372. PMID: 11156952, DOI: 10.1096/fj.00-0372com.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAnimalsAntigens, CDApoptosisBlood PlateletsCaspasesCattleCell DivisionCell LineCell MembraneCells, CulturedColonic NeoplasmsCulture MediaDipeptidesEndothelium, VascularEnzyme InhibitorsHumansPlatelet Endothelial Cell Adhesion Molecule-1Sequence DeletionSignal TransductionTransfectionTumor Cells, CulturedUmbilical VeinsConceptsFull-length PECAM-1Signal transduction cascadeSignal transduction eventsCaspase-8 cleavageCell proliferationPECAM-1SW480 colon carcinoma cellsCaspase substratesSHP-2Transduction cascadeTransduction eventsGrowth factor receptorCell adhesion moleculeGene constructsCell surface moleculesColon carcinoma cellsSoluble proteinStable expressionCell deathCulture mediumMatrix metalloproteinaseCell surfaceJNK phosphorylationUnique functionFactor receptor
1999
Extracellular Matrix-Driven Matrix Metalloproteinase Production in Endothelial Cells Implications for Angiogenesis
Haas T, Madri J. Extracellular Matrix-Driven Matrix Metalloproteinase Production in Endothelial Cells Implications for Angiogenesis. Trends In Cardiovascular Medicine 1999, 9: 70-77. PMID: 10578520, DOI: 10.1016/s1050-1738(99)00014-6.Peer-Reviewed Original ResearchConceptsInterstitial matrix moleculesCell-extracellular matrix interactionsBasement membrane matrixMatrix metalloproteinasesTranscriptional activationBlood vessel growthMatrix interactionsNew blood vessel growthMatrix moleculesCell surfaceExtracellular matrixMT1-MMPAdjacent cellsCell interactionsMatrix metalloproteinase productionCurrent understandingVessel growthParticular matrix metalloproteinasesEndothelial cell interactionsPotential roleAngiogenesisMetalloproteinase productionBasement membraneMMP-2Signaling
1993
Spatial organization of the extracellular matrix modulates the expression of PDGF-receptor subunits in mesangial cells
Marx M, Daniel T, Kashgarian M, Madri J. Spatial organization of the extracellular matrix modulates the expression of PDGF-receptor subunits in mesangial cells. Kidney International 1993, 43: 1027-1041. PMID: 8510381, DOI: 10.1038/ki.1993.145.Peer-Reviewed Original ResearchConceptsPDGF receptor subunitsMesangial cell phenotypeCell surfaceExtracellular matrixCell phenotypeExtracellular matrix environmentSpatial organizationPDGF responsivenessPDGF receptor alphaTwo-dimensional cultureMulticellular structuresThree-dimensional cultureMetabolic labelingDifferential expressionQuiescent cellsRat mesangial cell growthCell growthPDGF isoforms AASubunitsMatrix environmentCell proliferationPDGF isoformsReceptor subunitsUltrastructural analysisSurface expression
1992
Modulation of vascular cell behavior by transforming growth factors β
Madri J, Bell L, Merwin J. Modulation of vascular cell behavior by transforming growth factors β. Molecular Reproduction And Development 1992, 32: 121-126. PMID: 1637550, DOI: 10.1002/mrd.1080320207.Peer-Reviewed Original ResearchConceptsVascular cell typesCell typesCellular responsesCell surfaceTGF-beta receptorsVascular cell behaviorGrowth factor βDistinct bioassaysDifferent isoformsCell migrationCell behaviorInhibition of proliferationVascular cell responsesSmooth muscle cellsUnique binding profileAngiogenic assaysIsoformsBinding profileCell populationsBovine aortic endothelialFactor βMuscle cellsType IBASMCsAortic endothelial
1990
A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV
Yannariello-Brown J, Madri J. A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV. Biochemical Journal 1990, 265: 383-392. PMID: 2154186, PMCID: PMC1136898, DOI: 10.1042/bj2650383.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell MembraneCells, CulturedChromatography, AffinityChymotrypsinCollagenElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEndothelium, VascularFluorescent Antibody TechniqueImmune SeraMolecular WeightPeptide MappingPhosphoproteinsReceptors, Cell SurfaceReceptors, CollagenConceptsBovine aortic endothelial cellsSDS/PAGENon-equilibrium pH gel electrophoresisCollagen type IVCollagenous domainTwo-dimensional gel systemAortic endothelial cellsAdhesion assaysCell surface populationIndirect immunofluorescence experimentsGlobular NC1 domainCell surface labelingCollagen-binding proteinsChymotryptic peptide mapsEndothelial cellsGlobular domainIntracellular transportMinor isoformIndividual isoformsImmunofluorescence experimentsMolecular massGolgi regionCollagenous regionCell surfacePeptide maps
1987
Dependence on pH of polarized sorting of secreted proteins
Caplan M, Stow J, Newman A, Madri J, Anderson H, Farquhar M, Palade G, Jamieson J. Dependence on pH of polarized sorting of secreted proteins. Nature 1987, 329: 632-635. PMID: 2821405, DOI: 10.1038/329632a0.Peer-Reviewed Original ResearchConceptsSecretory proteinsMDCK cellsDifferent protein compositionsBasolateral cell surfacePolarized sortingMembrane proteinsBasolateral domainDefault pathwayPlasma membraneAcidic intracellular compartmentsIntracellular compartmentsProtein compositionMembrane componentsCell surfaceBasement membrane componentsProteinSecrete lamininDistinct setsRenal tubule cellsEpithelial cellsActive sortingBasolateral compartmentCellsSecretory productsSpecific regions
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
1980
The collagenous components of the subendothelium. Correlation of structure and function.
Madri J, Dreyer B, Pitlick F, Furthmayr H. The collagenous components of the subendothelium. Correlation of structure and function. Laboratory Investigation 1980, 43: 303-15. PMID: 7003251.Peer-Reviewed Original ResearchConceptsCell surfaceEndothelial cell surfaceEndothelial cellsSpecific immunoprecipitation techniquesBiosynthetic incorporationImmunofluorescence microscopyImmunoelectron microscopyImmunoprecipitation techniquesAB2 collagenCellsCollagenous componentsAggregation occursCorrelation of structureCollagen typesImportant roleMonolayer of endotheliumCollagenPlatelet adhesionPlatelet aggregationImportant determinantNonthrombogenic surfaceVascular wallTreesType IVAdhesion
1979
Isolation and tissue localization of type AB2 collagen from normal lung parenchyma.
Madri J, Furthmayr H. Isolation and tissue localization of type AB2 collagen from normal lung parenchyma. American Journal Of Pathology 1979, 94: 323-31. PMID: 371411, PMCID: PMC2042247.Peer-Reviewed Original ResearchConceptsNormal lung parenchymaLung parenchymaAffinity-purified rabbit antibodiesLung tissuePassive hemagglutinationPlacental membranesChorionic membraneAB2 collagenTissue localizationIndirect immunofluorescence microscopyRabbit antibodiesBasement membraneChain ratioParenchymaImmunofluorescence microscopyCollagenPolyacrylamide gel electrophoresisGel electrophoresisAlpha ADifferential salt extractionCell surface