1995
Expression of Transforming Growth Factor Type III Receptor in Vascular Endothelial Cells Increases Their Responsiveness to Transforming Growth Factor β2 ∗
Sankar S, Mahooti-Brooks N, Centrella M, McCarthy T, Madri J. Expression of Transforming Growth Factor Type III Receptor in Vascular Endothelial Cells Increases Their Responsiveness to Transforming Growth Factor β2 ∗. Journal Of Biological Chemistry 1995, 270: 13567-13572. PMID: 7768960, DOI: 10.1074/jbc.270.22.13567.Peer-Reviewed Original ResearchConceptsTGF beta 2Type II receptorBovine aortic endothelial cellsTGF beta 1Receptor proteinType III receptorII receptorsBeta 2TGF-beta type III receptorBeta 1Serine-threonine kinaseInhibitor-1 proteinPlasminogen activator inhibitor-1 proteinEndothelial cellsTGF beta sGrowth factor betaGrowth factor β2Inhibition of migrationVascular endothelial cellsSignaling capacityType IAortic endothelial cellsReceptor cDNAReceptor complexProtein
1993
Fibronectin expression correlates with U937 cell adhesion to migrating bovine aortic endothelial cells in vitro.
Hauser I, Setter E, Bell L, Madri J. Fibronectin expression correlates with U937 cell adhesion to migrating bovine aortic endothelial cells in vitro. American Journal Of Pathology 1993, 143: 173-80. PMID: 7686342, PMCID: PMC1886955.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell AdhesionCell MovementCells, CulturedDrug ResistanceEndothelium, VascularFibronectinsFluorescent Antibody TechniqueHumansIntegrinsLeukemia, Promyelocytic, AcuteNeomycinProto-Oncogene MasProto-Oncogene Proteins pp60(c-src)Transforming Growth Factor betaTumor Cells, CulturedConceptsCell adhesionU937 cell adhesionEndothelial cell populationSRC proto-oncogeneEndothelial cellsCell populationsExtracellular matrix componentsEndothelial cell migrationBovine aortic endothelial cellsExtracellular matrix synthesisDenudation injuryFibronectin depositionCell migrationProto-oncogeneVascular endothelial cellsU937 cellsAortic endothelial cellsAmount of fibronectinMatrix componentsMigratory responseEndothelial cell monolayersMatrix synthesisCellsCell monolayersAdhesion
1992
Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells.
Qian S, Burmester J, Merwin J, Madri J, Sporn M, Roberts A. Identification of a structural domain that distinguishes the actions of the type 1 and 2 isoforms of transforming growth factor beta on endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6290-6294. PMID: 1631120, PMCID: PMC49486, DOI: 10.1073/pnas.89.14.6290.Peer-Reviewed Original ResearchConceptsEndothelial cellsFetal bovine heart endothelial cellsMicrovascular endothelial cellsGrowth factor betaHeart endothelial cellsAortic endothelial cellsBovine aortic endothelial cellsFactor betaType 1Amino acids 40Beta moleculesInhibition of growthAmino acids 1Biological potencyCellsGreater activity
1991
Vascular cells respond differentially to transforming growth factors beta 1 and beta 2 in vitro.
Merwin J, Newman W, Beall L, Tucker A, Madri J. Vascular cells respond differentially to transforming growth factors beta 1 and beta 2 in vitro. American Journal Of Pathology 1991, 138: 37-51. PMID: 1846264, PMCID: PMC1886039.Peer-Reviewed Original ResearchConceptsBovine aortic endothelial cellsBovine aortic smooth muscle cellsGrowth factorGrowth factor beta 1Aortic smooth muscle cellsTGF-beta concentrationsSmooth muscle cellsProliferation of BAECsTGF-beta receptorsBovine aortic endothelial cell migrationType IAortic endothelial cellsTGF beta sCell typesMicrovascular endotheliumVascular cell typesReceptor assayMuscle cellsVascular cellsEndothelial cellsBeta 1Endothelial cell migrationBeta 2Angiogenic assaysBASMCs
1990
Alternative splicing of endothelial cell fibronectin mRNA in the IIICS region. Functional significance.
Kocher O, Kennedy S, Madri J. Alternative splicing of endothelial cell fibronectin mRNA in the IIICS region. Functional significance. American Journal Of Pathology 1990, 137: 1509-24. PMID: 2260635, PMCID: PMC1877716.Peer-Reviewed Original ResearchConceptsAlternative splicingIIICS regionBovine aortic endothelial cellsHuman umbilical vein endothelial cell cDNA libraryRecombinant proteinsEndothelial cell cDNA libraryCell cDNA librarySpecific gene expressionSmooth muscle cellsAortic endothelial cellsEndothelial cellsMuscle cellsB16F10 melanoma cellsMelanoma cellsVascular cell functionCell attachmentFibronectin mRNACDNA clonesCDNA libraryRGDS sequenceGene expressionDNA fragmentsSplicingSequence analysisDifferent cell populationsInfluence of the angiotensin system on endothelial and smooth muscle cell migration.
Bell L, Madri J. Influence of the angiotensin system on endothelial and smooth muscle cell migration. American Journal Of Pathology 1990, 137: 7-12. PMID: 2164777, PMCID: PMC1877705.Peer-Reviewed Original ResearchConceptsSmooth muscle cell migrationVessel wall responseMuscle cell migrationBovine aortic endothelial cellsAortic smooth muscle cell migrationMedial smooth muscle cellsEndothelial cellsAngiotensin system componentsIle8-angiotensin IIEnzyme inhibitor lisinoprilSmooth muscle cellsCell migrationAortic endothelial cellsAngiotensin systemAngiotensin-converting enzyme inhibitor lisinoprilInhibitor lisinoprilLuminal sizeVessel functionMuscle cellsCell monolayersInjuryCultured cell monolayersPresent studyImportant determinantCellsA 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
1988
Matrix-driven cell size change modulates aortic endothelial cell proliferation and sheet migration.
Madri J, Pratt B, Yannariello-Brown J. Matrix-driven cell size change modulates aortic endothelial cell proliferation and sheet migration. American Journal Of Pathology 1988, 132: 18-27. PMID: 3394798, PMCID: PMC1880627.Peer-Reviewed Original ResearchConceptsSheet migrationBovine aortic endothelial cellsCellular functionsCell size changesEndothelial cell proliferationCell proliferationMatrix componentsExtracellular matrix component lamininExtracellular matrix componentsEndothelial cellsNuclear sizeExtracellular matrixAortic endothelial cellsModel systemSize changesCurrent hypothesesProliferationPhysiologic homeostasisCellsType IV collagenComplex fashionDistinct patternsCell attachmentMigrationRate of attachment
1987
Aortic endothelial cell proteoheparan sulfate. II. Modulation by extracellular matrix.
Keller R, Pratt B, Furthmayr H, Madri J. Aortic endothelial cell proteoheparan sulfate. II. Modulation by extracellular matrix. American Journal Of Pathology 1987, 128: 299-306. PMID: 2956886, PMCID: PMC1899612.Peer-Reviewed Original ResearchConceptsExtracellular matrixPlasma membraneHS IProteoheparan sulfate speciesSulfate biosynthesisEndothelial cellsHS IIIHS IICell polarityMajor cell typesExtracellular matrix componentsPolarized secretionBovine aortic endothelial cellsOrgan cultureTissue culture plasticSubcellular matrixBiosynthetic phenotypeMedium of cellsDifferentiated phenotypeCell typesMatrix moleculesVascular endothelial cellsAortic endothelial cellsProteoheparan sulfateSpeciesAortic endothelial cell proteoheparan sulfate. I. Isolation and characterization of plasmamembrane-associated and extracellular species.
Keller R, Silbert J, Furthmayr H, Madri J. Aortic endothelial cell proteoheparan sulfate. I. Isolation and characterization of plasmamembrane-associated and extracellular species. American Journal Of Pathology 1987, 128: 286-98. PMID: 3039849, PMCID: PMC1899622.Peer-Reviewed Original ResearchConceptsDaltons apparent molecular weightProteoheparan sulfate speciesHeparan sulfate chainsApparent molecular weightHS IBovine aortic endothelial cellsSulfate chainsCultured bovine aortic endothelial cellsCore proteinAortic endothelial cellsCell surface localizationPlasma membrane fractionEndothelial cellsPulse-chase experimentsCsCl density centrifugationThird speciesPlasma membraneSubcellular fractionationExtracellular speciesSpecialized functionsMatrix localizationSurface localizationMembrane fractionSulfate biosynthesisMedium species
1984
Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix.
Pratt B, Harris A, Morrow J, Madri J. Mechanisms of cytoskeletal regulation. Modulation of aortic endothelial cell spectrin by the extracellular matrix. American Journal Of Pathology 1984, 117: 349-54. PMID: 6507585, PMCID: PMC1900592.Peer-Reviewed Original ResearchConceptsAortic endothelial cellsEndothelial cellsCultured aortic endothelial cellsSurface receptorsCalf aortic endothelial cellsVascular responsesExtracellular matrixVariety of stimuliPeripheral localizationWound repairReceptorsTransducers of informationMembrane receptorsCellsFibrillar formSpectrin distributionIntracellular distributionNonerythroid spectrinNeoplasiaInjuryFibronectin substrate