1994
Modulation of platelet-derived growth factor receptor expression in microvascular endothelial cells during in vitro angiogenesis.
Marx M, Perlmutter R, Madri J. Modulation of platelet-derived growth factor receptor expression in microvascular endothelial cells during in vitro angiogenesis. Journal Of Clinical Investigation 1994, 93: 131-139. PMID: 7506710, PMCID: PMC293745, DOI: 10.1172/jci116936.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsCell DivisionCells, CulturedElectrophoresis, Polyacrylamide GelEndothelium, VascularEpididymisImmunoblottingKineticsMaleMicrocirculationMolecular WeightNeovascularization, PathologicPlatelet-Derived Growth FactorRatsReceptors, Platelet-Derived Growth FactorRecombinant ProteinsTime FactorsConceptsMicrovascular endothelial cellsEndothelial cellsPDGF receptorReceptor expressionPlatelet-derived growth factor receptor expressionGrowth factor receptor expressionPDGF receptor expressionFactor receptor expressionPDGF receptor alphaReceptor surface expressionEndothelial cell growthNovel therapeutic applicationsCell growthSuramin treatmentProliferative responseEndothelial cell phenotypeReceptor alphaPDGF isoformsPDGF-AAInhibited proliferationReceptor regulationPDGF-BBPDGF-ABAngiogenesisCell proliferation
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 regionsAortic 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
1986
Mechanisms of cytoskeletal regulation: Modulation of aortic endothelial cell protein band 4.1 by the extracellular matrix
Leto T, Pratt B, Madri J. Mechanisms of cytoskeletal regulation: Modulation of aortic endothelial cell protein band 4.1 by the extracellular matrix. Journal Of Cellular Physiology 1986, 127: 423-431. PMID: 3519624, DOI: 10.1002/jcp.1041270311.Peer-Reviewed Original ResearchConceptsActin filamentsExtracellular matrixProtein 4.1Band 4.1Contact inhibitionCytoplasmic actin filamentsTransduction of informationCell-cell contactCortical membrane proteinsErythroid proteinCytoskeletal regulationSpecific cleavage productsMembrane proteinsSkeletal proteinsCysteine residuesCell cytoskeletonEndothelial cellsFilamentous distributionECM proteinsEndothelial cell cytoskeletonFibronectin substrateReorganization eventsCell nucleiComplex pathwaysImmunoblot analysis
1985
Characterization of the tissue form of type V collagen from chick bone.
Broek D, Madri J, Eikenberry E, Brodsky B. Characterization of the tissue form of type V collagen from chick bone. Journal Of Biological Chemistry 1985, 260: 555-562. PMID: 3965462, DOI: 10.1016/s0021-9258(18)89768-x.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisGlobular domainType V collagenCyanogen bromide peptide mapsTriple-helical domainGel electrophoresisIsolated alpha chainHelical domainTriple helixForm of alphaBanding patternsChick bonePeptide mapsProtein bandsBacterial collagenase digestionTerminal peptidesRotary shadowingHigh molecular weight formAlpha chainTissue formMolecular weight formsSlower mobilityHelix
1983
Ultrastructural morphology and domain structure of a unique collagenous component of basement membranes.
Madri J, Foellmer H, Furthmayr H. Ultrastructural morphology and domain structure of a unique collagenous component of basement membranes. Biochemistry 1983, 22: 2797-804. PMID: 6409144, DOI: 10.1021/bi00281a005.Peer-Reviewed Original Research
1982
Differential proteolytic susceptibility of laminin alpha and beta subunits
Rao C, Margulies I, Goldfarb R, Madri J, Woodley D, Liotta L. Differential proteolytic susceptibility of laminin alpha and beta subunits. Archives Of Biochemistry And Biophysics 1982, 219: 65-70. PMID: 6758704, DOI: 10.1016/0003-9861(82)90134-5.Peer-Reviewed Original Research
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 Research