2016
Targeted proteomics effectively quantifies differences between native lung and detergent-decellularized lung extracellular matrices
Calle EA, Hill RC, Leiby KL, Le AV, Gard AL, Madri JA, Hansen KC, Niklason LE. Targeted proteomics effectively quantifies differences between native lung and detergent-decellularized lung extracellular matrices. Acta Biomaterialia 2016, 46: 91-100. PMID: 27693690, PMCID: PMC5451113, DOI: 10.1016/j.actbio.2016.09.043.Peer-Reviewed Original ResearchConceptsExtracellular matrixLung extracellular matrixMatrix proteinsECM-associated proteinsCell-matrix interactionsProtein extraction methodsWhole organ regenerationRegenerative medicineOrganotypic cell culturesQuantitative proteomicsAcellular extracellular matrixECM proteinsOrgan regenerationCell adhesionProteomicsProtein analysisQuantitative biochemical dataProteinPotent substrateXenogeneic extracellular matrixTargeted proteomicsCell nuclear antigenBiochemical dataImportant glycoproteinCell cultures
2014
Temporal Regulation of venous Extracellular Matrix Components during Arteriovenous Fistula Maturation
Hall MR, Yamamoto K, Protack CD, Tsuneki M, Kuwahara G, Assi R, Brownson KE, Bai H, Madri JA, Dardik A. Temporal Regulation of venous Extracellular Matrix Components during Arteriovenous Fistula Maturation. The Journal Of Vascular Access 2014, 16: 93-106. PMID: 25262757, PMCID: PMC4405006, DOI: 10.5301/jva.5000290.Peer-Reviewed Original ResearchConceptsExtracellular matrix componentsTemporal regulationECM componentsStructural proteinsMatrix componentsGene microarray analysisMatrix metalloproteinasesRegulatory proteinsMicroarray analysisNon-collagenous proteinsDistinct temporal patternsECM degradationTemporal patternsProteinProtein expressionElastin expressionExpressionMaturationOsteopontin expressionProtease inhibitorsHuman AVF maturationRegulationTissue inhibitorDays of maturationMetalloproteinase-1
2009
Proteomic-Based Detection of a Protein Cluster Dysregulated during Cardiovascular Development Identifies Biomarkers of Congenital Heart Defects
Nath AK, Krauthammer M, Li P, Davidov E, Butler LC, Copel J, Katajamaa M, Oresic M, Buhimschi I, Buhimschi C, Snyder M, Madri JA. Proteomic-Based Detection of a Protein Cluster Dysregulated during Cardiovascular Development Identifies Biomarkers of Congenital Heart Defects. PLOS ONE 2009, 4: e4221. PMID: 19156209, PMCID: PMC2626248, DOI: 10.1371/journal.pone.0004221.Peer-Reviewed Original ResearchConceptsCardiovascular developmentMass spectrometry-based proteomicsSpectrometry-based proteomicsNormal cardiovascular developmentAdhesion/migrationHuman CHDsProteomic datasetsHeart developmentProtein clustersMurine embryosProtein pathwayMolecular pathwaysFunctional roleProteinEmbryonic survivalYolk sacProtein levelsIdentifies biomarkersCardiovascular defectsWestern blottingPathwayNovel avenuesEmbryosComplete understandingProtein biomarkers
2005
Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis
Wu Y, Stabach P, Michaud M, Madri JA. Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis. The Journal Of Immunology 2005, 175: 3484-3491. PMID: 16148090, DOI: 10.4049/jimmunol.175.6.3484.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell ShapeChemokine CXCL1ChemokinesChemokines, CXCChemotaxis, LeukocyteCytokinesInterleukin-8Intracellular Signaling Peptides and ProteinsMiceMice, KnockoutNeutrophilsPlatelet Endothelial Cell Adhesion Molecule-1Protein Phosphatase 1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, Interleukin-8BConceptsCell motilitySrc homology 2 domainF-actinSHP-1 phosphatase activityWild-type neutrophilsF-actin polymerizationPhosphatase 1Time-lapse videomicroscopyPECAM-1Cytokine-induced mobilizationPhosphatase activityExhibit lossMurine neutrophilsMotilityChemotaxisZigmond chamberCellsPECAMLeading frontCytoskeletonMoesinIL-8FMLP gradientProteinActin
2003
PECAM-1 promotes β-catenin accumulation and stimulates endothelial cell proliferation
Biswas P, Canosa S, Schoenfeld J, Schoenfeld D, Tucker A, Madri JA. PECAM-1 promotes β-catenin accumulation and stimulates endothelial cell proliferation. Biochemical And Biophysical Research Communications 2003, 303: 212-218. PMID: 12646189, DOI: 10.1016/s0006-291x(03)00313-9.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBeta CateninBlotting, WesternCell AdhesionCell DivisionCytoplasmCytoskeletal ProteinsEndotheliumFlow CytometryHumansLungMiceMice, KnockoutMicroscopy, FluorescencePlatelet Endothelial Cell Adhesion Molecule-1Precipitin TestsSignal TransductionTrans-ActivatorsTranscription, GeneticTransfectionConceptsPECAM-1-positive endothelial cellsBeta-catenin proteinCell proliferationEndothelial cellsPECAM-1Beta-catenin localizationCytoplasmic domainΒ-catenin accumulationFull-length PECAM-1Functional consequencesEndothelial cell proliferationCell membraneKnockout animalsAdhesion moleculesLess accumulationCellsAccumulationProliferative rateProliferationMembraneProteinBinds
2000
Matrix metalloproteinase activity is required for activity-induced angiogenesis in rat skeletal muscle
Haas T, Milkiewicz M, Davis S, Zhou A, Egginton S, Brown M, Madri J, Hudlicka O. Matrix metalloproteinase activity is required for activity-induced angiogenesis in rat skeletal muscle. AJP Heart And Circulatory Physiology 2000, 279: h1540-h1547. PMID: 11009439, DOI: 10.1152/ajpheart.2000.279.4.h1540.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCapillariesCell DivisionDipeptidesElectric StimulationImmunohistochemistryMatrix Metalloproteinase 2Matrix Metalloproteinase InhibitorsMatrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesMicroscopy, ElectronMotor ActivityMuscle, SkeletalNeovascularization, PhysiologicProtease InhibitorsRatsRNA, MessengerConceptsMembrane proteinsBasement membrane proteinsEndothelial cell sprout formationRat skeletal muscleSkeletal muscleMatrix metalloproteinasesMembrane type 1Inflammation-mediated angiogenesisPhysiological angiogenesisBasement membraneCell proliferationMMP proteolysisProtein levelsProteolysisSprout formationMajor classesCritical roleProteinMatrix metalloproteinase activityMetalloproteinase activityProliferationAngiogenesisNew capillariesMembraneMMP inhibition
1999
Egr-1 Mediates Extracellular Matrix-driven Transcription of Membrane Type 1 Matrix Metalloproteinase in Endothelium*
Haas T, Stitelman D, Davis S, Apte S, Madri J. Egr-1 Mediates Extracellular Matrix-driven Transcription of Membrane Type 1 Matrix Metalloproteinase in Endothelium*. Journal Of Biological Chemistry 1999, 274: 22679-22685. PMID: 10428849, DOI: 10.1074/jbc.274.32.22679.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCloning, MolecularDNA-Binding ProteinsEarly Growth Response Protein 1Endothelium, VascularExtracellular MatrixGene Expression Regulation, EnzymologicHalf-LifeImmediate-Early ProteinsMatrix Metalloproteinase 14Matrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesMiceMolecular Sequence DataNeovascularization, PhysiologicProtein BindingRatsRNA, MessengerSp1 Transcription FactorTranscription FactorsTranscription, GeneticUp-RegulationConceptsMembrane type 1 matrix metalloproteinaseEgr-1MT1-MMPTranscription factor Egr-1Number of proteinsExtracellular matrix environmentEnhanced transcriptional activityEndothelial cellsTranscriptional activityPromoter correlatesIncreased transcriptionCellular invasionInvasive phenotypeMatrix metalloproteinaseTranscriptionMatrix environmentMatrix metalloproteinase activityMetalloproteinase activityCellsMatrix metalloproteinasesInvasionIncrease productionAngiogenesisMetalloproteinaseProtein
1998
Immunofluorescence Characterization of Key Extracellular Matrix Proteins in Murine Bone Marrow In Situ
Nilsson S, Debatis M, Dooner M, Madri J, Quesenberry P, Becker P. Immunofluorescence Characterization of Key Extracellular Matrix Proteins in Murine Bone Marrow In Situ. Journal Of Histochemistry & Cytochemistry 1998, 46: 371-377. PMID: 9487119, DOI: 10.1177/002215549804600311.Peer-Reviewed Original ResearchConceptsExtracellular matrix proteinsMatrix proteinsKey extracellular matrix proteinsParticular extracellular matrix proteinsExtracellular matrix protein fibronectinStem cellsCentral marrow regionsMatrix protein fibronectinStem cell proliferationCollagen type IMurine bone marrowHemopoietic stem cellsProtein fibronectinBone marrow vesselsExtracellular matrixBone marrowMechanistic roleCell proliferationProteinMarrow microenvironmentImportant mechanistic roleMolecular interactionsImmunofluorescence labelingCollagen type IVType IThree-dimensional Type I Collagen Lattices Induce Coordinate Expression of Matrix Metalloproteinases MT1-MMP and MMP-2 in Microvascular Endothelial Cells*
Haas T, Davis S, Madri J. Three-dimensional Type I Collagen Lattices Induce Coordinate Expression of Matrix Metalloproteinases MT1-MMP and MMP-2 in Microvascular Endothelial Cells*. Journal Of Biological Chemistry 1998, 273: 3604-3610. PMID: 9452488, DOI: 10.1074/jbc.273.6.3604.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCollagenDrug CombinationsEndothelium, VascularEnzyme ActivationEnzyme InhibitorsGelatinasesLamininMatrix Metalloproteinase 2Matrix Metalloproteinases, Membrane-AssociatedMetalloendopeptidasesNeovascularization, PhysiologicProtein ConformationProteoglycansRatsRats, Sprague-DawleyRNA, MessengerSignal TransductionTissue Inhibitor of Metalloproteinase-2ConceptsMT1-MMPTwo-dimensional cultureEndothelial cellsThree-dimensional collagen matrixEndothelial cell organizationEndothelial cell angiogenesisEndothelial cell migrationCell organizationCoordinate expressionPutative activatorMT1-MMP activationMMP-2Matrix metalloproteinasesCell migrationFunctional roleMatrix interactionsMatrix remodelingCollagen matrixCell angiogenesisEndothelial cell networksMMP-2 proteinProtein
1996
Restitution at the cellular level: regulation of the migrating phenotype.
Basson M, Rashid Z, Turowski G, West A, Emenaker N, Sgambati S, Hong F, Perdikis D, Datta S, Madri J. Restitution at the cellular level: regulation of the migrating phenotype. The Yale Journal Of Biology And Medicine 1996, 69: 119-29. PMID: 9112743, PMCID: PMC2588988.Peer-Reviewed Original ResearchMeSH KeywordsActinsAlkaline PhosphataseAnimalsCell DifferentiationCell MovementCells, CulturedCollagenDipeptidyl-Peptidases and Tripeptidyl-PeptidasesEnterostomyEpidermal Growth FactorEpithelial CellsEpitheliumHumansHydrogen-Ion ConcentrationIntestinal MucosaIntestinesJejunumLamininMembrane ProteinsMicrovilliPentagastrinPeptide YYPeptidesPhosphoproteinsRatsRats, Sprague-DawleyZonula Occludens-1 ProteinConceptsIntestinal epithelial cellsCell matrix proteinsIntestinal epithelial differentiationIntestinal epithelial brush borderCaco-2 intestinal epithelial cellsCaco-2 migrationEpithelial cellsEpithelial brush borderRegulatory biologyHuman Caco-2 intestinal epithelial cellsSheet migrationCell biologyCell motilityMigratory stateMatrix proteinsDipeptidyl dipeptidaseCellular levelBrush borderCaco-2 cellsEpithelial differentiationCell linesBiologyProteinDifferentiationSpecific activity
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
1994
Glutamine modulates phenotype and stimulates proliferation in human colon cancer cell lines.
Turowski G, Rashid Z, Hong F, Madri J, Basson M. Glutamine modulates phenotype and stimulates proliferation in human colon cancer cell lines. Cancer Research 1994, 54: 5974-80. PMID: 7954430.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBeta-GalactosidaseCathepsin CCell AdhesionCell DifferentiationCell DivisionColonic NeoplasmsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDose-Response Relationship, DrugExtracellular Matrix ProteinsGlutamineHumansIntegrinsLactaseOligo-1,6-GlucosidasePhenotypeTumor Cells, CulturedConceptsMatrix proteinsHuman colon carcinoma cell lineColon carcinoma cell lineCell linesCarcinoma cell linesSurface expressionDigestive enzyme expressionGlutamine-free mediumCell-matrix interactionsColon cancer cell linesHuman colon cancer cell linesCaco-2 proliferationSerial cell countsIntegrin surface expressionSW620 cellsCancer cell linesDigestive enzymesProteinEnzyme expressionGlutamineSynthetic substratesAdherent cellsCathepsin CExpressionIntegrin expression
1988
Extracellular matrix specificity for the differentiation of capillary endothelial cells
Carley W, Milici A, Madri J. Extracellular matrix specificity for the differentiation of capillary endothelial cells. Experimental Cell Research 1988, 178: 426-434. PMID: 3049122, DOI: 10.1016/0014-4827(88)90411-9.Peer-Reviewed Original ResearchConceptsExtracellular matrixCapillary endothelial cellsEndothelial cellsSpecific extracellular matrixEndothelial cell migrationVivo phenotypeDifferentiated phenotypeCell migrationCell typesCell growthCell dedifferentiationEndothelial cell growthMatrix componentsMembrane structurePhenotypeCellsExpressionCulture methodCytoplasmProteinGrowthMadinDifferentiationDedifferentiationGreater number
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