2017
NOD Mice Having a Lyn Tyrosine Kinase Mutation Exhibit Abnormal Neutrophil Chemotaxis
Wu Y, Hannigan M, Zhan L, Madri JA, Huang C. NOD Mice Having a Lyn Tyrosine Kinase Mutation Exhibit Abnormal Neutrophil Chemotaxis. Journal Of Cellular Physiology 2017, 232: 1689-1695. PMID: 27591397, DOI: 10.1002/jcp.25583.Peer-Reviewed Original Research
2008
Targeted imaging of hypoxia-induced integrin activation in myocardium early after infarction
Kalinowski L, Dobrucki LW, Meoli DF, Dione DP, Sadeghi MM, Madri JA, Sinusas AJ. Targeted imaging of hypoxia-induced integrin activation in myocardium early after infarction. Journal Of Applied Physiology 2008, 104: 1504-1512. PMID: 18356482, DOI: 10.1152/japplphysiol.00861.2007.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBiomarkersBiotransformationDogsHeterocyclic Compounds, 1-RingHypoxiaImidazolesImmunohistochemistryIntegrin alphaVbeta3IntegrinsMaleMyocardial InfarctionMyocardial IschemiaMyocardiumNeovascularization, PhysiologicOrganometallic CompoundsOrganotechnetium CompoundsRadiopharmaceuticalsRatsRats, Sprague-DawleyTechnetium Tc 99m SestamibiTomography, Emission-Computed, Single-PhotonConceptsMyocardial infarctionInfarct regionCanine studyIschemic heart diseaseCoronary artery occlusionAcute myocardial infarctionMarkers of angiogenesisEx vivo analysisExpression/activationPotential novel targetHypoxia-induced angiogenesisVivo SPECT imagingAlphavbeta3 integrinBRU59-21Artery occlusionNovel noninvasive approachHeart diseaseHistological evidenceMyocardial hypoxiaMyocardial uptakeRP748Rodent studiesAngiogenic therapyInfarctionMyocardial angiogenesis
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
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
1989
Modulation of actin mRNAs in cultured vascular cells by matrix components and TGF-β1
Kocher O, Madri J. Modulation of actin mRNAs in cultured vascular cells by matrix components and TGF-β1. In Vitro Cellular & Developmental Biology 1989, 25: 424-434. PMID: 2659578, DOI: 10.1007/bf02624627.Peer-Reviewed Original ResearchConceptsTwo-dimensional cultureActin mRNAEndothelial cell populationSmooth muscle cellsIndividual extracellular matrix proteinsSmooth muscle cell differentiationCell typesRat capillary endothelial cellsMuscle cell differentiationActin mRNA expressionThree-dimensional type ISkeletal muscle cellsMatrix componentsExtracellular matrix proteinsCell populationsCytoplasmic actin mRNAsMuscle actin mRNAEndothelial cellsMuscle cellsSmooth muscle cell markersExtracellular matrix componentsCultured vascular cellsΑ-SM actinBovine aortic endothelial cellsMuscle cell markers
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