2001
pp60c-src Modulates Microvascular Endothelial Phenotype and in Vitro Angiogenesis
Marx M, Warren S, Madri J. pp60c-src Modulates Microvascular Endothelial Phenotype and in Vitro Angiogenesis. Experimental And Molecular Pathology 2001, 70: 201-213. PMID: 11417999, DOI: 10.1006/exmp.2001.2358.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsBecaplerminCell DivisionEndothelium, VascularGenes, srcGenetic VectorsMaleMicrocirculationMoloney murine leukemia virusNeovascularization, PhysiologicPlatelet-Derived Growth FactorProto-Oncogene Proteins c-sisProto-Oncogene Proteins pp60(c-src)RatsRecombinant ProteinsSignal TransductionTransfectionConceptsC-Src mutantC-SrcTwo-dimensional cultureThree-dimensional cultureWild-type c-SrcC-Src kinase activityC-Src tyrosine kinaseC-Src associatesC-src proteinPlatelet-derived growth factor receptorV-SrcPDGF signalCytoskeletal organizationGrowth factor receptorKinase activityCell shapeTyrosine kinaseVitro AngiogenesisTube-like structuresCell morphologyFactor receptorTube formationMutantsRegulatory effectsOverexpression
1997
Platelet Endothelial Cell Adhesion Molecule-1 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*
Lu T, Barreuther M, Davis S, Madri J. Platelet Endothelial Cell Adhesion Molecule-1 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*. Journal Of Biological Chemistry 1997, 272: 14442-14446. PMID: 9162084, DOI: 10.1074/jbc.272.22.14442.Peer-Reviewed Original ResearchConceptsSrc homology 2C-SrcGST-SrcCytoplasmic tailImmunoreceptor tyrosineCytoplasmic domain sequencesEndothelial cell adhesion molecule-1Src SH2 domainCell-cell bordersPECAM-1 functionsPECAM-1PECAM-1 phosphorylationUnidentified phosphoproteinsProtein associatesHomology 2Kinase assaysSignal transductionGlutathione S-transferaseSheet migrationConfluent endothelial cellsActivation motifConsensus sequenceDomain sequencesDomain interactionsEndothelial cells
1992
Autocrine angiotensin system regulation of bovine aortic endothelial cell migration and plasminogen activator involves modulation of proto-oncogene pp60c-src expression.
Bell L, Luthringer D, Madri J, Warren S. Autocrine angiotensin system regulation of bovine aortic endothelial cell migration and plasminogen activator involves modulation of proto-oncogene pp60c-src expression. Journal Of Clinical Investigation 1992, 89: 315-320. PMID: 1370299, PMCID: PMC442850, DOI: 10.1172/jci115578.Peer-Reviewed Original ResearchMeSH Keywords1-Sarcosine-8-Isoleucine Angiotensin IIAngiotensin IIAngiotensin Receptor AntagonistsAngiotensin-Converting Enzyme InhibitorsAnimalsAortaCattleCell MovementCells, CulturedEnalaprilEndothelium, VascularGene Expression Regulation, ViralLisinoprilPlasminogen ActivatorsProtein KinasesProto-Oncogene Proteins pp60(c-src)Receptors, AngiotensinRNA, MessengerConceptsEndothelial cell migrationC-Src expressionCell migrationC-SrcProto-oncogene c-srcC-Src kinase activityPp60c-src expressionCoding sequenceKinase activityU-PABovine aortic endothelial cell migrationAngiotensin-converting enzyme inhibitor lisinoprilRetroviral vectorsProtein 3Plasminogen activatorStable infectionExpressionDenudation injuryPlasminogen activator activityActivatorActivity 2Cell expressionAngiotensin system inhibitionActivator activityEndothelial cell expression