1996
Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin‐dependent pathway.
Schwartz M, Toksoz D, Khosravi‐Far R. Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin‐dependent pathway. The EMBO Journal 1996, 15: 6525-6530. PMID: 8978679, PMCID: PMC452477, DOI: 10.1002/j.1460-2075.1996.tb01043.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsA Kinase Anchor ProteinsAdaptor Proteins, Signal TransducingAnimalsCalciumCell DivisionCell Transformation, NeoplasticGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsIntegrinsKineticsMiceMinor Histocompatibility AntigensModels, BiologicalOncogenesPhosphatidylinositol 4,5-DiphosphateProto-Oncogene ProteinsRetroviridae Proteins, OncogenicRho GTP-Binding ProteinsSignal TransductionThrombinConceptsConstitutive activationCell growthIntegrin signal transductionSmall GTPase RhoIntegrin-dependent pathwaySignal transductionSignaling eventsGrowth factor receptorGTPase RhoSerum-dependent growthAnchorage independenceFactor receptorPathwayOncogeneUncontrolled growthRhoActivationImportant mediatorTumor cellsGrowthTransductionTransmit signalDblGrowth resultsAnchorage
1994
The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
Chong L, Traynor-Kaplan A, Bokoch G, Schwartz M. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994, 79: 507-513. PMID: 7954816, DOI: 10.1016/0092-8674(94)90259-3.Peer-Reviewed Original ResearchMeSH KeywordsADP Ribose TransferasesAnimalsBotulinum ToxinsCalciumCell AdhesionCells, CulturedDrosophila ProteinsFibroblastsGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)IntegrinsLovastatinMembrane ProteinsMiceMicroinjectionsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Platelet-Derived Growth FactorRecombinant ProteinsSignal TransductionThrombinConceptsPlatelet-derived growth factorBotulinum C3 exoenzymeSmall GTPPIP2 synthesisC3 exoenzymePIP2 hydrolysisProduction of phosphatidylinositolIntegrin-mediated adhesionEffects of RhoTreatment of cellsCalcium mobilizationActin cytoskeletonDiminished calcium mobilizationMammalian cellsProtein RhoPIP2 levelsCell lysatesGTP gamma SGTPRhoPhosphatidylinositolExoenzymeGamma SGrowth factorNonadherent cellsAlpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion
Schwartz M, Denninghoff K. Alpha v integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion. Journal Of Biological Chemistry 1994, 269: 11133-11137. PMID: 7512559, DOI: 10.1016/s0021-9258(19)78101-0.Peer-Reviewed Original ResearchConceptsAlpha 5 beta 1Alpha vBeta 1Intracellular calciumEndothelial cellsAnti-integrin monoclonal antibodiesElevation of intracellularAlpha v integrinsAnti-integrin antibodiesMonoclonal antibodiesV integrinsAntibodiesDistinct intracellularAgonistsIntegrin alpha subunitsAdhesion assaysFunction-blocking anti-integrin antibodiesIntegrinsSpecific integrinsCalciumFibronectinAlpha subunitCellsSame cellsIntracellular
1993
A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells.
Schwartz M, Brown E, Fazeli B. A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. Journal Of Biological Chemistry 1993, 268: 19931-19934. PMID: 8376355, DOI: 10.1016/s0021-9258(20)80675-9.Peer-Reviewed Original ResearchConceptsIntegrin-associated proteinExtracellular matrix proteinsMatrix proteinsEndothelial cellsIAP functionTransmembrane domainTyrosine phosphorylationPrimary sequenceEndothelial cell adhesionCell adhesionMembrane channelsProteinAnti-integrin antibodiesCalcium entryCellsIntracellular pHIon transportInflux of Ca2Activation of neutrophilsActivationCalcium channelsCalcium influxPhosphorylationNeutrophil functionMonoclonal antibodiesIntegrin beta 1- and beta 3-mediated endothelial cell migration is triggered through distinct signaling mechanisms.
Leavesley D, Schwartz M, Rosenfeld M, Cheresh D. Integrin beta 1- and beta 3-mediated endothelial cell migration is triggered through distinct signaling mechanisms. Journal Of Cell Biology 1993, 121: 163-170. PMID: 7681432, PMCID: PMC2119781, DOI: 10.1083/jcb.121.1.163.Peer-Reviewed Original ResearchConceptsExtracellular calciumBeta 3Extracellular calcium sourcesAlpha v beta 3Alpha 2 beta 1Absence of cytokinesNa/H antiporterBeta 1 mAbIntracellular calciumCalcium influxIntegrin alpha 2 beta 1Specific influxBeta 1Distinct signaling mechanismsEndothelial cell migrationGrowth factorMeasurable riseDistinct intracellularRespective integrinsH antiporterCellular migrationCell migrationCell contactCalciumMAbsSpreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium.
Schwartz M. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. Journal Of Cell Biology 1993, 120: 1003-1010. PMID: 7679387, PMCID: PMC2200079, DOI: 10.1083/jcb.120.4.1003.Peer-Reviewed Original ResearchConceptsCalcium channelsBasal levelsVoltage-independent calcium channelsEndothelial cellsVoltage-dependent calcium channelsIntracellular free calciumElevation of pHiNa-Ca exchangerHuman endothelial cellsBeta 1 integrinIntracellular calciumFura-2Extracellular calciumFree calciumSubunit antibodiesSame antibodyIntracellular pHSteady-state levelsAntibodiesElevationCalciumCellsHigh steady-state levelsInvolvementIntegrins