2019
MicroRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis
Moro A, Driscoll TP, Boraas LC, Armero W, Kasper DM, Baeyens N, Jouy C, Mallikarjun V, Swift J, Ahn SJ, Lee D, Zhang J, Gu M, Gerstein M, Schwartz M, Nicoli S. MicroRNA-dependent regulation of biomechanical genes establishes tissue stiffness homeostasis. Nature Cell Biology 2019, 21: 348-358. PMID: 30742093, PMCID: PMC6528464, DOI: 10.1038/s41556-019-0272-y.Peer-Reviewed Original ResearchConceptsArgonaute 2MicroRNA-dependent regulationMechanical homeostasisMicroRNA recognition elementsExtracellular matrix proteinsZebrafish finsMicroRNA familiesTarget mRNAsVertebrate tissuesHyper-contractile phenotypesRegulatory pathwaysUntranslated regionRecognition elementMatrix proteinsComprehensive identificationCaM mRNAConnective tissue growth factorExtracellular matrix depositionHomeostasisTissue growth factorMRNAFibroblast cellsMicroRNAsGrowth factorSoft substrates
2014
Chemokine-coupled β2 integrin–induced macrophage Rac2–Myosin IIA interaction regulates VEGF-A mRNA stability and arteriogenesis
Morrison AR, Yarovinsky TO, Young BD, Moraes F, Ross TD, Ceneri N, Zhang J, Zhuang ZW, Sinusas AJ, Pardi R, Schwartz MA, Simons M, Bender JR. Chemokine-coupled β2 integrin–induced macrophage Rac2–Myosin IIA interaction regulates VEGF-A mRNA stability and arteriogenesis. Journal Of Experimental Medicine 2014, 211: 1957-1968. PMID: 25180062, PMCID: PMC4172219, DOI: 10.1084/jem.20132130.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArteriesCD18 AntigensDNA PrimersFlow CytometryHumansMiceMice, Inbred C57BLMonocytesNeovascularization, PhysiologicNonmuscle Myosin Type IIARac GTP-Binding ProteinsReal-Time Polymerase Chain ReactionReceptors, CCR2RNA StabilityVascular Endothelial Growth Factor AX-Ray MicrotomographyConceptsMyosin IIASignal transduction eventsHuR translocationRapid nuclearTransduction eventsProteomic analysisProtein HuR.Induction of arteriogenesisMRNA stabilityMRNA stabilizationNovel roleCytosolic translocationMyosin-9ICAM-1 adhesionReceptor engagementDevelopmental vasculogenesisCellular effectorsMolecular triggersTranslocationHeavy chainGrowth factorMyeloid cellsVascular endothelial growth factorKey molecular triggerCCL2 stimulation
2012
Endothelial Nuclear Factor-&kgr;B–Dependent Regulation of Arteriogenesis and Branching
Tirziu D, Jaba IM, Yu P, Larrivée B, Coon BG, Cristofaro B, Zhuang ZW, Lanahan AA, Schwartz MA, Eichmann A, Simons M. Endothelial Nuclear Factor-&kgr;B–Dependent Regulation of Arteriogenesis and Branching. Circulation 2012, 126: 2589-2600. PMID: 23091063, PMCID: PMC3514045, DOI: 10.1161/circulationaha.112.119321.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBecaplerminBrainDisease Models, AnimalEndothelial CellsHindlimbHuman Umbilical Vein Endothelial CellsHumansHypoxia-Inducible Factor 1, alpha SubunitIschemiaMiceMice, TransgenicNeovascularization, PathologicNeovascularization, PhysiologicNF-kappa B p50 SubunitProto-Oncogene Proteins c-sisRetinaVascular Endothelial Growth Factor AConceptsNuclear factor-κB activationCollateral formationReduced adhesion molecule expressionHypoxia-inducible factor-1α levelsDistal tissue perfusionVascular endothelial growth factorAdhesion molecule expressionPlatelet-derived growth factor-BBEndothelial growth factorGrowth factor-BBMolecule expressionMonocyte influxCollateral networkTissue perfusionImmature vesselsArterial networkBaseline levelsNFκB activationNuclear factorFactor-BBGrowth factor
2005
Integrin-dependent actomyosin contraction regulates epithelial cell scattering
de Rooij J, Kerstens A, Danuser G, Schwartz MA, Waterman-Storer CM. Integrin-dependent actomyosin contraction regulates epithelial cell scattering. Journal Of Cell Biology 2005, 171: 153-164. PMID: 16216928, PMCID: PMC2171213, DOI: 10.1083/jcb.200506152.Peer-Reviewed Original ResearchConceptsCell-cell junctionsEpithelial cell scatteringCell-cell adhesionCell scatteringHepatocyte growth factorE-cadherin functionMadin-Darby canine kidneyMyosin regulatory light chainExtracellular matrix proteinsTime-lapse imagingPossible cross talkCarcinoma cell invasionTraction forceRegulatory light chainIntegrin adhesionEpithelial-mesenchymal transitionActomyosin contractionMatrix proteinsCell invasionHigh traction forceMimic key aspectsCross talkSubstrate complianceGrowth factorCanine kidney
2004
p21-activated Kinase Regulates Endothelial Permeability through Modulation of Contractility*
Stockton RA, Schaefer E, Schwartz MA. p21-activated Kinase Regulates Endothelial Permeability through Modulation of Contractility*. Journal Of Biological Chemistry 2004, 279: 46621-46630. PMID: 15333633, DOI: 10.1074/jbc.m408877200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBlotting, WesternCattleCell CommunicationCells, CulturedCytokinesCytoskeletonEndothelium, VascularEnzyme ActivationHumansInflammationIschemiaMicroscopy, FluorescenceMuscle ContractionMyosin Light ChainsP21-Activated KinasesPeptidesPhosphorylationProtein Serine-Threonine KinasesProtein TransportThrombinTime FactorsTransfectionUmbilical VeinsConceptsP21-activated kinaseClose cell-cell associationsEndothelial cell-cell junctionsCell-cell junctionsActin stress fibersCell-cell associationsSuitable drug targetsGrowth factorMyosin phosphorylationHuman umbilical vein endothelial cellsCentral regulatorStress fibersUmbilical vein endothelial cellsEndothelial cellsPAK activationDrug targetsVein endothelial cellsCell contractilityMultiple growth factorsParacellular poresEndothelial permeabilityPhosphorylationPathological processesPathological conditionsPotential role
2001
Integrins and cell proliferationregulation of cyclin-dependent kinases via cytoplasmic signaling pathways
Schwartz M, Assoian R. Integrins and cell proliferationregulation of cyclin-dependent kinases via cytoplasmic signaling pathways. Journal Of Cell Science 2001, 114: 2553-2560. PMID: 11683383, DOI: 10.1242/jcs.114.14.2553.Peer-Reviewed Original ResearchConceptsCyclin-dependent kinasesG1 phase cyclin-dependent kinasesPhase cyclin-dependent kinasesCell cycle progressionCycle progressionCytoplasmic signaling pathwaysIntegrin-dependent signalsMammalian cellsGrowth factor receptorSignaling pathwaysERK pathwayCell adhesionExtracellular matrixDiverse arrayFactor receptorCyclin D1KinaseRegulationPathwayGrowth factorIntegrinsRecent advancesIntegrated controlReceptorsAdhesionCoordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression
Assoian R, Schwartz M. Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Current Opinion In Genetics & Development 2001, 11: 48-53. PMID: 11163150, DOI: 10.1016/s0959-437x(00)00155-6.Peer-Reviewed Original ResearchConceptsCell cycle progressionReceptor tyrosine kinasesG1 phase cyclinsDependent kinasesTyrosine kinasePhase cell cycle progressionG1 phase cell cycle progressionExtracellular matrix proteinsSoluble growth factorsRho GTPasesGrowth factor receptorRegulated signalingMatrix proteinsKinaseG1 phaseCell proliferationIntegrinsCyclinGrowth factorRecent studiesGTPasesActivationReceptorsSignalingERK
2000
Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*
Baron V, Schwartz M. Cell Adhesion Regulates Ubiquitin-mediated Degradation of the Platelet-derived Growth Factor Receptor β*. Journal Of Biological Chemistry 2000, 275: 39318-39323. PMID: 11007771, DOI: 10.1074/jbc.m003618200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBlotting, WesternCell AdhesionCell DivisionCell LineCells, CulturedCysteine EndopeptidasesDose-Response Relationship, DrugDown-RegulationDynaminsEmbryo, MammalianEnzyme InhibitorsFibroblastsFibronectinsGTP PhosphohydrolasesHumansLigandsLysosomesMiceMultienzyme ComplexesPhosphorylationProteasome Endopeptidase ComplexProtein-Tyrosine KinasesReceptors, Platelet-Derived Growth FactorTemperatureTime FactorsTrypsinTyrphostinsUbiquitinsConceptsUbiquitin-dependent pathwayIntegrin-mediated adhesionPlatelet-derived growth factor receptor βPlatelet-derived growth factor receptor betaTyrosine kinase activityGrowth factor receptor βGrowth factor receptor betaProteasome pathwayDetachment of cellsReceptor autophosphorylationKinase activityCellular desensitizationPrimary fibroblastsExtracellular matrixCell detachmentAutophosphorylationProtein levelsCell linesPDGFGrowth factorReceptor betaReceptor βCellsPathwayRecent studiesAdhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
del Pozo M, Price L, Alderson N, Ren X, Schwartz M. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. The EMBO Journal 2000, 19: 2008-2014. PMID: 10790367, PMCID: PMC305684, DOI: 10.1093/emboj/19.9.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCdc42 GTP-Binding ProteinCell AdhesionCell LineCell MembraneCulture Media, Serum-FreeCytoplasmEnzyme ActivationExtracellular MatrixFibronectinsGrowth SubstancesGuanosine TriphosphateIntegrinsMiceMutationMyristic AcidP21-Activated KinasesProtein BindingProtein Serine-Threonine KinasesRac GTP-Binding ProteinsRatsRecombinant Fusion ProteinsTransfectionConceptsSmall GTPase RacExtracellular matrixGTPase RacEffector PAKMembrane-targeting sequenceCell cycle progressionAbility of RacSoluble growth factorsAdherent cellsRac mutantGrowth factorCytoskeletal organizationPAK activationOncogenic transformationGene expressionCycle progressionMembrane fractionCell adhesionNon-adherent cellsRacPAKMembraneCellsAdhesionActivation
1997
Growth factor activation of MAP kinase requires cell adhesion
Renshaw M, Ren X, Schwartz M. Growth factor activation of MAP kinase requires cell adhesion. The EMBO Journal 1997, 16: 5592-5599. PMID: 9312018, PMCID: PMC1170191, DOI: 10.1093/emboj/16.18.5592.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell AdhesionCell Transformation, NeoplasticEnzyme ActivationExtracellular Matrix ProteinsGenes, rasKineticsMAP Kinase Kinase Kinase 1MiceMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorProtein Serine-Threonine KinasesProto-Oncogene Proteins c-rafProto-OncogenesConceptsCell adhesionGrowth factor-regulated pathwaysMAP kinase ERK2Mutants of RasActivation of ERK2MAP kinase pathwayRas-transformed cellsGrowth factor activationExtracellular matrix proteinsSoluble growth factorsAnchorage-independent growthKinase ERK2Growth factorMAP kinaseOncogenic growthEndogenous RasKinase pathwayOncogenic activationMEK activityMatrix proteinsMajor regulatorERK2Factor activationRafMEK
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 cells
1993
The extracellular matrix as a cell survival factor.
Meredith J, Fazeli B, Schwartz M. The extracellular matrix as a cell survival factor. Molecular Biology Of The Cell 1993, 4: 953-961. PMID: 8257797, PMCID: PMC275725, DOI: 10.1091/mbc.4.9.953.Peer-Reviewed Original ResearchConceptsCell survival factorExtracellular matrixCell typesSurvival factorCell deathTyrosine phosphatase inhibitor sodium orthovanadateCell suicide pathwayRapid cell deathSuicide pathwayECM interactionsDNA degradationHuman endothelial cellsSodium orthovanadateCell growthPCDNucleus fragmentationTRPM-2Cell morphologyVascular cell adhesion molecule-1Class I histocompatibility antigenCell viabilityGrowth factorSpecific hormonesEndothelial cellsPotential roleIntegrin 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 contactCalciumMAbs
1992
Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor.
Schwartz M, Lechene C. Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6138-6141. PMID: 1378621, PMCID: PMC402137, DOI: 10.1073/pnas.89.13.6138.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAnimalsCarrier ProteinsCell AdhesionCells, CulturedExtracellular MatrixHydrogen-Ion ConcentrationIn Vitro TechniquesMiceNaphthalenesPlatelet-Derived Growth FactorPolycyclic CompoundsProtein Kinase CSignal TransductionSodium-Hydrogen ExchangersTetradecanoylphorbol AcetateConceptsProtein kinase CPlatelet-derived growth factorKinase CAdherent cellsGrowth factorExtracellular matrix proteinsPKC-dependent pathwayElevation of intracellularMatrix proteinsAnchorage-dependent cellsCell adhesionDependent activationPKC activationAntiporterPhorbol esterSolid substratumPharmacological inhibitionC3H 10T1/2 cellsCellsActivationPathwayIntracellular pHAdhesionProteinIntegrins
1991
Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape.
Schwartz M, Lechene C, Ingber D. Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 7849-7853. PMID: 1652767, PMCID: PMC52401, DOI: 10.1073/pnas.88.17.7849.Peer-Reviewed Original ResearchConceptsIntegrin alpha 5 beta 1Alpha 5 beta 1Cell shapeInsoluble extracellular matrix moleculesNa/H antiporterExtracellular matrix receptorsInsoluble fibronectinSurface-adsorbed fibronectinSoluble growth factorsExtracellular matrix moleculesH antiporterCell surface receptorsTransmembrane receptorsGrowth factor receptorBeta 1Matrix receptorsGrowth controlAnchorage-dependent cellsMatrix moleculesAntiporterFactor receptorSuppress growthSoluble mitogensGrowth factorFibronectin
1990
Cytoplasmic pH and anchorage-independent growth induced by v-Ki-ras, v-src or polyoma middle T.
Schwartz M, Rupp E, Frangioni J, Lechene C. Cytoplasmic pH and anchorage-independent growth induced by v-Ki-ras, v-src or polyoma middle T. Oncogene 1990, 5: 55-8. PMID: 2181378.Peer-Reviewed Original ResearchConceptsAnchorage-independent growthNormal cellsCytoplasmic pHPolyoma middle T oncogeneRas-transformed cellsCell linesExtracellular matrix proteinsMiddle T oncogeneV-SrcSrc oncogeneTissue culture plasticMatrix proteinsCellular requirementsCell growthControl growthOncogeneV-KiAlkaline pHiSeries of cellsCulture plasticGrowth factorCellsGrowthRAMutants