2015
KLF4 is a key determinant in the development and progression of cerebral cavernous malformations
Cuttano R, Rudini N, Bravi L, Corada M, Giampietro C, Papa E, Morini MF, Maddaluno L, Baeyens N, Adams RH, Jain MK, Owens GK, Schwartz M, Lampugnani MG, Dejana E. KLF4 is a key determinant in the development and progression of cerebral cavernous malformations. EMBO Molecular Medicine 2015, 8: 6-24. PMID: 26612856, PMCID: PMC4718159, DOI: 10.15252/emmm.201505433.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBone Morphogenetic Protein 6Cell ProliferationDisease Models, AnimalDisease ProgressionEndothelial CellsHEK293 CellsHemangioma, Cavernous, Central Nervous SystemHumansKRIT1 ProteinKruppel-Like Factor 4Kruppel-Like Transcription FactorsMiceMice, Inbred C57BLMice, KnockoutMicrotubule-Associated ProteinsMitogen-Activated Protein Kinase 7MutationProto-Oncogene ProteinsRNA InterferenceSignal TransductionSmad1 ProteinTransforming Growth Factor betaConceptsKruppel-like factor 4Cerebral cavernous malformationsEndothelial cellsCavernous malformationsFamilial cerebral cavernous malformationsCentral nervous systemDouble knockout miceGrowth factor-beta/bone morphogenetic protein signalingCerebral hemorrhageMouse mortalityPharmacological treatmentCurrent therapiesVascular malformationsKnockout miceTherapeutic targetNervous systemMesenchymal transitionKLF4 transcriptional activityMalformationsCCM3 genesFactor 4Function mutationsEndMTMorphogenetic protein signalingBone morphogenetic protein (BMP) signaling
2003
Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells
Tzima E, Reader J, Irani-Tehrani M, Ewalt K, Schwartz M, Schimmel P. Biologically active fragment of a human tRNA synthetase inhibits fluid shear stress-activated responses of endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 14903-14907. PMID: 14630953, PMCID: PMC299850, DOI: 10.1073/pnas.2436330100.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnimalsCattleCytoskeletonEndothelium, VascularGenetic VectorsHumansLuciferasesMicroscopy, FluorescenceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNeovascularization, PathologicNitric Oxide SynthaseProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionStress, MechanicalTemperatureTime FactorsTranscription, GeneticConceptsT2-TrpRSStress-responsive gene expressionHuman tryptophanyl-tRNA synthetaseStress-responsive genesExtracellular signal-regulated kinase 1/2Growth factor stimulationHuman tRNA SynthetaseSignal-regulated kinase 1/2Natural splice variantProtein kinase BShear stress-responsive genesVascular endothelial growth factor (VEGF) stimulationTryptophanyl-tRNA synthetaseVascular homeostasisGrowth factor-induced angiogenesisVascular endothelial growth factor-induced angiogenesisCytoskeletal reorganizationProtein kinaseFactor stimulationAngiogenesis-related activitiesGene expressionKinase BKinase 1/2TRNA synthetaseEndothelial cell responsesGuanine Exchange-Dependent and -Independent Effects of Vav1 on Integrin-Induced T Cell Spreading
del Pozo MA, Schwartz MA, Hu J, Kiosses WB, Altman A, Villalba M. Guanine Exchange-Dependent and -Independent Effects of Vav1 on Integrin-Induced T Cell Spreading. The Journal Of Immunology 2003, 170: 41-47. PMID: 12496381, DOI: 10.4049/jimmunol.170.1.41.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCdc42 GTP-Binding ProteinCell Cycle ProteinsCell SizeCells, CulturedDrug SynergismEnzyme ActivationFibronectinsGuanine Nucleotide Exchange FactorsHumansHybridomasIntegrinsJNK Mitogen-Activated Protein KinasesJurkat CellsMiceMitogen-Activated Protein KinasesP21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavRac GTP-Binding ProteinsT-Lymphocytes
2002
Integrins regulate the apoptotic response to DNA damage through modulation of p53
Lewis JM, Truong TN, Schwartz MA. Integrins regulate the apoptotic response to DNA damage through modulation of p53. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 3627-3632. PMID: 11904424, PMCID: PMC122574, DOI: 10.1073/pnas.062698499.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesApoptosisCaspase 3CaspasesCell AdhesionCell SurvivalChromosome AberrationsCyclin-Dependent Kinase Inhibitor p16DNA DamageFibroblastsHumansIntegrinsMelanomaMiceMutationNuclear ProteinsOrgan SpecificityProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Radiation, IonizingSarcomaTumor Cells, CulturedTumor Suppressor Protein p14ARFTumor Suppressor Protein p53ConceptsTumor cellsTherapy-resistant tumorsModulation of p53Susceptible tumor cellsDNA damageLevels of p53Low p53 levelsApoptosis of cellsTherapy resistanceAntiintegrin antibodiesCancer cellsP53 levelsSurvival of cellsP53Nonadherent cellsCell typesSurvivalApoptotic responseCellsP19 ARFApoptosisChromosomal instabilityFibroblastic cell typesDamageChemotherapy
2000
The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*
Obergfell A, Judd B, del Pozo M, Schwartz M, Koretzky G, Shattil S. The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*. Journal Of Biological Chemistry 2000, 276: 5916-5923. PMID: 11113155, DOI: 10.1074/jbc.m010639200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdaptor Proteins, Signal TransducingAnimalsBlood PlateletsCell AdhesionCell Cycle ProteinsCHO CellsCricetinaeCytoskeletonEnzyme PrecursorsFibrinogenHumansIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavPseudopodiaRac GTP-Binding ProteinsSignal TransductionSyk KinaseConceptsSLP-76SLAP-130Lamellipodia formationSLP-76 functionAdhesion-dependent activationCHO cell adhesionCell expression systemSLP-76 phosphorylationChinese hamster ovary cell expression systemSLP-76 expressionSyk tyrosine kinasePlatelet integrin αIIbβ3Sites of adhesionRac effectorPAK kinasesActin cytoskeletonAdherent CHO cellsExchange factorActin rearrangementCytoskeletal reorganizationActin reorganizationTyrosine phosphorylationExpression systemCell spreadingTyrosine kinase
1997
Suppression of Integrin Activation: A Novel Function of a Ras/Raf-Initiated MAP Kinase Pathway
Hughes P, Renshaw M, Pfaff M, Forsyth J, Keivens V, Schwartz M, Ginsberg M. Suppression of Integrin Activation: A Novel Function of a Ras/Raf-Initiated MAP Kinase Pathway. Cell 1997, 88: 521-530. PMID: 9038343, DOI: 10.1016/s0092-8674(00)81892-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell SizeCHO CellsCricetinaeCytoplasmDNA, ComplementaryEndoribonucleasesEnzyme ActivationExtracellular Matrix ProteinsFibronectinsFlow CytometryFungal ProteinsGene Expression Regulation, EnzymologicIntegrinsProtein BiosynthesisProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsProto-Oncogene Proteins c-rafRas ProteinsRecombinant Fusion ProteinsTranscription, GeneticConceptsMAP kinase pathwayKinase pathwayIntegrin activationBeta-subunit cytoplasmic domainH-RasTranscription-independent functionsSubunit cytoplasmic domainERK MAP kinase pathwayIntegrin affinity stateCell adhesion receptorsIntegrin cell adhesion receptorsActivation of integrinsNegative feedback loopSmall GTPCytoplasmic domainEffector kinaseIntegrin phosphorylationRaf-1Novel functionIntegrin functionNegative regulatorAdhesion receptorsProtein synthesisMRNA transcriptionDistinct alpha
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 resultsAnchorageInvolvement of the Small GTPase Rho in Integrin-mediated Activation of Mitogen-activated Protein Kinase*
Renshaw M, Toksoz D, Schwartz M. Involvement of the Small GTPase Rho in Integrin-mediated Activation of Mitogen-activated Protein Kinase*. Journal Of Biological Chemistry 1996, 271: 21691-21694. PMID: 8702960, DOI: 10.1074/jbc.271.36.21691.Peer-Reviewed Original ResearchA Kinase Anchor ProteinsAdaptor Proteins, Signal TransducingADP Ribose TransferasesAnimalsBotulinum ToxinsCalcium-Calmodulin-Dependent Protein KinasesCation Exchange ResinsCell AdhesionCell LineEnzyme ActivationFibronectinsGTP-Binding ProteinsIntegrinsLipidsMinor Histocompatibility AntigensMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesProto-Oncogene ProteinsRho GTP-Binding ProteinsTetradecanoylphorbol AcetateTransfection