2020
ANGPTL4: a multifunctional protein involved in metabolism and vascular homeostasis.
Fernández-Hernando C, Suárez Y. ANGPTL4: a multifunctional protein involved in metabolism and vascular homeostasis. Current Opinion In Hematology 2020, 27: 206-213. PMID: 32205586, PMCID: PMC9013473, DOI: 10.1097/moh.0000000000000580.Peer-Reviewed Original ResearchConceptsStem cell regulationPotential therapeutic targetLipid metabolismCell-specific functionsSpecific molecular eventsNonmetabolic functionsRegulatory circuitsMultifunctional proteinTherapeutic targetUnanticipated roleInvolvement of ANGPTL4Molecular eventsCell regulationPhysiological roleTherapeutic applicationsPredominant expressionVascular biologyPotential therapeutic applicationsVascular homeostasisPathophysiological conditionsDifferent disease settingsANGPTL4MetabolismFirst discoveryBiological effects
2019
Short AIP1 (ASK1-Interacting Protein-1) Isoform Localizes to the Mitochondria and Promotes Vascular Dysfunction
Li Z, Li L, Zhang H, Zhou HJ, Ji W, Min W. Short AIP1 (ASK1-Interacting Protein-1) Isoform Localizes to the Mitochondria and Promotes Vascular Dysfunction. Arteriosclerosis Thrombosis And Vascular Biology 2019, 40: 112-127. PMID: 31619063, PMCID: PMC7204498, DOI: 10.1161/atvbaha.119.312976.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAorta, ThoracicApoptosisArteriosclerosisBlotting, WesternCells, CulturedDisease Models, AnimalDNAEndothelium, VascularGene Expression RegulationGenome-Wide Association StudyHumansMiceMice, Inbred C57BLMice, TransgenicMicroscopy, FluorescenceMitochondriaras GTPase-Activating ProteinsSignal TransductionConceptsN-terminal pleckstrin homology domainHuman genome-wide association studiesGenome-wide association studiesPleckstrin homology domainMitochondrial reactive oxygen species generationEndothelial cellsH3K9 trimethylationHomology domainReactive oxygen species productionOxygen species productionReactive oxygen speciesReactive oxygen species generationAssociation studiesRegulatory factorsEpigenetic inhibitionEC activationOxygen species generationDependent pathwayVascular endothelial cellsProteolytic degradationSpecies productionOxygen speciesVascular homeostasisMitochondriaSpecies generation
2014
Restoration of Impaired Endothelial Myocyte Enhancer Factor 2 Function Rescues Pulmonary Arterial Hypertension
Kim J, Hwangbo C, Hu X, Kang Y, Papangeli I, Mehrotra D, Park H, Ju H, McLean DL, Comhair SA, Erzurum SC, Chun HJ. Restoration of Impaired Endothelial Myocyte Enhancer Factor 2 Function Rescues Pulmonary Arterial Hypertension. Circulation 2014, 131: 190-199. PMID: 25336633, PMCID: PMC4293354, DOI: 10.1161/circulationaha.114.013339.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApelinArteriolesCells, CulturedDisease Models, AnimalDrug Evaluation, PreclinicalEndothelial CellsFibroblast Growth Factor 2HemodynamicsHistone Deacetylase InhibitorsHydroxamic AcidsHypertension, PulmonaryHypertrophy, Right VentricularHypoxiaIntercellular Signaling Peptides and ProteinsMaleMEF2 Transcription FactorsMicroRNAsMonocrotalinePulmonary ArteryPyrrolesRatsRats, Sprague-DawleyRNA InterferenceRNA, Small InterferingTranscription, GeneticConceptsPulmonary arterial hypertensionPulmonary artery endothelial cellsPulmonary vascular homeostasisPAH-pulmonary artery endothelial cellsMyocyte enhancer factor 2Arterial hypertensionCauses of PAHVascular homeostasisExperimental pulmonary hypertension modelsIncreased pulmonary arterial pressurePulmonary artery smooth muscle cellsArtery smooth muscle cellsMEF2 activityRight ventricular failurePulmonary arterial pressurePulmonary hypertension modelPotential therapeutic strategyPotential therapeutic valueSmooth muscle cellsArtery endothelial cellsFactor 2Potential adverse effectsTranscription factor myocyte enhancer factor 2Class IIa HDACsVentricular failureFibroblast growth factor receptor 1 is a key inhibitor of TGFβ signaling in the endothelium
Chen PY, Qin L, Tellides G, Simons M. Fibroblast growth factor receptor 1 is a key inhibitor of TGFβ signaling in the endothelium. Science Signaling 2014, 7: ra90. PMID: 25249657, DOI: 10.1126/scisignal.2005504.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell TransdifferentiationCoronary VesselsEndothelium, VascularExtracellular MatrixFibroblastsGraft RejectionHeart TransplantationHeterograftsHindlimbHuman Umbilical Vein Endothelial CellsHumansIschemiaMesodermMiceMice, Mutant StrainsMicroRNAsMuscle, Smooth, VascularNeointimaReceptor, Fibroblast Growth Factor, Type 1Receptors, Fibroblast Growth FactorSignal TransductionSmad2 ProteinTransforming Growth Factor betaTransplantation ChimeraConceptsFibroblast growth factor receptor 1Growth factor receptor 1Factor receptor 1Extracellular matrixSmooth muscle cellsMuscle cellsEndothelial cell-specific knockoutKey regulatorReceptor 1TGFβ signalingCell-specific knockoutDecreased abundanceMesenchymal transitionKey inhibitorVascular homeostasisGrowth factorDevelopment of EndMTRecurrence of stenosisTGFβGrowth of neointimaCellsNeointima formationEndMTVascular lumenSignalingScience Signaling Podcast: 23 September 2014
Simons M, VanHook A. Science Signaling Podcast: 23 September 2014. Science Signaling 2014, 7 DOI: 10.1126/scisignal.2005857.Peer-Reviewed Original ResearchTGF-β signalingMesenchymal transitionReceptor FGFR1Line blood vesselsFibroblast growth factor (FGF) pathwayEndothelial cellsTGF-β receptorCell biologyPolarized cellsGrowth factor pathwaysScience SignalingSignalingBlood vesselsFactor pathwayVascular homeostasisFGFNormal functionCellsFGFR1EndMTNormal conditionsMicroRNAsSenior authorBiologyHomeostasisCeramide-Activated Phosphatase Mediates Fatty Acid–Induced Endothelial VEGF Resistance and Impaired Angiogenesis
Mehra VC, Jackson E, Zhang XM, Jiang XC, Dobrucki LW, Yu J, Bernatchez P, Sinusas AJ, Shulman GI, Sessa WC, Yarovinsky TO, Bender JR. Ceramide-Activated Phosphatase Mediates Fatty Acid–Induced Endothelial VEGF Resistance and Impaired Angiogenesis. American Journal Of Pathology 2014, 184: 1562-1576. PMID: 24606881, PMCID: PMC4005977, DOI: 10.1016/j.ajpath.2014.01.009.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaArteriesCattleCeramidesDiet, High-FatEndothelial CellsEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHaploinsufficiencyHindlimbHumansIschemiaMice, Inbred C57BLNeovascularization, PhysiologicNitric OxideNitric Oxide Synthase Type IIIPalmitic AcidPhosphorylationProtein Phosphatase 2Proto-Oncogene Proteins c-aktSerine C-PalmitoyltransferaseSignal TransductionVascular Endothelial Growth Factor AConceptsPP2A inhibitor okadaic acidProtein phosphatase 2AInhibitor okadaic acidVEGF-induced signalingSerine palmitoyltransferase inhibitor myriocinDe novo ceramide synthesisPhosphatase 2AENOS agonistsNovo ceramide synthesisPalmitic acidAngiogenic responsePotential molecular targetsOkadaic acidEndothelial cellsEarly speciesEndothelial cell responsesCord formationVEGFR2 phosphorylationSaturated free fatty acidVEGF resistanceCeramide synthesisResistance mechanismsMolecular targetsVascular homeostasisPhosphorylation
2013
D‐series resolvin attenuates vascular smooth muscle cell activation and neointimal hyperplasia following vascular injury
Miyahara T, Runge S, Chatterjee A, Chen M, Mottola G, Fitzgerald JM, Serhan CN, Conte MS. D‐series resolvin attenuates vascular smooth muscle cell activation and neointimal hyperplasia following vascular injury. The FASEB Journal 2013, 27: 2220-2232. PMID: 23407709, PMCID: PMC3659350, DOI: 10.1096/fj.12-225615.Peer-Reviewed Original ResearchConceptsD-series resolvinsVascular injuryLipid mediatorsNeointimal hyperplasiaBalloon-injured rabbit arteriesMonocyte adhesionVascular smooth muscle cell activationSuperoxide productionSmooth muscle cell activationSpecialized lipid mediatorsExpression of receptorsProinflammatory gene expressionDose-dependent inhibitionMuscle cell activationVascular smooth muscle cell phenotypeSmooth muscle cell phenotypeMuscle cell phenotypeArterial angioplastyLeukocyte recruitmentHuman VSMCsVSMC proliferationGene expression assaysRabbit arteriesVascular homeostasisRvD2
2012
An endothelial apelin-FGF link mediated by miR-424 and miR-503 is disrupted in pulmonary arterial hypertension
Kim J, Kang Y, Kojima Y, Lighthouse JK, Hu X, Aldred MA, McLean DL, Park H, Comhair SA, Greif DM, Erzurum SC, Chun HJ. An endothelial apelin-FGF link mediated by miR-424 and miR-503 is disrupted in pulmonary arterial hypertension. Nature Medicine 2012, 19: 74-82. PMID: 23263626, PMCID: PMC3540168, DOI: 10.1038/nm.3040.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApelinCell MovementCell ProliferationCells, CulturedCulture Media, ConditionedDown-RegulationEndothelial CellsFamilial Primary Pulmonary HypertensionFibroblast Growth Factor 2HumansHypertension, PulmonaryIntercellular Signaling Peptides and ProteinsMiceMice, Inbred C57BLMice, KnockoutMicroRNAsMuscle, Smooth, VascularMyocytes, Smooth MusclePulmonary ArteryRatsReceptor, Fibroblast Growth Factor, Type 1RNA InterferenceRNA, Small InterferingSignal TransductionVascular DiseasesConceptsPulmonary arterial hypertensionArterial hypertensionVascular smooth muscle cellsPulmonary endothelial cellsSmooth muscle cellsEndothelial cell proliferationPulmonary hypertensionPeptide apelinCytokine productionRat modelVascular homeostasisHypertensionMiR-503MiR-424Endothelial cellsCell proliferation
2008
Prohibitin-1 maintains the angiogenic capacity of endothelial cells by regulating mitochondrial function and senescence
Schleicher M, Shepherd BR, Suarez Y, Fernandez-Hernando C, Yu J, Pan Y, Acevedo LM, Shadel GS, Sessa WC. Prohibitin-1 maintains the angiogenic capacity of endothelial cells by regulating mitochondrial function and senescence. Journal Of Cell Biology 2008, 180: 101-112. PMID: 18195103, PMCID: PMC2213620, DOI: 10.1083/jcb.200706072.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCells, CulturedCellular SenescenceCytoskeletonElectron Transport Complex IEndothelial CellsEndothelium, VascularHumansMiceMice, Inbred StrainsMitochondriaMitochondrial MembranesNeovascularization, PhysiologicNeuropeptidesPhosphatidylinositol 3-KinasesProhibitinsProto-Oncogene Proteins c-aktrac GTP-Binding Proteinsrac1 GTP-Binding ProteinReactive Oxygen SpeciesRepressor ProteinsSignal TransductionConceptsProhibitin 1Mitochondrial functionKnockdown of PHB1Inner mitochondrial membraneEndothelial cell motilityEndothelial cellsCytoskeletal rearrangementsMitochondrial membraneVivo angiogenesis assaysCell motilityAngiogenic capacityCellular senescenceReactive oxygen speciesMitochondrial productionFunctional blood vesselsImportant regulatorSenescenceAngiogenesis assayTube formationOxygen speciesVascular homeostasisCellsVascular systemRac1Yeast
2007
Acute tissue-type plasminogen activator release in human microvascular endothelial cells: The roles of Gαq, PLC-β, IP3 and 5,6-epoxyeicosatrienoic acid
Muldowney JA, Painter CA, Sanders-Bush E, Brown NJ, Vaughan DE. Acute tissue-type plasminogen activator release in human microvascular endothelial cells: The roles of Gαq, PLC-β, IP3 and 5,6-epoxyeicosatrienoic acid. Thrombosis And Haemostasis 2007, 97: 263-271. PMID: 17264956, DOI: 10.1160/th05-02-0092.Peer-Reviewed Original ResearchMeSH Keywords8,11,14-Eicosatrienoic AcidAortaBiological FactorsCell ProliferationCells, CulturedDose-Response Relationship, DrugEndothelial CellsEpoprostenolGTP-Binding Protein alpha Subunits, Gq-G11HumansInositol 1,4,5-TrisphosphateIsoenzymesMicrocirculationNitric OxidePhospholipase C betaPotassiumSignal TransductionThrombinTime FactorsTissue Plasminogen ActivatorType C PhospholipasesUmbilical VeinsConceptsT-PA releaseHuman microvascular endothelial cellsMicrovascular endothelial cellsEpoxyeicosatrienoic acidsTissue-type plasminogen activatorTissue-type plasminogen activator releaseEndothelial cellsIP3 receptor antagonistCalcium signalingT-PA antigenRole of GαqPlasminogen activator releaseMS-PPOHPhysiologic releaseCytochrome P450 inhibitorsL-NAMEEET antagonistReceptor antagonistActivator releaseVascular homeostasisNitric oxideProstacyclinPlasminogen activatorEET-methyl esterMicroM concentration
2005
A mechanosensory complex that mediates the endothelial cell response to fluid shear stress
Tzima E, Irani-Tehrani M, Kiosses WB, Dejana E, Schultz DA, Engelhardt B, Cao G, DeLisser H, Schwartz MA. A mechanosensory complex that mediates the endothelial cell response to fluid shear stress. Nature 2005, 437: 426-431. PMID: 16163360, DOI: 10.1038/nature03952.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDCadherinsCattleCell AdhesionCells, CulturedEndothelial CellsFemaleGene DeletionMechanotransduction, CellularMiceMice, KnockoutMultiprotein ComplexesNF-kappa BPlatelet Endothelial Cell Adhesion Molecule-1RatsStress, MechanicalVascular Endothelial Growth Factor Receptor-2ConceptsDownstream inflammatory genesPECAM-1 knockout miceVascular endothelial cell cadherinVascular remodellingHigh-affinity stateInflammatory genesNF-κBVascular homeostasisEndothelial cell responsesCell responsesMechanosensory complexPECAM-1Heterologous cellsPathway upstreamCardiac developmentIntegrin activationAtherogenesisMechanism of transductionPathwayMice
2004
A new role for Nogo as a regulator of vascular remodeling
Acevedo L, Yu J, Erdjument-Bromage H, Miao RQ, Kim JE, Fulton D, Tempst P, Strittmatter SM, Sessa WC. A new role for Nogo as a regulator of vascular remodeling. Nature Medicine 2004, 10: 382-388. PMID: 15034570, DOI: 10.1038/nm1020.Peer-Reviewed Original ResearchConceptsSmooth muscle cellsVascular remodelingMuscle cellsVascular smooth muscle cellsCentral nervous systemIntact blood vesselsVascular injuryAxonal regenerationNeointimal proliferationMice promotesKnockout miceNervous systemVascular homeostasisFamily of proteinsVascular expansionEndothelial cellsBlood vesselsNogoNogo isoformsLipid raftsProteomic analysisN-terminusRemodelingGene transferCells
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 responses
2000
Redox Control of Vascular Nitric Oxide Bioavailability
Price D, Vita J, Keaney J. Redox Control of Vascular Nitric Oxide Bioavailability. Antioxidants And Redox Signaling 2000, 2: 919-935. PMID: 11213492, DOI: 10.1089/ars.2000.2.4-919.BooksConceptsVascular nitric oxide bioavailabilityImportant public health implicationsNitric oxide bioavailabilityVascular oxidative stressPublic health implicationsVascular diseaseVascular homeostasisAntioxidant stressOxidative stressBiologic activityDisease statesHealth implicationsDiseaseHuman diseasesClear mechanism
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