2021
CCM3 Loss-Induced Lymphatic Defect Is Mediated by the Augmented VEGFR3-ERK1/2 Signaling
Qin L, Zhang H, Li B, Jiang Q, Lopez F, Min W, Zhou JH. CCM3 Loss-Induced Lymphatic Defect Is Mediated by the Augmented VEGFR3-ERK1/2 Signaling. Arteriosclerosis Thrombosis And Vascular Biology 2021, 41: 2943-2960. PMID: 34670407, PMCID: PMC8613000, DOI: 10.1161/atvbaha.121.316707.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosis Regulatory ProteinsCells, CulturedEndothelial CellsEndothelium, LymphaticFemaleGene DeletionHemangioma, Cavernous, Central Nervous SystemHyperplasiaMaleMAP Kinase Signaling SystemMice, Inbred StrainsModels, AnimalNF-kappa BTranslocation, GeneticVascular Endothelial Growth Factor Receptor-3ConceptsLymphatic ECsLymphatic defectsCerebral cavernous malformationsPan-endothelial cellsGrowth factor receptorTranscriptional levelTransport assaysLymphatic hyperplasiaCCM genesLymphatic dysfunctionNuclear translocationGenesFactor receptorVEGFR3ERK1/2Nuclear factorDeletionEC proliferationInhibition of VEGFR3Dependent mannerVascular endothelial growth factor receptorEndothelial growth factor receptorEC deletionAbnormal valve structureKPNA2Caveolae-mediated Tie2 signaling contributes to CCM pathogenesis in a brain endothelial cell-specific Pdcd10-deficient mouse model
Zhou HJ, Qin L, Jiang Q, Murray KN, Zhang H, Li B, Lin Q, Graham M, Liu X, Grutzendler J, Min W. Caveolae-mediated Tie2 signaling contributes to CCM pathogenesis in a brain endothelial cell-specific Pdcd10-deficient mouse model. Nature Communications 2021, 12: 504. PMID: 33495460, PMCID: PMC7835246, DOI: 10.1038/s41467-020-20774-0.Peer-Reviewed Original ResearchConceptsCerebral cavernous malformationsCCM lesionsSmooth muscle actin-positive pericytesEndothelial cell lossRegions of brainCCM pathogenesisPost-capillary venulesCerebral hemorrhagePharmacological blockadeVascular abnormalitiesEC-specific deletionCavernous malformationsMouse modelCell lossMicrovascular bedGenetic deletionLesion formationLesionsVascular dynamicsBarrier functionMicrovascular structureTwo-photon microscopyTie2PathogenesisMice
2020
Mural Cell-Specific Deletion of Cerebral Cavernous Malformation 3 in the Brain Induces Cerebral Cavernous Malformations
Wang K, Zhang H, He Y, Jiang Q, Tanaka Y, Park IH, Pober JS, Min W, Zhou HJ. Mural Cell-Specific Deletion of Cerebral Cavernous Malformation 3 in the Brain Induces Cerebral Cavernous Malformations. Arteriosclerosis Thrombosis And Vascular Biology 2020, 40: 2171-2186. PMID: 32640906, DOI: 10.1161/atvbaha.120.314586.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosis Regulatory ProteinsBrainCell CommunicationCell MovementCells, CulturedCoculture TechniquesEndothelial CellsFemaleFocal AdhesionsGene DeletionGenetic Predisposition to DiseaseHemangioma, Cavernous, Central Nervous SystemHumansMaleMembrane ProteinsMice, KnockoutMicrovesselsMyocytes, Smooth MusclePaxillinPericytesPhenotypeProtein StabilityProto-Oncogene ProteinsSignal TransductionConceptsCerebral cavernous malformationsBrain mural cellsCCM lesionsMural cellsCavernous malformationsSevere brain hemorrhageCCM pathogenesisSmooth muscle cellsWeeks of ageCell-specific deletionMural cell coverageBrain pericytesBrain hemorrhageNeonatal stageBrain vasculatureLesionsEntire brainMuscle cellsCerebral cavernous malformation 3Endothelial cellsMicePericytesSpecific deletionAdhesion formationPathogenesisBMX Represses Thrombin-PAR1–Mediated Endothelial Permeability and Vascular Leakage During Early Sepsis
Li Z, Yin M, Zhang H, Ni W, Pierce R, Zhou HJ, Min W. BMX Represses Thrombin-PAR1–Mediated Endothelial Permeability and Vascular Leakage During Early Sepsis. Circulation Research 2020, 126: 471-485. PMID: 31910739, PMCID: PMC7035171, DOI: 10.1161/circresaha.119.315769.Peer-Reviewed Original ResearchConceptsPAR1 internalizationPuncture-induced sepsisCecal ligationVascular leakageEndothelial permeabilityExpression of BmxThrombin-PAR1Early sepsisEndothelial cellsPuncture modelSignal inactivationPAR1 antagonist SCH79797Negative regulatorLung epithelial cellsTransendothelial electrical resistanceAdult stageEmbryonic stagesCultured endothelial cellsPulmonary leakageCellular analysisLung injuryPathological stimuliEndothelium dysfunctionPlatelet dysfunctionSepsis
2019
Nuclear localization of the tyrosine kinase BMX mediates VEGFR2 expression
Liu T, Li Y, Su H, Zhang H, Jones D, Zhou HJ, Ji W, Min W. Nuclear localization of the tyrosine kinase BMX mediates VEGFR2 expression. Journal Of Cellular And Molecular Medicine 2019, 24: 126-138. PMID: 31642192, PMCID: PMC6933376, DOI: 10.1111/jcmm.14663.Peer-Reviewed Original ResearchConceptsTyrosine kinase BMXVEGFR2 promoter activityPromoter activityNuclear localizationVEGFR2 promoterKinase-inactive formGene promoter activityEndothelial cellsNucleus of ECsVascular endothelial growth factor receptorSiRNA-mediated silencingAngiogenesis-related diseasesChromatin immunoprecipitationDirect transactivationSH3 domainTranscription factorsGrowth factor receptorVEGFR2 expressionNovel functionVEGFR2 transcriptionSp1Human endothelial cellsLuciferase assayEC migrationFactor receptorShort 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 generationCD34+KLF4+ Stromal Stem Cells Contribute to Endometrial Regeneration and Repair
Yin M, Zhou HJ, Lin C, Long L, Yang X, Zhang H, Taylor H, Min W. CD34+KLF4+ Stromal Stem Cells Contribute to Endometrial Regeneration and Repair. Cell Reports 2019, 27: 2709-2724.e3. PMID: 31141693, PMCID: PMC6548470, DOI: 10.1016/j.celrep.2019.04.088.Peer-Reviewed Original ResearchConceptsEndometrial regenerationEndometrial epitheliumStem cellsLocal stem cellsEndometrial repairHuman endometriumUterine hyperplasiaStromal stem cellsCD34Regenerative capacitySM22αEpitheliumCellsProliferative signalingTranscriptional activityRepairKLF4EndometriumHyperplasiaERαProtein SUMOylationRegeneration modelMice
2015
Thioredoxin-2 Inhibits Mitochondrial Reactive Oxygen Species Generation and Apoptosis Stress Kinase-1 Activity to Maintain Cardiac Function
Huang Q, Zhou HJ, Zhang H, Huang Y, Hinojosa-Kirschenbaum F, Fan P, Yao L, Belardinelli L, Tellides G, Giordano FJ, Budas GR, Min W. Thioredoxin-2 Inhibits Mitochondrial Reactive Oxygen Species Generation and Apoptosis Stress Kinase-1 Activity to Maintain Cardiac Function. Circulation 2015, 131: 1082-1097. PMID: 25628390, PMCID: PMC4374031, DOI: 10.1161/circulationaha.114.012725.Peer-Reviewed Original ResearchConceptsMitochondrial reactive oxygen species generationReactive oxygen species generationOxygen species generationASK1-dependent apoptosisMitochondrial reactive oxygen species productionPhosphorylation/activityKey mitochondrial proteinsSpecies generationMitochondrial membrane depolarizationKinase 1 activityMitochondrial proteinsReactive oxygen species productionCellular redoxMitochondrial Trx2Inhibition of ASK1Apoptotic signalingOxygen species productionThioredoxin 2Protein expression levelsKinase 1ATP productionASK1 inhibitionKnockout miceMitochondrial ultrastructureASK1 inhibitors
2014
AIP1 Mediates Vascular Endothelial Cell Growth Factor Receptor-3–Dependent Angiogenic and Lymphangiogenic Responses
Zhou HJ, Chen X, Huang Q, Liu R, Zhang H, Wang Y, Jin Y, Liang X, Lu L, Xu Z, Min W. AIP1 Mediates Vascular Endothelial Cell Growth Factor Receptor-3–Dependent Angiogenic and Lymphangiogenic Responses. Arteriosclerosis Thrombosis And Vascular Biology 2014, 34: 603-615. PMID: 24407031, PMCID: PMC3952062, DOI: 10.1161/atvbaha.113.303053.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCells, CulturedCorneaEndocytosisEndothelial CellsEndothelium, VascularEye ProteinsGuanylate KinasesHumansLymphangiogenesisMiceMice, KnockoutMicroRNAsNeuronsRas GTPase-Activating ProteinsReceptors, NotchRecombinant ProteinsRetinal NeovascularizationRNA InterferenceRNA, Small InterferingVascular Endothelial Growth Factor CVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-3ConceptsLymphatic endothelial cellsASK1-interacting protein-1VEGFR-3 signalingHuman lymphatic endothelial cellsVEGFR-3Vascular endothelial cell growth factor receptorEndothelial cellsReduced expressionDevelopmental lymphangiogenesisScaffold proteinAIP1 functionsGrowth factor receptorLymphangiogenic signalingNovel functionVEGFR-2 activityRNA knockdownCell growth factor receptorLymphangiogenic responseSimilar defectsFirst insightProtein 1Vascular endothelial cellsPathological angiogenesisSpecific deletionFactor receptor
2013
SOCS1 Prevents Graft Arteriosclerosis by Preserving Endothelial Cell Function
Qin L, Huang Q, Zhang H, Liu R, Tellides G, Min W, Yu L. SOCS1 Prevents Graft Arteriosclerosis by Preserving Endothelial Cell Function. Journal Of The American College Of Cardiology 2013, 63: 21-29. PMID: 23994402, PMCID: PMC3932325, DOI: 10.1016/j.jacc.2013.08.694.Peer-Reviewed Original ResearchConceptsAdhesion molecule-1Cell adhesion molecule-1Graft arteriosclerosisMolecule-1Aortic endothelial cellsEndothelial cellsEndothelial functionGA progressionNeointima formationLate cardiac allograft failureVascular cell adhesion molecule-1Intercellular adhesion molecule-1Cytokine-induced adhesion molecule expressionCardiac allograft failureNormal endothelial functionEndothelial inflammatory responseInflammatory cell infiltrationMouse aortic endothelial cellsAdhesion molecule expressionPlatelet/endothelial cell adhesion molecule-1Better vascular functionEndothelial cell adhesion molecule-1Cytokine-induced expressionEndothelial adhesion moleculesCultured aortic endothelial cells
2012
Both Internalization and AIP1 Association Are Required for Tumor Necrosis Factor Receptor 2-Mediated JNK Signaling
Ji W, Li Y, Wan T, Wang J, Zhang H, Chen H, Min W. Both Internalization and AIP1 Association Are Required for Tumor Necrosis Factor Receptor 2-Mediated JNK Signaling. Arteriosclerosis Thrombosis And Vascular Biology 2012, 32: 2271-2279. PMID: 22743059, PMCID: PMC3421067, DOI: 10.1161/atvbaha.112.253666.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBinding SitesCells, CulturedEndothelial CellsEnzyme ActivationHuman Umbilical Vein Endothelial CellsHumansJNK Mitogen-Activated Protein KinasesMiceMice, KnockoutNF-kappa BProtein Interaction Domains and MotifsProtein TransportRas GTPase-Activating ProteinsReceptors, Tumor Necrosis Factor, Type IReceptors, Tumor Necrosis Factor, Type IISequence DeletionSignal TransductionTime FactorsTNF Receptor-Associated Factor 2TransfectionTumor Necrosis Factor-alphaConceptsJNK signalingApoptotic signalingJNK activationDomain IICaspase-dependent cell deathCell deathTNF receptor 1C-Jun N-terminal kinaseDependent cell survivalN-terminal kinaseNF-κB activationNF-κBDeletion analysisTNF responseLL motifPlasma membraneIntracellular regionCell survivalDomain IJNKSignalingDistinct rolesTNFR2 deletionProtein 1Specific deletion
2011
AIP1 Prevents Graft Arteriosclerosis by Inhibiting Interferon-&ggr;–Dependent Smooth Muscle Cell Proliferation and Intimal Expansion
Yu L, Qin L, Zhang H, He Y, Chen H, Pober JS, Tellides G, Min W. AIP1 Prevents Graft Arteriosclerosis by Inhibiting Interferon-&ggr;–Dependent Smooth Muscle Cell Proliferation and Intimal Expansion. Circulation Research 2011, 109: 418-427. PMID: 21700930, PMCID: PMC3227522, DOI: 10.1161/circresaha.111.248245.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAorta, AbdominalAorta, ThoracicArteriosclerosisCell MovementCell ProliferationCells, CulturedDisease Models, AnimalHumansInterferon-gammaJanus Kinase 2MaleMiceMice, KnockoutMinor Histocompatibility AntigensMuscle, Smooth, VascularRas GTPase-Activating ProteinsReceptors, InterferonSignal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorTime FactorsTunica IntimaVascular GraftingConceptsASK1-interacting protein-1Neointima formationTransplantation modelIntimal expansionSingle minor histocompatibility antigenSmooth muscle cell proliferationMinor histocompatibility antigensAortic transplantation modelAorta transplantation modelMuscle cell proliferationVSMC accumulationDonor graftsGraft arteriosclerosisIntimal formationIntravenous administrationHistocompatibility antigensVSMC proliferationMouse aortaVSMC migrationIFNProliferative diseasesEndothelial cellsProtein 1Cell proliferationJAK-STAT signaling
2010
Functional Analyses of the Bone Marrow Kinase in the X Chromosome in Vascular Endothelial Growth Factor–Induced Lymphangiogenesis
Jones D, Xu Z, Zhang H, He Y, Kluger MS, Chen H, Min W. Functional Analyses of the Bone Marrow Kinase in the X Chromosome in Vascular Endothelial Growth Factor–Induced Lymphangiogenesis. Arteriosclerosis Thrombosis And Vascular Biology 2010, 30: 2553-2561. PMID: 20864667, PMCID: PMC3106279, DOI: 10.1161/atvbaha.110.214999.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCorneaEndothelial CellsFemaleHumansLymphangiogenesisLymphatic VesselsMaleMiceMice, Inbred C57BLMice, KnockoutPhosphorylationProtein-Tyrosine KinasesRecombinant ProteinsRNA InterferenceSignal TransductionSkinTransfectionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor CVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor Receptor-3ConceptsBone marrow kinaseX chromosomeLymphatic endothelial cell tube formationVascular endothelial growth factorVEGFR-3 receptorRole of BmxLymphatic endothelial cellsEndothelial cell tube formationVEGFR-2 activationCell tube formationLymphangiogenic signalingReceptor autophosphorylationFunctional analysisLymphangiogenic responseFirst insightPathological angiogenesisWild-type micePharmacological inhibitionTube formationBMXChromosomesKinaseVEGFR-3Critical roleSignaling
2009
AIP1 Functions as Arf6-GAP to Negatively Regulate TLR4 Signaling2
Wan T, Liu T, Zhang H, Tang S, Min W. AIP1 Functions as Arf6-GAP to Negatively Regulate TLR4 Signaling2. Journal Of Biological Chemistry 2009, 285: 3750-3757. PMID: 19948740, PMCID: PMC2823516, DOI: 10.1074/jbc.m109.069385.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsAmino Acid SequenceAnimalsCarrier ProteinsCattleCell LineCells, CulturedChlorocebus aethiopsCOS CellsGTPase-Activating ProteinsGuanylate KinasesHumansImmunoblottingLipopolysaccharidesMembrane GlycoproteinsMiceMice, KnockoutMitogen-Activated Protein KinasesMolecular Sequence DataMyeloid Differentiation Factor 88NF-kappa BPhosphatidylinositol 4,5-DiphosphateProtein BindingReceptors, Interleukin-1Sequence Homology, Amino AcidToll-Like Receptor 4TransfectionConceptsGTPase-activating proteinsArf6 GAPAIP1 functionsNovel GTPase-activating proteinInhibition of ARF6Pleckstrin homologyGAP domainAdaptor proteinSmall GTPaseDisrupts formationPlasma membraneAIP1MAPK pathwayLipid precursorsToll-like receptor 4Arf6NF-kappaBComplex componentsToll-like receptorsProteinRich sitesGTPaseHomologyComplexesCells increases
2008
AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation
Min W, Lin Y, Tang S, Yu L, Zhang H, Wan T, Luhn T, Fu H, Chen H. AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation. Circulation Research 2008, 102: 840-848. PMID: 18292600, DOI: 10.1161/circresaha.107.168153.Peer-Reviewed Original ResearchConceptsASK1-JNK signalingASK1 dephosphorylationAssociation of PP2APP2A catalytic subunitCatalytic inactive formPP2A inhibitor okadaicASK1-JNK activationC-Jun N-terminal kinaseActivation of JNKEndothelial cellsN-terminal kinasePhosphatase PP2ACritical rolePotential phosphataseProtein phosphataseGAP domainInhibitor okadaicProtein familyCatalytic subunitC2 domainPP2AAIP1Novel memberApoptotic signalingRNA knockdownSENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
Li X, Luo Y, Yu L, Lin Y, Luo D, Zhang H, He Y, Kim YO, Kim Y, Tang S, Min W. SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis. Cell Death & Differentiation 2008, 15: 739-750. PMID: 18219322, DOI: 10.1038/sj.cdd.4402303.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAnimalsAntioxidantsApoptosisCarrier ProteinsCattleCells, CulturedCysteine EndopeptidasesCytoplasmEndopeptidasesEndothelial CellsFibroblastsHumansMAP Kinase Kinase Kinase 5MiceMice, KnockoutMutationProtein KinasesProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProtein TransportReactive Oxygen SpeciesRecombinant ProteinsRNA InterferenceRNA, Small InterferingSignal TransductionSmall Ubiquitin-Related Modifier ProteinsThioredoxinsTime FactorsTransfectionTumor Necrosis Factor-alphaConceptsASK1-dependent apoptosisASK1-JNK activationCytoplasmic translocationMouse embryonic fibroblast cellsNuclear translocationSUMO-specific proteasesWild-type formEmbryonic fibroblast cellsNuclear importAntioxidant protein thioredoxinHIPK1Mutant formsEndothelial cellsDeSUMOylationProtein thioredoxinSubsequent cytoplasmic translocationSENP1TranslocationCritical functionsThioredoxinFibroblast cellsApoptosisCellsActivationSUMO
2007
RIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*
Zhang R, Zhang H, Lin Y, Li J, Pober JS, Min W. RIP1-mediated AIP1 Phosphorylation at a 14-3-3-binding Site Is Critical for Tumor Necrosis Factor-induced ASK1-JNK/p38 Activation*. Journal Of Biological Chemistry 2007, 282: 14788-14796. PMID: 17389591, DOI: 10.1074/jbc.m701148200.Peer-Reviewed Original ResearchMeSH Keywords14-3-3 ProteinsAdaptor Proteins, Signal TransducingAmino Acid SubstitutionAnimalsApoptosisCarrier ProteinsCattleCells, CulturedEndothelial CellsEnzyme ActivationGuanylate KinasesHumansMAP Kinase Kinase 4MAP Kinase Kinase Kinase 5MAP Kinase Signaling SystemMultiprotein ComplexesMutation, MissenseP38 Mitogen-Activated Protein KinasesPhosphorylationProtein BindingProtein Processing, Post-TranslationalProteinsReceptor-Interacting Protein Serine-Threonine KinasesTNF Receptor-Associated Factor 2Tumor Necrosis Factor-alphaConceptsJNK/p38 activationP38 activationTRAF2-ASK1ASK1-JNK activationPhospho-specific antibodiesTNF treatmentEndothelial cellsComplex formationGAP domainProtein familyTerminal domainAIP1Novel memberApoptotic signalingTNF signalingRNA knockdownRIP1PhosphorylationProtein 1ASK1-interacting protein-1EC apoptosisTRAF2ASK1Similar kineticsTumor necrosis factorEndothelial-Specific Expression of Mitochondrial Thioredoxin Improves Endothelial Cell Function and Reduces Atherosclerotic Lesions
Zhang H, Luo Y, Zhang W, He Y, Dai S, Zhang R, Huang Y, Bernatchez P, Giordano FJ, Shadel G, Sessa WC, Min W. Endothelial-Specific Expression of Mitochondrial Thioredoxin Improves Endothelial Cell Function and Reduces Atherosclerotic Lesions. American Journal Of Pathology 2007, 170: 1108-1120. PMID: 17322393, PMCID: PMC1864879, DOI: 10.2353/ajpath.2007.060960.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaApolipoproteins EAtherosclerosisCells, CulturedEndothelial CellsFlow CytometryImmunoblottingImmunohistochemistryMiceMice, TransgenicMicroscopy, ConfocalMitochondrial ProteinsNitric OxideReactive Oxygen SpeciesReverse Transcriptase Polymerase Chain ReactionThioredoxinsVasodilationConceptsTg miceAtherosclerotic lesionsOxidative stressNitric oxide levelsEC functionDeficient mouse modelEndothelial cell functionAtherosclerosis developmentEnhanced vasodilationVascular EC functionEndothelium functionApolipoprotein EControl littermatesMouse modelOxide levelsMice showCapacity of ECEndothelial-specific expressionEndothelial cellsCritical roleReactive oxygen speciesCell functionMiceTotal antioxidantsLesions
2006
SOCS1 Inhibits Tumor Necrosis Factor-induced Activation of ASK1-JNK Inflammatory Signaling by Mediating ASK1 Degradation*
He Y, Zhang W, Zhang R, Zhang H, Min W. SOCS1 Inhibits Tumor Necrosis Factor-induced Activation of ASK1-JNK Inflammatory Signaling by Mediating ASK1 Degradation*. Journal Of Biological Chemistry 2006, 281: 5559-5566. PMID: 16407264, DOI: 10.1074/jbc.m512338200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCells, CulturedEndothelial CellsEnzyme ActivationInflammationIntracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase Kinase 5MiceMice, KnockoutRecombinant Fusion ProteinsRepressor ProteinsSignal TransductionSrc Homology DomainsSuppressor of Cytokine Signaling 1 ProteinSuppressor of Cytokine Signaling 3 ProteinSuppressor of Cytokine Signaling ProteinsTumor Necrosis Factor-alphaConceptsASK1 degradationDissociation of ASK1Member of suppressorTumor necrosis factor-induced activationEndothelial cellsActivation of JNKPhosphotyrosine bindingUndergoes ubiquitinationSH2 domainProteasomal inhibitorsASK1 activationNegative regulatorApoptotic responseASK1Cytokine signalingSOCS1 functionsASK1 expressionSOCS1Tumor necrosis factorSignalingSOCS1-deficient mice