2022
Mitochondrial dysfunction induces ALK5-SMAD2-mediated hypovascularization and arteriovenous malformations in mouse retinas
Zhang H, Li B, Huang Q, López-Giráldez F, Tanaka Y, Lin Q, Mehta S, Wang G, Graham M, Liu X, Park I, Eichmann A, Min W, Zhou J. Mitochondrial dysfunction induces ALK5-SMAD2-mediated hypovascularization and arteriovenous malformations in mouse retinas. Nature Communications 2022, 13: 7637. PMID: 36496409, PMCID: PMC9741628, DOI: 10.1038/s41467-022-35262-w.Peer-Reviewed Original ResearchConceptsMitochondrial dysfunctionThioredoxin 2Single-cell RNA-seq analysisRNA-seq analysisMutant miceNuclear genesMitochondrial proteinsMitochondrial localizationHuman retinal diseasesTranscriptional factorsGene expressionMutant retinasMitochondrial activityExtracellular matrixNovel mechanismVascular maturationArteriovenous malformationsGenetic deficiencyVessel growthSmad2Mouse retinaVascular malformationsMechanistic studiesBasement membraneRetinal vascular malformations
2021
Caveolae-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
Mitophagy-mediated adipose inflammation contributes to type 2 diabetes with hepatic insulin resistance
He F, Huang Y, Song Z, Zhou HJ, Zhang H, Perry RJ, Shulman GI, Min W. Mitophagy-mediated adipose inflammation contributes to type 2 diabetes with hepatic insulin resistance. Journal Of Experimental Medicine 2020, 218: e20201416. PMID: 33315085, PMCID: PMC7927432, DOI: 10.1084/jem.20201416.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAdipose TissueAnimalsDiabetes Mellitus, Type 2Diet, High-FatEnergy MetabolismFatty LiverGene DeletionGene TargetingGluconeogenesisHomeostasisHumansHyperglycemiaInflammationInsulin ResistanceLipogenesisLiverMaleMice, Inbred C57BLMice, KnockoutMitochondriaMitophagyNF-kappa BOxidative StressPhenotypeReactive Oxygen SpeciesSequestosome-1 ProteinSignal TransductionThioredoxinsConceptsHepatic insulin resistanceWhite adipose tissueInsulin resistanceAdipose inflammationType 2 diabetes mellitusLipid metabolic disordersNF-κB inhibitorAdipose-specific deletionWhole-body energy homeostasisAltered fatty acid metabolismFatty acid metabolismT2DM progressionT2DM patientsDiabetes mellitusReactive oxygen species pathwayHepatic steatosisMetabolic disordersNF-κBP62/SQSTM1Adipose tissueHuman adipocytesEnergy homeostasisExcessive mitophagyOxygen species pathwayInflammationMural 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 generation
2018
SUMOylation of VEGFR2 regulates its intracellular trafficking and pathological angiogenesis
Zhou HJ, Xu Z, Wang Z, Zhang H, Zhuang Z, Simons M, Min W. SUMOylation of VEGFR2 regulates its intracellular trafficking and pathological angiogenesis. Nature Communications 2018, 9: 3303. PMID: 30120232, PMCID: PMC6098000, DOI: 10.1038/s41467-018-05812-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCorneaCysteine EndopeptidasesDiabetes MellitusEndopeptidasesGene DeletionGene Knock-In TechniquesGene SilencingGolgi ApparatusHuman Umbilical Vein Endothelial CellsHumansIntracellular SpaceMaleMice, Inbred C57BLMice, KnockoutNeovascularization, PathologicProtein TransportRetinaSignal TransductionSUMO-1 ProteinSumoylationVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2ConceptsPathological angiogenesisPotential therapeutic targetRegulation of VEGFR2Non-sumoylated formEndothelial-specific deletionDiabetic miceHindlimb ischemiaTherapeutic targetDiabetic settingControl of angiogenesisEndothelial cellsAngiogenesisVEGFR2Surface expressionVEGFR2 activityTissue repairSENP1
2017
Lead promotes abnormal angiogenesis induced by CCM3 gene defects via mitochondrial pathway
Sun Y, Zhang H, Xing X, Zhao Z, He J, Li J, Chen J, Wang M, He Y. Lead promotes abnormal angiogenesis induced by CCM3 gene defects via mitochondrial pathway. Journal Of Developmental Origins Of Health And Disease 2017, 9: 182-190. PMID: 29110746, DOI: 10.1017/s2040174417000782.Peer-Reviewed Original ResearchConceptsMouse embryosYolk sacHeterozygous mouse embryosGene defectsCCM3 genesPrimary human umbilical vein endothelial cellsLead exposureMitochondrial DNAEmbryonic developmentMtDNA biogenesisMitochondrial morphologyCardiovascular developmentHuman umbilical vein endothelial cellsMitochondrial pathwayGene knockoutEndothelial cellsUmbilical vein endothelial cellsVascular developmentMitochondria pathwayVein endothelial cellsPrimary cellsGenesRNA expressionCell proliferationEmbryos
2015
AIP1 Expression in Tumor Niche Suppresses Tumor Progression and Metastasis
Ji W, Li Y, He Y, Yin M, Zhou HJ, Boggon TJ, Zhang H, Min W. AIP1 Expression in Tumor Niche Suppresses Tumor Progression and Metastasis. Cancer Research 2015, 75: 3492-3504. PMID: 26139244, PMCID: PMC4558200, DOI: 10.1158/0008-5472.can-15-0088.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBreast NeoplasmsCarrier ProteinsCell Line, TumorEpithelial-Mesenchymal TransitionGene Expression Regulation, NeoplasticGuanylate KinasesHumansMelanoma, ExperimentalMiceNeoplasm MetastasisNeovascularization, PathologicProtein Kinase InhibitorsSignal TransductionTumor MicroenvironmentVascular Endothelial Growth Factor Receptor-2ConceptsEpithelial-mesenchymal transitionPremetastatic niche formationTumor growthAugments tumor growthBreast cancer modelSuppresses tumor progressionVascular endothelial cellsNiche formationSystemic administrationCancer modelVEGFR2 kinase inhibitorTumor neovascularizationTumor progressionTumor angiogenesisTumor microenvironmentTumor cellsEndothelial cellsMetastasisKinase inhibitorsTumor nicheVascular ECsSpecific deletionVascular environmentEMT switchAIP1 gene
2013
AIP1 Suppresses Atherosclerosis by Limiting Hyperlipidemia-Induced Inflammation and Vascular Endothelial Dysfunction
Huang Q, Qin L, Dai S, Zhang H, Pasula S, Zhou H, Chen H, Min W. AIP1 Suppresses Atherosclerosis by Limiting Hyperlipidemia-Induced Inflammation and Vascular Endothelial Dysfunction. Arteriosclerosis Thrombosis And Vascular Biology 2013, 33: 795-804. PMID: 23413429, PMCID: PMC3637885, DOI: 10.1161/atvbaha.113.301220.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortic DiseasesApolipoproteins EAtherosclerosisBiomarkersBone Marrow TransplantationCholesterolCytokinesDisease Models, AnimalDose-Response Relationship, DrugEndothelium, VascularGene Expression RegulationHyperlipidemiasInflammationInflammation MediatorsLipoproteinsLipoproteins, LDLMacrophagesMiceMice, KnockoutNF-kappa BRas GTPase-Activating ProteinsSignal TransductionTriglyceridesVasoconstrictionVasoconstrictor AgentsVasodilationVasodilator AgentsConceptsInflammatory responseAtherosclerotic lesionsAortic ECsNuclear factor-κB (NF-κB) activityVascular endothelial dysfunctionPlasma inflammatory cytokinesWestern-type dietTotal cholesterol levelsIncreased inflammatory responseNuclear factor-κB signalingEndothelial cell dysfunctionAccumulation of macrophagesDouble knockout miceFactor-κB signalingNull mouse modelEndothelial dysfunctionProinflammatory mediatorsSuppresses AtherosclerosisControl miceInflammatory moleculesLipoprotein profileInflammatory cytokinesCholesterol levelsAortic rootEC dysfunction
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 roleSignalingChapter 19 Thioredoxin and Redox Signaling in Vasculature—Studies Using Trx2 Endothelium-Specific Transgenic Mice
Min W, Xu L, Zhou H, Huang Q, Zhang H, He Y, Zhe X, Luo Y. Chapter 19 Thioredoxin and Redox Signaling in Vasculature—Studies Using Trx2 Endothelium-Specific Transgenic Mice. Methods In Enzymology 2010, 474: 315-324. PMID: 20609919, DOI: 10.1016/s0076-6879(10)74019-2.Peer-Reviewed Original ResearchConceptsReactive oxygen speciesCellular reactive oxygen speciesMitochondrial antioxidant systemVivo functional assaysTRX2 geneRedox signalingTransgenic miceRedox genesThioredoxin 2Functional analysisHuman diseasesFunctional assaysAntioxidant systemOxygen speciesGenesCritical roleEndothelial cell culturesCell culturesPrimary lineTrx2TransgenesisThioredoxinMitochondriaSignalingSpeciesStabilization of VEGFR2 Signaling by Cerebral Cavernous Malformation 3 Is Critical for Vascular Development
He Y, Zhang H, Yu L, Gunel M, Boggon TJ, Chen H, Min W. Stabilization of VEGFR2 Signaling by Cerebral Cavernous Malformation 3 Is Critical for Vascular Development. Science Signaling 2010, 3: ra26. PMID: 20371769, PMCID: PMC3052863, DOI: 10.1126/scisignal.2000722.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCardiovascular SystemEndothelial CellsFluorescent Antibody Technique, IndirectGene DeletionGene Expression ProfilingGene Knockdown TechniquesHematopoiesisHumansImmunoblottingImmunohistochemistryImmunoprecipitationMiceReverse Transcriptase Polymerase Chain ReactionSignal TransductionVascular Endothelial Growth Factor Receptor-2ConceptsCarboxyl-terminal domainVascular endothelial growth factor receptor 2Vascular developmentHuman vascular malformationsCerebral cavernous malformation 3Early embryonic stagesCerebral cavernous malformationsEndothelial cell-specific deletionApoptotic stimuliCell-specific deletionVivo functionEmbryonic angiogenesisEndothelial growth factor receptor 2Unknown functionVEGF stimulationVEGFR2 signalingEmbryonic stagesMessenger RNASmooth muscle cellsGrowth factor receptor 2DeletionCCM3 genesFactor receptor 2Muscle cellsGenes
2009
DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis
Xie D, Gore C, Zhou J, Pong RC, Zhang H, Yu L, Vessella RL, Min W, Hsieh JT. DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 19878-19883. PMID: 19903888, PMCID: PMC2785260, DOI: 10.1073/pnas.0908458106.Peer-Reviewed Original ResearchConceptsDAB2IP proteinCell survivalDeath-signaling moleculePI3K-Akt activityPI3K-Akt activationMetastatic prostate cancer cellsPI3K-Akt pathwayCell cycle arrestASK1 activityScaffold proteinPotent growth inhibitorDeath signalsC2 domainSignal moleculesASK1 activationFunctional analysisCell homeostasisApoptotic defectsConstitutive activationJNK pathwayProstate cancer cellsASK1 pathwayPI3K-AktDAB2IP expressionCycle arrestJAK2 and SHP2 Reciprocally Regulate Tyrosine Phosphorylation and Stability of Proapoptotic Protein ASK1*
Yu L, Min W, He Y, Qin L, Zhang H, Bennett AM, Chen H. JAK2 and SHP2 Reciprocally Regulate Tyrosine Phosphorylation and Stability of Proapoptotic Protein ASK1*. Journal Of Biological Chemistry 2009, 284: 13481-13488. PMID: 19287004, PMCID: PMC2679448, DOI: 10.1074/jbc.m809740200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell LineEndothelial CellsEnzyme StabilityHumansInterferon-gammaJanus Kinase 2MAP Kinase Kinase Kinase 5MiceMice, KnockoutMultienzyme ComplexesMutationPhosphorylationProtein Tyrosine Phosphatase, Non-Receptor Type 11Signal TransductionSuppressor of Cytokine Signaling 1 ProteinSuppressor of Cytokine Signaling ProteinsTumor Necrosis Factor-alphaConceptsTyrosine phosphorylationSubstrate-trapping mutantProtein tyrosine phosphatase 2Phosphatase-inactive mutantProteasomal inhibitor MG132ASK1-JNK signalingEndothelial cellsJAK2-specific inhibitorIFN-gamma-induced tyrosine phosphorylationASK1 degradationASK1 dephosphorylationInactive mutantMouse endothelial cellsASK1 phosphorylationPhosphatase 2Inhibitor MG132SHP2Wild typeASK1DephosphorylationMutantsPhosphorylationEnhanced associationJAK2EC apoptosisEndothelial-Specific Expression of Mitochondrial Thioredoxin Promotes Ischemia-Mediated Arteriogenesis and Angiogenesis
Dai S, He Y, Zhang H, Yu L, Wan T, Xu Z, Jones D, Chen H, Min W. Endothelial-Specific Expression of Mitochondrial Thioredoxin Promotes Ischemia-Mediated Arteriogenesis and Angiogenesis. Arteriosclerosis Thrombosis And Vascular Biology 2009, 29: 495-502. PMID: 19150880, PMCID: PMC2734510, DOI: 10.1161/atvbaha.108.180349.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisArteriesBlood Flow VelocityCell MovementDisease Models, AnimalEndothelial CellsHindlimbIschemiaJNK Mitogen-Activated Protein KinasesMaleMAP Kinase Kinase Kinase 5MiceMice, TransgenicMitochondriaMuscle, SkeletalNeovascularization, PhysiologicNitric OxideOxidative StressReactive Oxygen SpeciesRegional Blood FlowSignal TransductionThioredoxinsTime FactorsConceptsEndothelial cellsFlow recoveryFemoral artery ligation modelIschemia-mediated arteriogenesisIschemic reserve capacityLimb perfusion recoveryENOS-deficient miceENOS-KO miceNitric oxide bioavailabilityIschemia-induced angiogenesisEC apoptosisArtery ligation modelEC survivalENOS deletionNontransgenic littermatesStress-induced activationLigation modelPerfusion recoveryLower limbsUpper limbEndothelial-specific expressionSevere impairmentMajor antioxidant proteinsIschemiaMice
2008
AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice
Zhang H, He Y, Dai S, Xu Z, Luo Y, Wan T, Luo D, Jones D, Tang S, Chen H, Sessa WC, Min W. AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice. Journal Of Clinical Investigation 2008, 118: 3904-3916. PMID: 19033661, PMCID: PMC2575835, DOI: 10.1172/jci36168.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell MovementCorneal NeovascularizationDisease Models, AnimalEndothelial CellsHumansInflammationMiceMice, KnockoutNeovascularization, PathologicOrgan SpecificityPhosphatidylinositol 3-KinasesRas GTPase-Activating ProteinsSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2ConceptsASK1-interacting protein-1Inflammatory angiogenesisKO miceEndogenous inhibitorInhibition of VEGFR2PI3K p85Retina neovascularizationAdaptive angiogenesisVEGF-VEGFR2 signalingRetinal angiogenesisEC migrationMiceVascular ECsVEGF responseAngiogenesisProtein 1EC apoptosisVEGFR2Late phaseVEGFMechanistic dataVascular developmentAIP1 functionsK-complexesInhibitors