2018
Regulation of Yes-Associated Protein by Laminar Flow
Chitragari G, Shalaby SY, Sumpio BJ, Kurita J, Sumpio BE. Regulation of Yes-Associated Protein by Laminar Flow. Annals Of Vascular Surgery 2018, 52: 183-191. PMID: 29758328, DOI: 10.1016/j.avsg.2018.03.002.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCell ShapeCells, CulturedCytoskeletonDown-RegulationHuman Umbilical Vein Endothelial CellsHumansMechanotransduction, CellularPhosphoproteinsPhosphorylationProteolysisPulsatile FlowRegional Blood FlowStress, MechanicalTime FactorsTranscription FactorsYAP-Signaling ProteinsConceptsHuman umbilical vein endothelial cellsTotal YAPExposure of HUVECsRelease of mediatorsYAP levelsSignificant decreaseUbiquitin-proteasome system inhibitorsUmbilical vein endothelial cellsEndothelial cell proliferationVein endothelial cellsVascular healthSystem inhibitorsYes-Associated ProteinDisease modulationIntimal hyperplasiaDisturbed flowEndothelial cellsBlood vesselsDisease statesPotential targetCell proliferationProteasome-independent mechanismExposureKey regulatorPYAP
2013
PECAM-1 phosphorylation and tissue factor expression in HUVECs exposed to uniform and disturbed pulsatile flow and chemical stimuli
Moriguchi T, Sumpio BE. PECAM-1 phosphorylation and tissue factor expression in HUVECs exposed to uniform and disturbed pulsatile flow and chemical stimuli. Journal Of Vascular Surgery 2013, 61: 481-488. PMID: 24342062, DOI: 10.1016/j.jvs.2013.09.059.Peer-Reviewed Original Research
2011
The role of mechanical forces and adenosine in the regulation of intestinal enterochromaffin cell serotonin secretion
Chin A, Svejda B, Gustafsson B, Granlund A, Sandvik A, Timberlake A, Sumpio B, Pfragner R, Modlin I, Kidd M. The role of mechanical forces and adenosine in the regulation of intestinal enterochromaffin cell serotonin secretion. AJP Gastrointestinal And Liver Physiology 2011, 302: g397-g405. PMID: 22038827, PMCID: PMC3287403, DOI: 10.1152/ajpgi.00087.2011.Peer-Reviewed Original ResearchMeSH KeywordsAcetamidesAdenosineAdenosine A2 Receptor AgonistsAdenosine A2 Receptor AntagonistsAdenosine-5'-(N-ethylcarboxamide)AdultAgedCell Line, TumorCells, CulturedColonCrohn DiseaseCyclic AMPCyclic AMP Response Element-Binding ProteinCyclic AMP-Dependent Protein KinasesEnterochromaffin CellsFemaleGene ExpressionHumansMaleMAP Kinase Kinase 1MAP Kinase Signaling SystemMechanotransduction, CellularMiddle AgedPhosphorylationProto-Oncogene Proteins c-aktPurinesReceptor, Adenosine A1Receptor, Adenosine A2AReceptor, Adenosine A2BReceptor, Adenosine A3SerotoninSignal TransductionStress, MechanicalTryptophan HydroxylaseVesicular Monoamine Transport ProteinsConceptsInflammatory bowel diseaseEC cellsCell functionEC cell functionMechanical stimulationDevelopment of agentsSecrete serotoninBowel diseaseIntracellular cAMP levelsGut motilityEnterochromaffin cellsAdenosine responsivenessReceptor agonistReceptor expressionHuman EC cellsSerotonin secretionAdenosine receptorsMRS1754CAMP productionSecretionCAMP levelsNECANeoplasiaMechanosensory cellsDiseaseLaminar shear, but not orbital shear, has a synergistic effect with thrombin stimulation on tissue factor expression in human umbilical vein endothelial cells
Rochier A, Nixon A, Yamashita N, Abe R, Abe R, Madri JA, Sumpio BE. Laminar shear, but not orbital shear, has a synergistic effect with thrombin stimulation on tissue factor expression in human umbilical vein endothelial cells. Journal Of Vascular Surgery 2011, 54: 480-488. PMID: 21367569, DOI: 10.1016/j.jvs.2011.01.002.Peer-Reviewed Original ResearchAnalysis of VarianceBlotting, WesternCell Culture TechniquesCells, CulturedEndothelial CellsEnzyme ActivationHumansMechanotransduction, CellularMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3P38 Mitogen-Activated Protein KinasesPhosphorylationProtein Kinase InhibitorsRNA, MessengerStress, MechanicalThrombinThromboplastinTime FactorsUp-Regulation
2008
Thrombospondin-1-Induced Migration Is Functionally Dependent Upon Focal Adhesion Kinase
Wang XJ, Maier K, Fuse S, Willis AI, Olson E, Nesselroth S, Sumpio BE, Gahtan V. Thrombospondin-1-Induced Migration Is Functionally Dependent Upon Focal Adhesion Kinase. Vascular And Endovascular Surgery 2008, 42: 256-262. PMID: 18319354, DOI: 10.1177/1538574408314440.Peer-Reviewed Original ResearchDifferential Effects of Shear Stress and Cyclic Strain on Sp1 Phosphorylation by Protein Kinase Cζ Modulates Membrane Type 1–Matrix Metalloproteinase in Endothelial Cells
Kim JI, Cordova AC, Hirayama Y, Madri JA, Sumpio BE. Differential Effects of Shear Stress and Cyclic Strain on Sp1 Phosphorylation by Protein Kinase Cζ Modulates Membrane Type 1–Matrix Metalloproteinase in Endothelial Cells. Endothelium 2008, 15: 33-42. PMID: 18568943, PMCID: PMC2644408, DOI: 10.1080/10623320802092260.Peer-Reviewed Original ResearchConceptsSp1 phosphorylationMT1-MMP expressionPromoter sitesPKCzeta inhibitorProtein kinase CzetaAffinity of Sp1Egr-1 bindingProtein kinase CζExtracellular matrix remodelingEndothelial cell migrationSp1Cell migrationPhosphorylationMatrix remodelingProtein expressionCyclic strainExpressionMembrane typeEndothelial cellsKey roleCzetaInhibitorsCζMetalloproteinaseAffinity
2007
Direct comparison of endothelial cell and smooth muscle cell response to supercooling and rewarming
Yiu WK, Cheng SW, Sumpio BE. Direct comparison of endothelial cell and smooth muscle cell response to supercooling and rewarming. Journal Of Vascular Surgery 2007, 46: 557-564.e2. PMID: 17826245, DOI: 10.1016/j.jvs.2007.04.072.Peer-Reviewed Original ResearchAnimalsAorta, ThoracicApoptosisBlotting, WesternCattleCell ProliferationCells, CulturedCryopreservationDensitometryEndothelial CellsEnzyme ActivationIn Situ Nick-End LabelingMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Muscle, Smooth, VascularPhosphorylationProto-Oncogene Proteins c-aktRewarmingPhosphatase PTEN is inactivated in bovine aortic endothelial cells exposed to cyclic strain
Hoshino Y, Nishimura K, Sumpio BE. Phosphatase PTEN is inactivated in bovine aortic endothelial cells exposed to cyclic strain. Journal Of Cellular Biochemistry 2007, 100: 515-526. PMID: 16927376, DOI: 10.1002/jcb.21085.Peer-Reviewed Original ResearchConceptsCasein kinase 2Transfection of ECsPTEN plasmidVascular cell morphologyEndothelial cellsPI3K activitySuppression of apoptosisPI3K-Akt pathwayLipid phosphataseMaximal activityPhosphatase PTENPhospho-PTENPTEN activityBovine aortic endothelial cellsIntracellular phosphatidylinositolUpstream regulatorAkt activityKinase 2Phospho-AKT activityK activityTime-dependent mannerAortic endothelial cellsCell morphologyCell proliferationPTENRole of Ligand-Specific Integrins in Endothelial Cell Alignment and Elongation Induced by Cyclic Strain
Hirayama Y, Sumpio BE. Role of Ligand-Specific Integrins in Endothelial Cell Alignment and Elongation Induced by Cyclic Strain. Endothelium 2007, 14: 275-283. PMID: 18080865, DOI: 10.1080/10623320701746248.Peer-Reviewed Original ResearchConceptsEndothelial cellsP38 MAPKAnti-alpha2 integrin antibodyMorphological changesP38 mitogen-activated protein kinase (MAPK) pathwayCycles/minIntegrin-blocking antibodiesP38 MAPK pathwayMitogen-activated protein kinase pathwayAlpha 5Integrin antibodyProtein kinase pathwayMAPK pathwayAntibodiesKinase pathwayMAPKMultiple biological processesActivationIntegrinsCritical roleCyclic strainPathway
2006
Vascular Smooth Muscle Cell Apoptosis Induced by “Supercooling” and Rewarming
Yiu WK, Cheng SW, Sumpio BE. Vascular Smooth Muscle Cell Apoptosis Induced by “Supercooling” and Rewarming. Journal Of Vascular And Interventional Radiology 2006, 17: 1971-1977. PMID: 17185696, DOI: 10.1097/01.rvi.0000244868.65867.fb.Peer-Reviewed Original ResearchPECAM-1 Affects GSK-3β-Mediated β-Catenin Phosphorylation and Degradation
Biswas P, Canosa S, Schoenfeld D, Schoenfeld J, Li P, Cheas LC, Zhang J, Cordova A, Sumpio B, Madri JA. PECAM-1 Affects GSK-3β-Mediated β-Catenin Phosphorylation and Degradation. American Journal Of Pathology 2006, 169: 314-324. PMID: 16816383, PMCID: PMC1698776, DOI: 10.2353/ajpath.2006.051112.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBlotting, WesternCapillary PermeabilityCells, CulturedEndothelial CellsFluorescent Antibody TechniqueGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHistamineHistamine AgentsHumansMiceModels, BiologicalPhosphatidylinositol 3-KinasesPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Proto-Oncogene Proteins c-aktReceptors, HistamineSignal TransductionConceptsAdherens junctionsSerine phosphorylationSrc homology 2 domainBeta-catenin expression levelsAdherens junction componentsSerine phosphorylation levelEndothelial cellsΒ-catenin phosphorylationPECAM-1Cell biological responsesCytoplasmic domainSHP-2Proteosomal degradationGSK-3betaDynamic regulatorJunction componentsPhosphorylation levelsPhosphorylationEndothelial cell adhesion molecule-1Expression levelsGSK-3βBiological responsesEndothelial barrier permeabilityMice exhibitCell adhesion molecule-1Role of AKT in cyclic strain-induced endothelial cell proliferation and survival
Nishimura K, Li W, Hoshino Y, Kadohama T, Asada H, Ohgi S, Sumpio BE. Role of AKT in cyclic strain-induced endothelial cell proliferation and survival. American Journal Of Physiology - Cell Physiology 2006, 290: c812-c821. PMID: 16469863, DOI: 10.1152/ajpcell.00347.2005.Peer-Reviewed Original ResearchConceptsEndothelial cellsCycles/minRole of AktEC proliferationCultured bovine aortic endothelial cellsSurvival of ECsAortic endothelial cellsApoptotic endothelial cellsGSK-3betaBovine aortic endothelial cellsEndothelial cell proliferationFrequency of strainsPositive cellsGlycogen synthase kinaseKinase-dead AktCell proliferationCaspase-3AktSurvivalCell numberSynthase kinaseProliferationEarly phosphorylationBad phosphorylationNicotine enhances human vascular endothelial cell expression of ICAM-1 and VCAM-1 via protein kinase C, p38 mitogen-activated protein kinase, NF-κB, and AP-1
Ueno H, Pradhan S, Schlessel D, Hirasawa H, Sumpio BE. Nicotine enhances human vascular endothelial cell expression of ICAM-1 and VCAM-1 via protein kinase C, p38 mitogen-activated protein kinase, NF-κB, and AP-1. Cardiovascular Toxicology 2006, 6: 39-50. PMID: 16845181, DOI: 10.1385/ct:6:1:39.Peer-Reviewed Original ResearchConceptsHuman umbilical vein endothelial cellsICAM-1VCAM-1NF-κBAdhesion moleculesP38 mitogen-activated protein kinaseProtein kinase CMitogen-activated protein kinaseVascular cell adhesion moleculeEndothelial cellsExposure of HUVECsCellular adhesion molecule expressionAP-1Vascular endothelial cell expressionMajor risk factorEffects of nicotineEtiology of atherosclerosisP38 MAPKAdhesion molecule expressionIntercellular adhesion moleculeTranscription factor NF-κBCellular adhesion moleculesEndothelial cell expressionFactor NF-κBUmbilical vein endothelial cellsp38 Mitogen-Activated Protein Kinase Activation in Endothelial Cell Is Implicated in Cell Alignment and Elongation Induced by Fluid Shear Stress
Kadohama T, Akasaka N, Nishimura K, Hoshino Y, Sasajima T, Sumpio BE. p38 Mitogen-Activated Protein Kinase Activation in Endothelial Cell Is Implicated in Cell Alignment and Elongation Induced by Fluid Shear Stress. Endothelium 2006, 13: 43-50. PMID: 16885066, DOI: 10.1080/10623320600660219.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesAtherosclerosisBlood PressureBlood VesselsCattleCell PolarityCell ShapeCells, CulturedDose-Response Relationship, DrugEndothelial CellsEnzyme ActivationEnzyme InhibitorsHemodynamicsMAP Kinase Signaling SystemP38 Mitogen-Activated Protein KinasesPhosphorylationRegional Blood FlowStress, MechanicalTime FactorsConceptsStatic endothelial cellsFluid shear stressP38 MAPKP38 Mitogen-Activated Protein Kinase ActivationMitogen-Activated Protein Kinase ActivationEndothelial cellsProtein kinase activationP38 MAPK inhibitor SB-203580Inhibitor SB 203580Cell alignmentProtein kinaseBovine aortic endothelial cellsLaminar shear stressKinase activationSB 203580P38 mitogenCultured bovine aortic endothelial cellsEC elongationAortic endothelial cellsMAPKCellsElongationActivationMorphometric analysisKinase
2005
Differential responsiveness of early- and late-passage endothelial cells to shear stress
Kudo FA, Warycha B, Juran PJ, Asada H, Teso D, Aziz F, Frattini J, Sumpio BE, Nishibe T, Cha C, Dardik A. Differential responsiveness of early- and late-passage endothelial cells to shear stress. The American Journal Of Surgery 2005, 190: 763-769. PMID: 16226955, DOI: 10.1016/j.amjsurg.2005.07.017.Peer-Reviewed Original ResearchMeSH KeywordsAgingAnimalsAortaApoptosisBlotting, WesternCattleCell CountCell DivisionCell ProliferationCells, CulturedEndothelium, VascularIn Vitro TechniquesMuscle, Smooth, VascularPhosphorylationProliferating Cell Nuclear AntigenProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktShear StrengthStress, MechanicalTumor Suppressor Protein p53ConceptsLate passage endothelial cellsOrbital shear stressEarly passage cellsSmooth muscle cell migrationMuscle cell migrationEndothelial cellsSenescence modelAkt phosphorylationCell migrationProtein kinase B activationPassage cellsKinase B activationCell proliferationVascular disease increasesLate passage cellsBovine aortic endothelial cellsNuclear antigen reactivityAortic endothelial cellsEndothelial cell proliferationNeointimal hyperplasiaAntigen reactivityTotal AktBoyden chamberB activationWestern blottingSustained orbital shear stress stimulates smooth muscle cell proliferation via the extracellular signal-regulated protein kinase 1/2 pathway
Asada H, Paszkowiak J, Teso D, Alvi K, Thorisson A, Frattini JC, Kudo FA, Sumpio BE, Dardik A. Sustained orbital shear stress stimulates smooth muscle cell proliferation via the extracellular signal-regulated protein kinase 1/2 pathway. Journal Of Vascular Surgery 2005, 42: 772-780. PMID: 16242567, DOI: 10.1016/j.jvs.2005.05.046.Peer-Reviewed Original ResearchConceptsOrbital shear stressPresence of PD98059Synthetic phenotypeERK1/2 pathwayExtracellular signal-regulated proteinSMC proliferationSmooth muscle cell proliferationMuscle cell proliferationPathway inhibitor PD98059Cell proliferationExtracellular signal-regulated protein kinase 1/2 (ERK1/2) phosphorylationKinase 1/2 phosphorylationPresence of SB203580Bovine SMCsSMC phenotypeInhibitor PD98059Inhibitor SB203580Contractile phenotypePD98059Long-term culturePhenotypeCell nuclear antigenExpression of markersPathwaySB203580Negative Regulation of Monocyte Adhesion to Arterial Elastic Laminae by Signal Regulatory Protein α and Src Homology 2 Domain-containing Protein-Tyrosine Phosphatase-1*
Liu SQ, Alkema PK, Tieché C, Tefft BJ, Liu DZ, Li YC, Sumpio BE, Caprini JA, Paniagua M. Negative Regulation of Monocyte Adhesion to Arterial Elastic Laminae by Signal Regulatory Protein α and Src Homology 2 Domain-containing Protein-Tyrosine Phosphatase-1*. Journal Of Biological Chemistry 2005, 280: 39294-39301. PMID: 16159885, DOI: 10.1074/jbc.m503866200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArteriesCell AdhesionElastic TissueIn Vitro TechniquesIntracellular Signaling Peptides and ProteinsLeukocytesMonocytesPhosphorylationProtein Phosphatase 1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesRatsRats, Sprague-DawleyReceptors, Cell SurfaceRNA, Small InterferingConceptsSHP-1Arterial elastic laminaeSrc homology 2 domain-containing protein tyrosine phosphataseSIRP-alphaSrc homology 2 domain-containing protein tyrosine phosphatase 1Protein tyrosine phosphatase 1Protein tyrosine phosphataseSignal regulatory protein alphaSignal regulatory protein αRegulatory protein alphaExtracellular matrix constituentsMonocyte adhesionArterial morphogenesisPhosphatase 1Regulatory protein αNegative regulationProtein alphaProtein αImportant functionsInduced activationDegradation peptidesInhibitory effectElasticity of arteriesAdhesionMatrix constituentsThe role of STAT-3 in the mediation of smooth muscle cell response to cyclic strain
Kakisis JD, Pradhan S, Cordova A, Liapis CD, Sumpio BE. The role of STAT-3 in the mediation of smooth muscle cell response to cyclic strain. The International Journal Of Biochemistry & Cell Biology 2005, 37: 1396-1406. PMID: 15833272, DOI: 10.1016/j.biocel.2005.01.009.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCell ProliferationCells, CulturedDNA-Binding ProteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Myocytes, Smooth MusclePhosphorylationPyrazolesPyrimidinesRatsSerineSignal TransductionSrc-Family KinasesSTAT3 Transcription FactorStress, MechanicalTrans-ActivatorsTyrosineConceptsSerine phosphorylationTyrosine phosphorylationSmooth muscle cellsSTAT-3Vascular smooth muscle cellsSTAT-3 tyrosine phosphorylationSpecific inhibitorVascular cell morphologyExtracellular signal-regulated kinase 1/2Extracellular mechanical signalsSignal-regulated kinase 1/2Basal serine phosphorylationInhibition of SrcA7r5 smooth muscle cellsNegative feedback loopInhibition of ERK1/2Cells sensePhosphospecific antibodiesPhosphatidylinositol 3Signal transducerTranscription 3Kinase 2Kinase 1/2Smooth muscle cell responseBasal phosphorylationHomocysteine promotes p38-dependent chemotaxis in bovine aortic smooth muscle cells
Akasaka K, Akasaka N, Di Luozzo G, Sasajima T, Sumpio BE. Homocysteine promotes p38-dependent chemotaxis in bovine aortic smooth muscle cells. Journal Of Vascular Surgery 2005, 41: 517-522. PMID: 15838488, DOI: 10.1016/j.jvs.2004.12.043.Peer-Reviewed Original ResearchConceptsEffect of homocysteineMigration of SMCsLevels of homocysteineProgressive intimal thickeningAortic smooth muscle cellsSmooth muscle cell migrationBovine aortic smooth muscle cellsPotential therapeutic implicationsSmooth muscle cellsP38 activationExposure of SMCMuscle cell migrationSMC chemotaxisRisk factorsSelective blockadeIntimal thickeningTherapeutic implicationsP38-dependent pathwaySMC proliferationBoyden chamberChemotactic potentialMuscle cellsHomocysteineFetal bovine serumP38 inhibitorMAPKs (ERK½, p38) and AKT Can Be Phosphorylated by Shear Stress Independently of Platelet Endothelial Cell Adhesion Molecule-1 (CD31) in Vascular Endothelial Cells*
Sumpio BE, Yun S, Cordova AC, Haga M, Zhang J, Koh Y, Madri JA. MAPKs (ERK½, p38) and AKT Can Be Phosphorylated by Shear Stress Independently of Platelet Endothelial Cell Adhesion Molecule-1 (CD31) in Vascular Endothelial Cells*. Journal Of Biological Chemistry 2005, 280: 11185-11191. PMID: 15668248, DOI: 10.1074/jbc.m414631200.Peer-Reviewed Original ResearchAnimalsCattleCell CommunicationEndothelial CellsEnzyme ActivationHumansMechanoreceptorsMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3P38 Mitogen-Activated Protein KinasesPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktStress, MechanicalTyrosine