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 cellsDisease
2009
Lovastatin Inhibits Thrombospondin-1-Induced Smooth Muscle Cell Chemotaxis1
Esemuede N, Lee T, Maier KG, Sumpio BE, Gahtan V. Lovastatin Inhibits Thrombospondin-1-Induced Smooth Muscle Cell Chemotaxis1. Journal Of Surgical Research 2009, 168: 149-154. PMID: 20338582, DOI: 10.1016/j.jss.2009.11.728.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell ProliferationCells, CulturedChemotaxisDose-Response Relationship, DrugHydroxymethylglutaryl-CoA Reductase InhibitorsLovastatinMevalonic AcidModels, AnimalMonomeric GTP-Binding ProteinsMuscle, Smooth, VascularRas ProteinsSignal TransductionThrombospondin 1Tunica IntimaTunica MediaConceptsTSP-1-induced chemotaxisGeranylgeranyl transferase inhibitorSerum-free mediumThrombospondin-1HMG-CoA reductase inhibitorsVascular smooth muscle cell migrationSmooth muscle cell migrationTransferase inhibitorsEffect of lovastatinG proteinsMuscle cell migrationRas activationRho-kinase inhibitorCell migrationPost-hoc testingFarnesyl transferase inhibitorsCholesterol loweringLovastatin doseVascular restenosisIntimal hyperplasiaBoyden chamberPleiotropic propertiesReductase inhibitorsWestern blotInhibition of Ras
2007
Effect of different frequencies of tensile strain on human dermal fibroblast proliferation and survival
Nishimura K, Blume P, Ohgi S, Sumpio BE. Effect of different frequencies of tensile strain on human dermal fibroblast proliferation and survival. Wound Repair And Regeneration 2007, 15: 646-656. PMID: 17971010, DOI: 10.1111/j.1524-475x.2007.00295.x.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseP38 mitogen-activated protein kinaseMAPK/ERK kinaseExtracellular signal-regulated kinaseDominant-negative AktHuman dermal fibroblastsSignal-regulated kinaseCell numberERK kinaseProtein kinaseTransduction pathwaysDermal fibroblastsRelevant transduction pathwaysRelevant signal pathwaysDermal fibroblast proliferationHuman dermal fibroblast proliferationCultured human dermal fibroblastsSurvival of fibroblastsSignal pathwayKinaseNecrotic fibroblastsDNA synthesisCell proliferationAktTransferase-mediated dUTP nick-end labeling staining
2006
PECAM-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-1
2005
Sustained 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 markersPathwaySB203580The 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 phosphorylationShear stress-stimulated endothelial cells induce smooth muscle cell chemotaxis via platelet-derived growth factor-BB and interleukin-1α
Dardik A, Yamashita A, Aziz F, Asada H, Sumpio BE. Shear stress-stimulated endothelial cells induce smooth muscle cell chemotaxis via platelet-derived growth factor-BB and interleukin-1α. Journal Of Vascular Surgery 2005, 41: 321-331. PMID: 15768016, DOI: 10.1016/j.jvs.2004.11.016.Peer-Reviewed Original ResearchConceptsSignal transduction pathwaysPlatelet-derived growth factorSMC chemotaxisCell signal transduction pathwaysMitogen-activated protein kinase pathwaySmooth muscle cell chemotaxisERK1/2 phosphorylationPDGF-BBExtracellular signal-regulated protein kinase 1/2Pathway inhibitor PD98059Protein kinase pathwayEndothelial cellsERK1/2 signal transduction pathwayProtein kinase 1/2Vascular smooth muscle cell migrationBovine aortic endothelial cellsKinase pathwayInhibitor PD98059Smooth muscle cell migrationHemodynamic forcesKinase 1/2Platelet-derived growthMuscle cell migrationWestern blot analysisTarget pathways
2004
Strain-induced vascular endothelial cell proliferation requires PI3K-dependent mTOR-4E-BP1 signal pathway
Li W, Sumpio BE. Strain-induced vascular endothelial cell proliferation requires PI3K-dependent mTOR-4E-BP1 signal pathway. AJP Heart And Circulatory Physiology 2004, 288: h1591-h1597. PMID: 15591103, DOI: 10.1152/ajpheart.00382.2004.Peer-Reviewed Original ResearchMeSH Keywords3-Phosphoinositide-Dependent Protein KinasesAndrostadienesAnimalsAntibiotics, AntineoplasticAortaCarrier ProteinsCattleCell DivisionCells, CulturedChromonesEndothelium, VascularEnzyme InhibitorsFlavonoidsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MorpholinesPhosphatidylinositol 3-KinasesPhosphodiesterase InhibitorsPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRibosomal Protein S6 KinasesSignal TransductionSirolimusTOR Serine-Threonine KinasesWortmanninConceptsVascular endothelial cell proliferationEndothelial cell proliferationStrain-induced activationSignal pathwayEC proliferationPD 98059Cell proliferationPI3K inhibitor wortmanninPI3K inhibitorsCycles/minExtracellular signal-regulated kinases 1Inhibitor PD 98059MTOR pathwaySignal-regulated kinases 1Bovine aortic ECsMammalian targetMTOR-4EK inhibitorsEukaryotic initiation factor 4EAortic ECsInitiation factor 4EMEK1 inhibitor PD 98059K activationProliferationRapamycinCell signalling in vascular cells exposed to cyclic strain: the emerging role of protein phosphatases
Lee T, Sumpio BE. Cell signalling in vascular cells exposed to cyclic strain: the emerging role of protein phosphatases. Biotechnology And Applied Biochemistry 2004, 39: 129-139. PMID: 15032733, DOI: 10.1042/ba20030104.Peer-Reviewed Original ResearchConceptsPhosphorylation stateSerine/threonine residuesProtein phosphatase type 2AAbnormal phosphorylation stateCritical cellular functionsPhosphorylation of tyrosineRole of phosphatasesVascular cellsRole of proteinsThreonine residuesCellular functionsProtein kinaseIntracellular proteinsCellular growthHuman diseasesProteinPhosphataseType 2AEndothelial cellsCellsCardiac hypertrophyKinasePhosphorylationHaemodynamic forcesRoleVascular Smooth Muscle Cell Migration: Current Research and Clinical Implications
Willis AI, Pierre-Paul D, Sumpio BE, Gahtan V. Vascular Smooth Muscle Cell Migration: Current Research and Clinical Implications. Vascular And Endovascular Surgery 2004, 38: 11-23. PMID: 14760473, DOI: 10.1177/153857440403800102.Peer-Reviewed Original ResearchConceptsVSMC migrationVascular smooth muscle cell migrationSmooth muscle cell migrationPotential therapeutic approachMuscle cell migrationDiabetes mellitusEndothelial injuryTherapeutic approachesIntimal hyperplasiaClinical implicationsMajor causeDevelopment of strategiesInjuryCell migrationMultiple stimuliHypertensionMellitusHyperlipidemiaMorbiditySmokingHyperplasiaMortality
2003
Oscillatory shear stress increases smooth muscle cell proliferation and akt phosphorylation
Haga M, Yamashita A, Paszkowiak J, Sumpio BE, Dardik A. Oscillatory shear stress increases smooth muscle cell proliferation and akt phosphorylation. Journal Of Vascular Surgery 2003, 37: 1277-1284. PMID: 12764276, DOI: 10.1016/s0741-5214(03)00329-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell Physiological PhenomenaDisease Models, AnimalHemodynamicsIn Vitro TechniquesMyocytes, Smooth MuscleOscillometryPhosphatidylinositol 3-KinasesPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktShear StrengthSignal TransductionStress, PhysiologicalVascular DiseasesConceptsSignal transduction pathwaysAkt phosphorylationTransduction pathwaysPI3K-Akt signal transduction pathwaySmooth muscle cell proliferationMuscle cell proliferationCell proliferationControl cellsOscillatory shear stressMaximal phosphorylationPI3K inhibitorsCell numberSurvival pathwaysAkt activationBovine aortic SMCSMC survivalInhibitor LY294002Akt pathwayPhosphorylationWestern blot techniqueControl survivalDNA synthesisK inhibitorsAortic SMCsPathwayShear Stress and Cyclic Strain May Suppress Apoptosis in Endothelial Cells by Different Pathways
Haga M, Chen A, Gortler D, Dardik A, Sumpio B. Shear Stress and Cyclic Strain May Suppress Apoptosis in Endothelial Cells by Different Pathways. Endothelium 2003, 10: 149-157. DOI: 10.1080/713715223.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBcl-Associated Death ProteinCarrier ProteinsCattleCells, CulturedCulture Media, Serum-FreeEndothelial CellsEnzyme InhibitorsHemodynamicsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionStress, MechanicalTranscription, GeneticConceptsPhosphorylation of AktEndothelial cellsPI3K inhibitionInhibition of apoptosisK inhibitionHemodynamic forcesAortic endothelial cellsBovine aortic endothelial cellsEffect of SSArterial levelsIntimal hyperplasiaDownstream target BadNormal endotheliumMaximal stimulationAkt phosphorylationLaminar shear stressApoptosisDownstream phosphorylationAktInhibitionCell survivalEC growthSerum withdrawalAlternate pathwayPhosphorylation of BadShear Stress and Cyclic Strain May Suppress Apoptosis in Endothelial Cells by Different Pathways
Haga M, Chen A, Gortler D, Dardik A, Sumpio B. Shear Stress and Cyclic Strain May Suppress Apoptosis in Endothelial Cells by Different Pathways. Endothelium 2003, 10: 149-157. PMID: 13129818, DOI: 10.1080/10623320390233463.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBcl-Associated Death ProteinCarrier ProteinsCattleCells, CulturedCulture Media, Serum-FreeEndothelial CellsEnzyme InhibitorsHemodynamicsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionStress, MechanicalTranscription, GeneticConceptsPhosphorylation of AktEndothelial cellsPI3K inhibitionInhibition of apoptosisK inhibitionHemodynamic forcesAortic endothelial cellsBovine aortic endothelial cellsEffect of SSArterial levelsIntimal hyperplasiaDownstream target BadNormal endotheliumMaximal stimulationAkt phosphorylationLaminar shear stressApoptosisDownstream phosphorylationAktInhibitionCell survivalEC growthSerum withdrawalAlternate pathwayPhosphorylation of Bad
2002
Parathyroid hormone effects on signaling pathways in endothelial cells vary with peptide concentration
Throckmorton D, Kurscheid-Reich D, Rosales OR, Rodriguez-Commes J, Lopez R, Sumpio B, Zhong Q, Ding K, McCarthy R, Barrett PQ, Isales CM. Parathyroid hormone effects on signaling pathways in endothelial cells vary with peptide concentration. Peptides 2002, 23: 79-85. PMID: 11814621, DOI: 10.1016/s0196-9781(01)00582-4.Peer-Reviewed Original ResearchConceptsParathyroid hormoneEndothelial cell lineVoltage-sensitive calcium channelsParathyroid hormone effectsSensitive calcium channelsUmbilical vein endothelial cell lineHuman umbilical vein endothelial cell lineCell linesProtein kinase CCalcium channelsHormone effectsEndothelial cellsFurther studiesPhospholipid turnoverPeptide concentrationPKC translocationSpecific effectsKinase CCell homogenatesPKC isoformsParticulate fraction
2001
The Integrin-Mediated Cyclic Strain-Induced Signaling Pathway in Vascular Endothelial Cells
Frangos S, Knox R, Yano Y, Chen E, Di Luozzo G, Chen A, Sumpio B. The Integrin-Mediated Cyclic Strain-Induced Signaling Pathway in Vascular Endothelial Cells. Endothelium 2001, 8: 1-10. PMID: 11409847, DOI: 10.3109/10623320109063153.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinase (MAPK) familyCytoplasmic protein kinaseProtein kinase familySignal transduction pathwaysFocal adhesion kinaseExtracellular matrix receptorsProcess of phosphorylationEndothelial cellsKinase familySignal transductionTranscription factorsAdhesion kinaseProtein kinaseTransduction pathwaysMatrix receptorsGene expressionTyrosine residuesSignaling pathwaysCyclic circumferential strainVascular endothelial cellsPathwayKinaseIntegrinsHemodynamic forcesVasculature results
2000
Endothelial cell response to different mechanical forces
Azuma N, Duzgun S, Ikeda M, Kito H, Akasaka N, Sasajima T, Sumpio B. Endothelial cell response to different mechanical forces. Journal Of Vascular Surgery 2000, 32: 789-794. PMID: 11013043, DOI: 10.1067/mva.2000.107989.Peer-Reviewed Original ResearchAnimalsAortaCattleCells, CulturedEndothelium, VascularEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesFocal AdhesionsHumansImmunoblottingJNK Mitogen-Activated Protein KinasesMechanoreceptorsMitogen-Activated Protein KinasesPhosphorylationProtein-Tyrosine KinasesSignal TransductionStress, MechanicalFunctional parathyroid hormone receptors are present in an umbilical vein endothelial cell line
Isales C, Sumpio B, Bollag R, Zhong Q, Ding K, Du W, Rodriguez-Commes J, Lopez R, Rosales O, Gasalla-Herraiz J, McCarthy R, Barrett P. Functional parathyroid hormone receptors are present in an umbilical vein endothelial cell line. AJP Endocrinology And Metabolism 2000, 279: e654-e662. PMID: 10950835, DOI: 10.1152/ajpendo.2000.279.3.e654.Peer-Reviewed Original ResearchMeSH KeywordsCalciumCell LineChromatography, High Pressure LiquidCyclic AMPEndothelin-1Endothelium, VascularFluorescent DyesFura-2Glyceraldehyde-3-Phosphate DehydrogenasesHumansInositol PhosphatesParathyroid HormoneReceptors, Parathyroid HormoneReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSignal TransductionThymidineUmbilical VeinsConceptsParathyroid hormoneUmbilical vein endothelial cell lineParathyroid hormone receptorEndothelial cell lineHormone receptorsVascular smooth muscle relaxationEndothelin-1 secretionSmooth muscle relaxationVascular smooth muscleHuman umbilical vein endothelial cell lineCell linesCellular cAMP contentPossible direct effectPeptide receptor mRNAEndothelium-derived cellsBlood pressureContinuous infusionMuscle relaxationIntracellular calciumSmooth muscleReceptor mRNAHormone exposureVascular endotheliumEndothelial cellsCAMP contentRole of Caveolin in Hemodynamic Force-Mediated Endothelial Changes
Fujioka K, Azuma N, Kito H, Gahtan V, Esato K, Sumpio B. Role of Caveolin in Hemodynamic Force-Mediated Endothelial Changes. Journal Of Surgical Research 2000, 92: 7-10. PMID: 10864474, DOI: 10.1006/jsre.2000.5838.Peer-Reviewed Original ResearchInhibition of phosphatidylinositol 3-kinase and protein kinase C attenuates extracellular matrix protein-induced vascular smooth muscle cell chemotaxis
Willis A, Fuse S, Wang X, Chen E, Tuszynski G, Sumpio B, Gahtan V. Inhibition of phosphatidylinositol 3-kinase and protein kinase C attenuates extracellular matrix protein-induced vascular smooth muscle cell chemotaxis. Journal Of Vascular Surgery 2000, 31: 1160-1167. PMID: 10842153, DOI: 10.1067/mva.2000.106489.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell CountCell DivisionCells, CulturedChemotaxisChromonesEnzyme InhibitorsExtracellular Matrix ProteinsFibronectinsHyperplasiaIndolesMaleimidesMorpholinesMuscle, Smooth, VascularPhosphoinositide-3 Kinase InhibitorsProtein Kinase CSignal TransductionStatistics as TopicThrombospondin 1Tunica IntimaVitronectinConceptsProtein kinase CVSMC migrationLY-294002Thrombospondin-1ECM proteinsKinase CSmooth muscle cell chemotaxisSerum-free mediumCellular signaling pathwaysInhibition of phosphatidylinositolVascular smooth muscle cell chemotaxisVascular smooth muscle cell migrationPI3K inhibitorsSmooth muscle cell migrationSignaling pathwaysMuscle cell migrationBisindolylmaleimide ICell migrationPKC inhibitorGF 109203XExtracellular matrix depositionTop wellsK inhibitorsAortic VSMCsCell chemotaxisMitogen‐activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions
Duzgun S, Rasque H, Kito H, Azuma N, Li W, Basson M, Gahtan V, Dudrick S, Sumpio B. Mitogen‐activated protein phosphorylation in endothelial cells exposed to hyperosmolar conditions. Journal Of Cellular Biochemistry 2000, 76: 567-571. PMID: 10653976, DOI: 10.1002/(sici)1097-4644(20000315)76:4<567::aid-jcb5>3.0.co;2-w.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCattleCell SizeEndothelium, VascularGlucoseJNK Mitogen-Activated Protein KinasesMannitolMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesOsmolar ConcentrationOsmotic PressureP38 Mitogen-Activated Protein KinasesPhosphorylationSignal TransductionSodium ChlorideTime FactorsUrea