2016
Rac2 Modulates Atherosclerotic Calcification by Regulating Macrophage Interleukin-1&bgr; Production
Ceneri N, Zhao L, Young BD, Healy A, Coskun S, Vasavada H, Yarovinsky TO, Ike K, Pardi R, Qin L, Qin L, Tellides G, Hirschi K, Meadows J, Soufer R, Chun HJ, Sadeghi M, Bender JR, Morrison AR. Rac2 Modulates Atherosclerotic Calcification by Regulating Macrophage Interleukin-1&bgr; Production. Arteriosclerosis Thrombosis And Vascular Biology 2016, 37: 328-340. PMID: 27834690, PMCID: PMC5269510, DOI: 10.1161/atvbaha.116.308507.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaAortic DiseasesApolipoproteins EAtherosclerosisCells, CulturedCoronary Artery DiseaseCoronary VesselsFemaleGenetic Predisposition to DiseaseHumansInflammation MediatorsInterleukin 1 Receptor Antagonist ProteinInterleukin-1betaMacrophagesMaleMice, Inbred C57BLMice, KnockoutMuscle, Smooth, VascularMyocytes, Smooth MuscleNeuropeptidesPhenotypePlaque, AtheroscleroticPrognosisRac GTP-Binding ProteinsRac1 GTP-Binding ProteinSignal TransductionTransfectionUp-RegulationVascular CalcificationConceptsCoronary calcium burdenIL-1β expressionCalcium burdenSerum IL-1β levelsElevated IL-1βIL-1β levelsCoronary artery diseaseInterleukin-1β expressionCalcified coronary arteryCardiovascular deathCardiovascular eventsArtery diseaseIndependent predictorsClinical outcomesVascular calcificationCoronary arteryIL-1βPlaque calciumAtherosclerotic calcificationExperimental atherogenesisInflammatory regulatorsMacrophage interleukinAtherosclerotic plaquesTherapeutic targetProgressive calcification
2003
Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
Li L, Haynes MP, Bender JR. Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 4807-4812. PMID: 12682286, PMCID: PMC153637, DOI: 10.1073/pnas.0831079100.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBase SequenceCell LineCell MembraneCOS CellsEndothelium, VascularEstrogen Receptor alphaGenes, ReporterGenetic VariationHumansNitric Oxide SynthaseNitric Oxide Synthase Type IIIProtein Processing, Post-TranslationalReceptors, EstrogenRecombinant ProteinsRNA, MessengerSubcellular FractionsTranscriptional ActivationTransfectionConceptsPlasma membranePalmitoylation-dependent mannerPlasma membrane localizationInhibition of palmitoylationFull-length ER alphaReporter gene transactivationCOS-7 cellsEndothelial cell proteinsMembrane localizationAlternative splicingEstrogen receptor α variantsOestrogen receptor-alpha variantsN-terminusHuman endothelial cellsCell proteinsER46Synthase pathwayAcid labelingHy926 cellsNonendothelial cellsENOS activationENOS phosphorylationCellsEndothelial cellsMembrane
2002
Src Kinase Mediates Phosphatidylinositol 3-Kinase/Akt-dependent Rapid Endothelial Nitric-oxide Synthase Activation by Estrogen*
Haynes MP, Li L, Sinha D, Russell KS, Hisamoto K, Baron R, Collinge M, Sessa WC, Bender JR. Src Kinase Mediates Phosphatidylinositol 3-Kinase/Akt-dependent Rapid Endothelial Nitric-oxide Synthase Activation by Estrogen*. Journal Of Biological Chemistry 2002, 278: 2118-2123. PMID: 12431978, DOI: 10.1074/jbc.m210828200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBlotting, WesternCell LineCells, CulturedElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumEndothelium, VascularEnzyme ActivationEnzyme InhibitorsEstrogensHumansMiceMutationNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IINitric Oxide Synthase Type IIIPhosphatidylinositol 3-KinasesPhosphorylationPrecipitin TestsProtein BindingProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptors, EstrogenSignal TransductionSrc-Family KinasesTime FactorsTransfectionTyrosineConceptsC-SrcPI3-kinaseAkt phosphorylationSrc kinaseUpstream regulatorKinase-dead c-SrcC-Src associationActive c-SrcC-Src phosphorylationMurine embryonic fibroblastsBasal Akt phosphorylationC-Src expressionCritical upstream regulatorEndothelial nitric oxide synthaseSrc familyActive AktEmbryonic fibroblastsComplex formation resultsEndothelial cellsHuman endothelial cellsAkt activationPhosphorylationKinaseAktPhosphatidylinositol
2000
Human vascular endothelial cells contain membrane binding sites for estradiol, which mediate rapid intracellular signaling
Russell K, Haynes M, Sinha D, Clerisme E, Bender J. Human vascular endothelial cells contain membrane binding sites for estradiol, which mediate rapid intracellular signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 5930-5935. PMID: 10823945, PMCID: PMC18536, DOI: 10.1073/pnas.97.11.5930.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalCell LineCell Membrane PermeabilityCells, CulturedCyclic GMPEndothelium, VascularEstradiolFlow CytometryHumansMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNitric OxideReceptors, EstrogenRecombinant Fusion ProteinsSerum Albumin, BovineSignal TransductionTime FactorsTransfectionConceptsHuman endothelial cellsEstrogen receptorEndothelial cellsMitogen-activated protein kinaseER antagonist ICIHuman vascular endothelial cellsMembrane estrogen receptorsMembrane-impermeant formVascular endothelial cellsRapid intracellularRapid nongenomic responsesAntagonist ICIVascular functionE2 treatmentAcute effectsERalpha antibodyCGMP productionCardiovascular systemNongenomic responsesCytometric analysisEstrogen inducesGuanylate cyclaseRapid effectsNO releaseEarly effects
1999
A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2
Liu Y, Pan J, Zhang C, Fan W, Collinge M, Bender J, Weissman S. A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 4313-4318. PMID: 10200259, PMCID: PMC16329, DOI: 10.1073/pnas.96.8.4313.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsB-LymphocytesBase SequenceCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsCell LineChromosomes, Artificial, YeastCOS CellsGenes, MHC Class IHL-60 CellsHumansJurkat CellsMad2 ProteinsMolecular Sequence DataPolymerase Chain ReactionRepressor ProteinsSequence AlignmentSequence Homology, Amino AcidT-LymphocytesTransfectionTumor Cells, CulturedUbiquitinsConceptsSpindle assembly checkpoint protein Mad2Two-hybrid screeningCheckpoint protein Mad2Ubiquitin-like proteinHuman MHC class I regionCell cycle checkpointsMHC class I regionSpindle assemblyI geneProtein stabilityCell developmentDendritic cell developmentClass I regionImmunoprecipitation studiesCell growthMad2Gamma-interferon inductionProteinProtein expressionFAT10I regionCellsLymphoblastoid linesAnaphaseTranscriptionHuman single-chain Fv immunoconjugates targeted to a melanoma-associated chondroitin sulfate proteoglycan mediate specific lysis of human melanoma cells by natural killer cells and complement
Wang B, Chen Y, Ayalon O, Bender J, Garen A. Human single-chain Fv immunoconjugates targeted to a melanoma-associated chondroitin sulfate proteoglycan mediate specific lysis of human melanoma cells by natural killer cells and complement. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 1627-1632. PMID: 9990075, PMCID: PMC15540, DOI: 10.1073/pnas.96.4.1627.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell LineCells, CulturedCHO CellsChondroitin Sulfate ProteoglycansChromatography, LiquidComplement System ProteinsCricetinaeCytotoxicity, ImmunologicDrosophila melanogasterEndothelium, VascularHumansImmunoconjugatesImmunoglobulin FragmentsImmunoglobulin GImmunoglobulin Variable RegionKiller Cells, NaturalMass SpectrometryMelanomaMolecular Sequence DataRestriction MappingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTransfectionTumor Cells, CulturedConceptsHuman melanoma cellsNatural killer cellsNK cellsMelanoma cellsKiller cellsChondroitin sulfate proteoglycanCytolytic responsesMost human melanoma cellsTumor cellsVaccinated melanoma patientsCultured human melanoma cellsCytolytic immune responseFusion phage librarySpecific cytolytic responseMelanoma-associated chondroitin sulfate proteoglycanHuman single-chain FvSulfate proteoglycanMelanoma patientsSpecific lysisImmune responseMelanoma tumorsComplement cascadeTargeted tumor cellsImmunoconjugatesHuman IgG1
1998
Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis
Ayalon O, Hughes E, Cresswell P, Lee J, O’Donnell L, Pardi R, Bender J. Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2435-2440. PMID: 9482903, PMCID: PMC19366, DOI: 10.1073/pnas.95.5.2435.Peer-Reviewed Original ResearchConceptsMHC IInduction of transportersEndothelial cellsNK-resistant cell linesNatural killer-mediated lysisMajor histocompatibility complex INK inhibitory receptorsNK effector cellsPretreatment of ECB-lymphoblastoid cell linesEC sensitivityDermal microvascular endothelial cellsMicrovascular endothelial cellsCell linesHuman umbilical vein endothelial cellsExpression/functionUmbilical vein endothelial cellsAdenoviral-mediated transductionVascular vulnerabilityVein endothelial cellsNK assaysEffector cellsEndothelial activationInhibitory receptorsDeficient targets
1996
Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase.
Rovere P, Inverardi L, Bender J, Pardi R. Feedback modulation of ligand-engaged alpha L/beta 2 leukocyte integrin (LFA-1) by cyclic AMP-dependent protein kinase. The Journal Of Immunology 1996, 156: 2273-9. PMID: 8690918, DOI: 10.4049/jimmunol.156.6.2273.Peer-Reviewed Original ResearchConceptsProtein kinase CAdhesion receptorsKinase CCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCytoskeletal anchoring proteinsIntegrin-dependent activationCAMP-dependent kinase activationIntracellular cAMP elevationCAMP elevationHeterologous cell linesLeukocyte integrinsAnchoring proteinsRegulated processProtein kinaseAdenylyl cyclase isoformsMolecular basisKinase activationIntercellular adhesionF-actinCell deadhesionHuman intercellular adhesion molecule-1LFA-1 receptorsDependent adhesionShort-term regulation
1995
Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association.
Pardi R, Bossi G, Inverardi L, Rovida E, Bender J. Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. The Journal Of Immunology 1995, 155: 1252-63. PMID: 7636193, DOI: 10.4049/jimmunol.155.3.1252.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAmino Acid SequenceAnimalsCell CompartmentationCell Line, TransformedChlorocebus aethiopsCytoskeletonEndoplasmic ReticulumLymphocyte Function-Associated Antigen-1Molecular Sequence DataProtein ConformationProtein MultimerizationProtein Structure, TertiaryRecombinant Fusion ProteinsSequence DeletionT-LymphocytesTetradecanoylphorbol AcetateTransfectionConceptsAlpha L beta 2Cytoplasmic domainEndoplasmic reticulum retentionCytoskeletal associationBeta subunitAlpha L subunitAlpha beta complexFunction of integrinsBeta 2GFFKR motifAdherent cellsDeletion mutantsSubstitution mutantsEctopic expressionIntegrin alphaPlasma membraneHeterodimer formationConserved regionsAdhesion receptorsBeta complexCytoplasmic truncationRegulated functionsL subunitsStructural determinantsAlpha LContact-dependent endothelial class II HLA gene activation induced by NK cells is mediated by IFN-gamma-dependent and -independent mechanisms.
Watson C, Petzelbauer P, Zhou J, Pardi R, Bender J. Contact-dependent endothelial class II HLA gene activation induced by NK cells is mediated by IFN-gamma-dependent and -independent mechanisms. The Journal Of Immunology 1995, 154: 3222-33. PMID: 7897208, DOI: 10.4049/jimmunol.154.7.3222.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, Differentiation, B-LymphocyteBase SequenceBlotting, NorthernCell AdhesionCells, CulturedEndothelium, VascularGene Expression RegulationHistocompatibility Antigens Class IIHLA-DR AntigensHumansInterferon-gammaKiller Cells, NaturalMolecular Sequence DataOrgan Culture TechniquesPromoter Regions, GeneticSkinTranscriptional ActivationTransfectionConceptsNK cellsNK lymphocytesEndothelial cellsIFN-gammaMHC class II AgIFN-gamma dependenceT cell recruitmentClass II HLAClass II expressionHLA-DR inductionClass II AgT cell proliferationMembrane expressionTrans-well experimentsReceptor AbEndothelial activationImmune amplificationCell recruitmentMicrovessel endotheliumHuman IFN-gammaPromoter constructsClonal expansionCoculture modelCell proliferationChinese hamster ovary cells
1994
Epican, a heparan/chondroitin sulfate proteoglycan form of CD44, mediates cell-cell adhesion
Milstone L, Hough-Monroe L, Kugelman L, Bender J, Haggerty J. Epican, a heparan/chondroitin sulfate proteoglycan form of CD44, mediates cell-cell adhesion. Journal Of Cell Science 1994, 107: 3183-3190. PMID: 7699015, DOI: 10.1242/jcs.107.11.3183.Peer-Reviewed Original Research