2023
Organic Anion Transporting Polypeptide (OATP) 1B3 is a Significant Transporter for Hepatic Uptake of Conjugated Bile Acids in Humans
Pan Q, Zhu G, Xu Z, Zhu J, Ouyang J, Tong Y, Zhao N, Zhang X, Cheng Y, Zhang L, Tan Y, Li J, Zhang C, Chen W, Cai S, Boyer J, Chai J. Organic Anion Transporting Polypeptide (OATP) 1B3 is a Significant Transporter for Hepatic Uptake of Conjugated Bile Acids in Humans. Cellular And Molecular Gastroenterology And Hepatology 2023, 16: 223-242. PMID: 37146714, PMCID: PMC10394288, DOI: 10.1016/j.jcmgh.2023.04.007.Peer-Reviewed Original ResearchConceptsBA uptake transportersBile duct ligationHepatic neutrophil infiltrationCholestatic liver injuryProinflammatory cytokine productionCholic acid dietAdaptive protective responseLiver-specific overexpressionWild-type miceConjugated bile acidsUptake transportersPrimary hepatocytesUDCA feedingNeutrophil infiltrationBDL miceLiver injuryCytokine productionBile flowDuct ligationOrganic anion transporting polypeptide (OATP) 1B3Conjugated BAsTransgenic miceHepatic uptakeBile acidsProtective response
2022
Dectin-1 signaling in neutrophils up-regulates PD-L1 and triggers ROS-mediated suppression of CD4+ T cells
Deerhake ME, Cardakli ED, Shinohara ML. Dectin-1 signaling in neutrophils up-regulates PD-L1 and triggers ROS-mediated suppression of CD4+ T cells. Journal Of Leukocyte Biology 2022, 112: 1413-1425. PMID: 36073780, PMCID: PMC9701158, DOI: 10.1002/jlb.3a0322-152rr.Peer-Reviewed Original ResearchConceptsPD-L1 expressionExperimental autoimmune encephalomyelitisPD-L1T cellsT cell-suppressive propertiesUp-regulating PD-L1T cell-driven inflammationImmune checkpoint factorsNeutrophil PD-L1Suppression of CD4T cell responsesProinflammatory cytokine productionT cell viabilityHost defense functionsAutoimmune encephalomyelitisDendritic cellsCytokine productionMHC-IINeutrophil responseCD4Disease severityCell responsesNeutrophilsFungal infectionsReactive oxygen species
2018
Bacterial Lipoproteins Constitute the TLR2-Stimulating Activity of Serum Amyloid A
Burgess EJ, Hoyt LR, Randall MJ, Mank MM, Bivona JJ, Eisenhauer PL, Botten JW, Ballif BA, Lam YW, Wargo MJ, Boyson JE, Ather JL, Poynter ME. Bacterial Lipoproteins Constitute the TLR2-Stimulating Activity of Serum Amyloid A. The Journal Of Immunology 2018, 201: 2377-2384. PMID: 30158125, PMCID: PMC6179936, DOI: 10.4049/jimmunol.1800503.Peer-Reviewed Original ResearchConceptsEukaryotic cellsBacterial proteinsSerum amyloid ANumerous bacterial proteinsProteomic analysisMouse cellsRecombinant proteinsBacterial lipoproteinsProteinRecombinant serum amyloid ASAA1 proteinProinflammatory cytokine productionProduction of TNFCytokine productionProinflammatory functionsAmyloid ASerum amyloidCellsLipoprotein lipaseLipoproteinFuture studiesDifferentiationEscherichiaBindingLipopeptides
2016
The cystic fibrosis transmembrane conductance regulator controls biliary epithelial inflammation and permeability by regulating Src tyrosine kinase activity
Fiorotto R, Villani A, Kourtidis A, Scirpo R, Amenduni M, Geibel PJ, Cadamuro M, Spirli C, Anastasiadis PZ, Strazzabosco M. The cystic fibrosis transmembrane conductance regulator controls biliary epithelial inflammation and permeability by regulating Src tyrosine kinase activity. Hepatology 2016, 64: 2118-2134. PMID: 27629435, PMCID: PMC5115965, DOI: 10.1002/hep.28817.Peer-Reviewed Original ResearchConceptsBiliary epithelial cellsLiver diseaseToll-like receptor 4 activityToll-like receptor 4 responsesCystic fibrosis transmembrane conductance regulatorToll-like receptor 4Nuclear factorEpithelial cellsProinflammatory cytokine productionNovel therapeutic targetEpithelial barrier functionActivated B cellsFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorCytokine productionEpithelial inflammationInflammatory cellsInflammatory processReceptor 4Biliary damageInflammatory responseInflammatory cholangiopathyProtective effectBile secretionImmune pathwaysThe role of adipose-derived inflammatory cytokines in type 1 diabetes
Shao L, Feng B, Zhang Y, Zhou H, Ji W, Min W. The role of adipose-derived inflammatory cytokines in type 1 diabetes. Adipocyte 2016, 5: 270-274. PMID: 27617172, PMCID: PMC5014003, DOI: 10.1080/21623945.2016.1162358.Peer-Reviewed Original ResearchType 1 diabetesCytokine productionNF-κB-dependent cytokine productionAdipose-derived inflammatory cytokinesPancreatic isletsEffector T cell subsetsType 1 diabetes mellitusAcquisition of Th1Adipose tissue dysfunctionOnset of diabetesT cell subsetsDevelopment of diabetesProinflammatory cytokine productionDirect cytotoxic effectNF-κB inhibitorNF-κB activityAdipocyte-specific deletionDiabetes mellitusPancreatic inflammationPersistent inflammationProinflammatory cytokinesCCL5 expressionCell subsetsInflammatory cytokinesImmune regulation
2015
Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*
Park E, Choi S, Shin B, Yu J, Yu J, Hwang J, Yun H, Chung Y, Choi J, Choi Y, Rho J. Tumor Necrosis Factor (TNF) Receptor-associated Factor (TRAF)-interacting Protein (TRIP) Negatively Regulates the TRAF2 Ubiquitin-dependent Pathway by Suppressing the TRAF2-Sphingosine 1-Phosphate (S1P) Interaction*. Journal Of Biological Chemistry 2015, 290: 9660-9673. PMID: 25716317, PMCID: PMC4392267, DOI: 10.1074/jbc.m114.609685.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCytokinesGene ExpressionHEK293 CellsHeLa CellsHumansImmunoblottingLysineLysophospholipidsNF-kappa BProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionSphingosineTNF Receptor-Associated Factor 2Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor-alphaUbiquitinUbiquitinationConceptsTRAF-interacting proteinTNFR-associated factor 2TNF-induced inflammatory responseE3 ubiquitin (Ub) ligase activityTNF receptor signaling complexE3 Ub ligasesUbiquitin-dependent pathwayCellular binding partnersMitogen-activated protein kinase activationNF-kB activationNegative regulator of proinflammatory cytokine productionProtein kinase activityDownstream signaling cascadesCell proliferationTNF receptorsUb ligasesTNFR signaling pathwayDown-regulation of proinflammatory cytokine productionLigase activityRING domainTumor necrosis factorProinflammatory cytokine productionAdaptor moleculeCellular processesRegulation of proinflammatory cytokine production
2014
Prolonged Proinflammatory Cytokine Production in Monocytes Modulated by Interleukin 10 After Influenza Vaccination in Older Adults
Mohanty S, Joshi SR, Ueda I, Wilson J, Blevins TP, Siconolfi B, Meng H, Devine L, Raddassi K, Tsang S, Belshe RB, Hafler DA, Kaech SM, Kleinstein SH, Trentalange M, Allore HG, Shaw AC. Prolonged Proinflammatory Cytokine Production in Monocytes Modulated by Interleukin 10 After Influenza Vaccination in Older Adults. The Journal Of Infectious Diseases 2014, 211: 1174-1184. PMID: 25367297, PMCID: PMC4366602, DOI: 10.1093/infdis/jiu573.Peer-Reviewed Original ResearchMeSH KeywordsAdultAge FactorsAgedCytokinesDual Specificity Phosphatase 1FemaleGene Expression RegulationGPI-Linked ProteinsHumansImmunity, InnateInfluenza VaccinesInfluenza, HumanInterleukin-10Interleukin-6Lipopolysaccharide ReceptorsMaleMonocytesPhosphorylationReceptors, IgGSignal TransductionSTAT3 Transcription FactorTumor Necrosis Factor-alphaVaccinationYoung AdultConceptsOlder adultsInfluenza vaccinationInflammatory monocytesInterleukin-10Cytokine productionOlder subjectsAnti-inflammatory cytokine interleukin-10Influenza vaccine antibody responseTumor necrosis factor αImpaired vaccine responsesVaccine antibody responseIL-10 productionCytokine interleukin-10Proinflammatory cytokine productionNecrosis factor αAge-associated elevationPhosphorylated signal transducerVaccine responsesAntibody responseInterleukin-6Immune responseMonocyte populationsDay 28Intracellular stainingVaccinationTyro3, Axl, and Mertk Receptor Signaling in Inflammatory Bowel Disease and Colitis-associated Cancer
Rothlin CV, Leighton JA, Ghosh S. Tyro3, Axl, and Mertk Receptor Signaling in Inflammatory Bowel Disease and Colitis-associated Cancer. Inflammatory Bowel Diseases 2014, 20: 1472-1480. PMID: 24846720, PMCID: PMC4343000, DOI: 10.1097/mib.0000000000000050.BooksConceptsInflammatory bowel diseaseBowel diseaseImmune responseT-cell-dependent adaptive immune responsesApoptotic cellsReceptor tyrosine kinasesProinflammatory cytokine productionSuppression of inflammationAdaptive immune responsesInnate immune responseTAM receptor tyrosine kinasesPotent therapeutic opportunityDisease remissionTyrosine kinaseIntestinal inflammationCytokine productionInflammatory responseLigand Gas6Potent negative regulatorTherapeutic opportunitiesGenetic ablationInflammationProtein SReceptor signalingSuccessful management
2013
CD44 Deficiency Contributes to Enhanced Experimental Autoimmune Encephalomyelitis A Role in Immune Cells and Vascular Cells of the Blood–Brain Barrier
Flynn KM, Michaud M, Madri JA. CD44 Deficiency Contributes to Enhanced Experimental Autoimmune Encephalomyelitis A Role in Immune Cells and Vascular Cells of the Blood–Brain Barrier. American Journal Of Pathology 2013, 182: 1322-1336. PMID: 23416161, PMCID: PMC3620422, DOI: 10.1016/j.ajpath.2013.01.003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlood-Brain BarrierBone Marrow CellsCell AdhesionCell MovementCell PolarityChimeraEncephalomyelitis, Autoimmune, ExperimentalEndothelial CellsGene DeletionHyaluronan ReceptorsInflammationInflammation MediatorsMiceMice, Inbred C57BLMice, KnockoutPermeabilityProtein Serine-Threonine KinasesReceptor, Transforming Growth Factor-beta Type IReceptors, Transforming Growth Factor betaStromal CellsT-Lymphocytes, RegulatoryConceptsExperimental autoimmune encephalomyelitisBlood-brain barrierCD44-deficient miceCytokine productionT cellsCD44 deficiencyDisease severityBone marrow chimeric animalsMyelin oligodendrocyte glycoprotein peptideBlood-brain barrier integrityT helper 17 (Th17) cellsT cell-endothelial cell interactionsImmune cell numbersRegulatory T cellsCD4 T cellsHelper 17 cellsCD44 knockout miceProinflammatory cytokine productionWild-type miceCentral nervous systemGreater disease severityT cell differentiationAdhesion molecule CD44Type I expressionMultiple protective roles
2011
A Small-Molecule Macrophage Migration Inhibitory Factor Antagonist Protects against Glomerulonephritis in Lupus-Prone NZB/NZW F1 and MRL/lpr Mice
Leng L, Chen L, Fan J, Greven D, Arjona A, Du X, Austin D, Kashgarian M, Yin Z, Huang XR, Lan HY, Lolis E, Nikolic-Paterson D, Bucala R. A Small-Molecule Macrophage Migration Inhibitory Factor Antagonist Protects against Glomerulonephritis in Lupus-Prone NZB/NZW F1 and MRL/lpr Mice. The Journal Of Immunology 2011, 186: 527-538. PMID: 21106847, PMCID: PMC3124407, DOI: 10.4049/jimmunol.1001767.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Migration InhibitionFemaleGene Expression ProfilingGenetic Predisposition to DiseaseGlomerulonephritisHumansIntramolecular OxidoreductasesIsoxazolesLupus Erythematosus, SystemicMacrophage Migration-Inhibitory FactorsMiceMice, Inbred MRL lprMice, Inbred NZBMice, KnockoutMolecular Sequence DataRandom AllocationReceptors, ImmunologicConceptsMacrophage migration inhibitory factorMRL/lpr miceNZB/NZW F1Systemic lupus erythematosusMigration inhibitory factorLupus erythematosusLpr miceDihydro-5-isoxazole acetic acid methyl esterHigh-expression MIF allelesInhibitory factorExcessive proinflammatory responsesRetention of monocytesEnd-organ injuryEnd-organ damageProinflammatory cytokine productionDifferent autoimmune diseasesB cell activationMIF antagonismMIF antagonistAutoantibody productionChemokine expressionProinflammatory cytokinesAutoimmune diseasesCytokine productionMIF alleles
2008
Reduced Expression of Basal and Probiotic-inducible G-CSF in Intestinal Mononuclear Cells Is Associated with Inflammatory Bowel Disease
Martins A, Colquhoun P, Reid G, Kim S. Reduced Expression of Basal and Probiotic-inducible G-CSF in Intestinal Mononuclear Cells Is Associated with Inflammatory Bowel Disease. Inflammatory Bowel Diseases 2008, 15: 515-525. PMID: 19058228, DOI: 10.1002/ibd.20808.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEscherichia coliGranulocyte Colony-Stimulating FactorHumansInflammatory Bowel DiseasesInterleukin-12Interleukin-23Intestinal MucosaLacticaseibacillus rhamnosusLeukocytes, MononuclearMiceMice, Inbred C57BLMucous MembraneProbioticsReceptors, Granulocyte Colony-Stimulating FactorTumor Necrosis Factor-alphaConceptsGranulocyte-colony stimulating factorInflammatory bowel diseaseHuman peripheral blood mononuclear cellsPeripheral blood mononuclear cellsG-CSF productionIntestinal mononuclear cellsBlood mononuclear cellsMononuclear cellsRhamnosus GR-1L. rhamnosus GR-1IL-23Bowel diseaseIntestinal lamina propria mononuclear cellsGr-1Intestinal lamina propria cellsLamina propria mononuclear cellsNon-IBD patientsReceptor knockout miceReceptor-deficient miceProinflammatory cytokine productionLamina propria cellsBone marrow-derived macrophagesIntestinal tissue samplesMarrow-derived macrophagesG-CSF release
2007
Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome
Sutterwala FS, Mijares LA, Li L, Ogura Y, Kazmierczak BI, Flavell RA. Immune recognition of Pseudomonas aeruginosa mediated by the IPAF/NLRC4 inflammasome. Journal Of Experimental Medicine 2007, 204: 3235-3245. PMID: 18070936, PMCID: PMC2150987, DOI: 10.1084/jem.20071239.Peer-Reviewed Original ResearchConceptsInnate immune responseImmune responseP. aeruginosaCaspase-1Proinflammatory cytokine productionProinflammatory cytokines interleukinInfection of macrophagesCell deathHost cellsCapase-1Pseudomonas aeruginosaOpportunistic infectionsCytokine productionCytokines interleukinInflammatory responseImmune recognitionNLRC4 inflammasomeEffector moleculesType III secretion systemInfectionIPAFMacrophagesGram-negative bacteriumDeathAeruginosa
2005
A novel artemisinin derivative, 3-(12-β-artemisininoxy) phenoxyl succinic acid (SM735), mediates immunosuppressive effects in vitro and in vivo
Zhou W, Wu J, Wu Q, Wang J, Zhou Y, Zhou R, He P, Li X, Yang Y, Zhang Y, Li Y, Zuo J. A novel artemisinin derivative, 3-(12-β-artemisininoxy) phenoxyl succinic acid (SM735), mediates immunosuppressive effects in vitro and in vivo. Acta Pharmacologica Sinica 2005, 26: 1352-1358. PMID: 16225758, DOI: 10.1111/j.1745-7254.2005.00232.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory Agents, Non-SteroidalArtemisininsCell ProliferationCells, CulturedCytokinesDose-Response Relationship, DrugHemolysisHypersensitivity, DelayedImmunosuppressive AgentsInhibitory Concentration 50Interferon-gammaInterleukin-12Lymphocyte Culture Test, MixedMaleMiceMice, Inbred BALB CMice, Inbred C57BLSuccinatesConceptsDelayed-type hypersensitivityMixed lymphocyte reactionProliferation of splenocytesSheep red blood cellsImmunosuppressive agentsCytokine productionT-cell-mediated delayed-type hypersensitivityImmunosuppressive activityVivo immune activityProinflammatory cytokine productionIL-2 secretionNovel artemisinin derivativesEnzyme-linked immunosorbentDose-dependent mannerStrong immunosuppressive activityPotential immunosuppressive agentsRed blood cellsLymphocyte reactionImmunosuppressive effectsQuantitative hemolysisImmune activityMouse modelArtemisinin derivativesConA stimulationBlood cellsEnhanced TLR4 reactivity following injury is mediated by increased p38 activation
Maung AA, Fujimi S, Miller ML, MacConmara MP, Mannick JA, Lederer JA. Enhanced TLR4 reactivity following injury is mediated by increased p38 activation. Journal Of Leukocyte Biology 2005, 78: 565-573. PMID: 15857937, DOI: 10.1189/jlb.1204698.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBurnsCells, CulturedEnzyme ActivationEnzyme InhibitorsExtracellular Signal-Regulated MAP KinasesGene Expression RegulationImidazolesLipopolysaccharidesMacrophagesMaleMembrane GlycoproteinsMiceMyoD ProteinProtein KinasesPyridinesReceptors, Cell SurfaceSignal TransductionSpleenToll-Like Receptor 4Toll-Like ReceptorsConceptsMitogen-activated protein kinaseExtracellular signal-regulated kinaseStress-activated protein kinaseP38 activationJun N-terminal kinase (JNK) mitogen-activated protein kinaseProtein kinaseKinase mitogen-activated protein kinaseSAPK/JNK activationProtein-2 proteinTLR4 reactivitySham miceSpecific p38 inhibitorSignal-regulated kinaseInterleukin-1 receptor-associated kinaseDay 1Receptor-associated kinaseMyeloid differentiation primary response protein 88Tumor necrosis factor-alpha productionToll-like receptor 4Necrosis factor-alpha productionCell surface expressionTLR4 mRNA expressionInjury-induced increaseProinflammatory cytokine productionInjury-induced changes
2002
Murine Lyme Arthritis Development Mediated by p38 Mitogen-Activated Protein Kinase Activity
Anguita J, Barthold SW, Persinski R, Hedrick MN, Huy CA, Davis RJ, Flavell RA, Fikrig E. Murine Lyme Arthritis Development Mediated by p38 Mitogen-Activated Protein Kinase Activity. The Journal Of Immunology 2002, 168: 6352-6357. PMID: 12055252, PMCID: PMC4309983, DOI: 10.4049/jimmunol.168.12.6352.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, BacterialArthritis, InfectiousBorrelia burgdorferiCD4-Positive T-LymphocytesCell LineEnzyme ActivationInflammationInterferon-gammaLyme DiseaseMAP Kinase Kinase 3MAP Kinase Signaling SystemMiceMice, KnockoutMitogen-Activated Protein Kinase KinasesMitogen-Activated Protein Kinasesp38 Mitogen-Activated Protein KinasesPhagocytesPhosphorylationProtein-Tyrosine KinasesReceptors, InterferonConceptsProinflammatory cytokine productionCytokine productionT helper type 1 responsePhagocytic cellsDevelopment of arthritisPotential new therapeutic approachType 1 responseInfection of miceExperimental murine modelMurine Lyme arthritisNew therapeutic approachesLyme arthritis developmentTreatment of inflammationCytokine burstArthritis developmentJoint inflammationLyme arthritisNF-kappa BProinflammatory cytokinesTNF-alphaT cellsMurine modelTherapeutic approachesP38 MAP kinaseSpecific Abs
2000
The proinflammatory mediator macrophage migration inhibitory factor induces glucose catabolism in muscle
Benigni F, Atsumi T, Calandra T, Metz C, Echtenacher B, Peng T, Bucala R. The proinflammatory mediator macrophage migration inhibitory factor induces glucose catabolism in muscle. Journal Of Clinical Investigation 2000, 106: 1291-1300. PMID: 11086030, PMCID: PMC381433, DOI: 10.1172/jci9900.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell MovementFructosediphosphatesGlucoseGlycolysisHumansLactic AcidLiverMacrophage Migration-Inhibitory FactorsMacrophagesMiceMusclesPhosphofructokinase-2Phosphoric Monoester HydrolasesPhosphotransferases (Alcohol Group Acceptor)RatsTumor Cells, CulturedTumor Necrosis Factor-alphaConceptsMacrophage migration inhibitory factorMigration inhibitory factorTNF-alphaInhibitory factorTNF-alpha knockout miceMediator macrophage migration inhibitory factorAddition of MIFSystemic inflammatory responseSevere metabolic derangementProinflammatory cytokine productionSerum glucose levelsImmune cell activationAnterior pituitary glandPositive allosteric regulatorMetabolic derangementsAutocrine stimuliCytokine productionGlucose disposalImmune cellsSevere infectionsCatabolic effectsInflammatory responseGlucose levelsInsulin releaseCatabolic response
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