2019
Syk-dependent glycolytic reprogramming in dendritic cells regulates IL-1β production to β-glucan ligands in a TLR-independent manner
Thwe PM, Fritz DI, Snyder JP, Smith PR, Curtis KD, O'Donnell A, Galasso NA, Sepaniac LA, Adamik BJ, Hoyt LR, Rodriguez PD, Hogan TC, Schmidt AF, Poynter ME, Amiel E. Syk-dependent glycolytic reprogramming in dendritic cells regulates IL-1β production to β-glucan ligands in a TLR-independent manner. Journal Of Leukocyte Biology 2019, 106: 1325-1335. PMID: 31509298, PMCID: PMC6883127, DOI: 10.1002/jlb.3a0819-207rr.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GlucansDendritic CellsGlycolysisInterleukin-1betaLectins, C-TypeLigandsMiceMyeloid Differentiation Factor 88NLR Family, Pyrin Domain-Containing 3 ProteinPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktSignal TransductionSyk KinaseToll-Like ReceptorsConceptsTLR-independent mannerDendritic cellsGlucan ligandMetabolic regulationMetabolic reprogramming eventsGlycolytic reprogrammingPyrin domain-containing protein 3 (NLRP3) inflammasome activationActivation of DCsProtein 3 inflammasome activationC-type lectin receptorsImmune effector functionsReprogramming eventsIL-1β productionImmune cell activationInnate immune receptorsFungal microbesMetabolic reprogrammingTyrosine kinaseReprogrammingImmune receptorsCytokine productionIL-1βT cellsInflammasome activationEffector functions
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
Uricase Inhibits Nitrogen Dioxide–Promoted Allergic Sensitization to Inhaled Ovalbumin Independent of Uric Acid Catabolism
Ather JL, Burgess EJ, Hoyt LR, Randall MJ, Mandal MK, Matthews DE, Boyson JE, Poynter ME. Uricase Inhibits Nitrogen Dioxide–Promoted Allergic Sensitization to Inhaled Ovalbumin Independent of Uric Acid Catabolism. The Journal Of Immunology 2016, 197: 1720-1732. PMID: 27465529, PMCID: PMC4992621, DOI: 10.4049/jimmunol.1600336.Peer-Reviewed Original ResearchConceptsAllergic airway diseaseAllergic sensitizationAirway diseaseUric acidDevelopment of OVAOVA-specific responsesAirways of miceUric acid levelsAdaptive immune responsesOVA-specific AbT cell proliferationPowerful inhibitory effectEnvironmental air pollutantsImmune deviationOVA challengeOVA uptakeDendritic cellsCytokine productionAdjuvant activityImmune responseRespiratory diseaseMouse modelUric acid formationInhibitory effectAcid levels
2015
Anti-Inflammatory Effects of Levalbuterol-Induced 11β-Hydroxysteroid Dehydrogenase Type 1 Activity in Airway Epithelial Cells
Randall MJ, Kostin SF, Burgess EJ, Hoyt LR, Ather JL, Lundblad LK, Poynter ME. Anti-Inflammatory Effects of Levalbuterol-Induced 11β-Hydroxysteroid Dehydrogenase Type 1 Activity in Airway Epithelial Cells. Frontiers In Endocrinology 2015, 5: 236. PMID: 25628603, PMCID: PMC4290686, DOI: 10.3389/fendo.2014.00236.Peer-Reviewed Original ResearchAirway epithelial cellsPro-inflammatory cytokine productionNF-κB activationAsthmatic subjectsCytokine productionRacemic albuterolEpithelial cellsEpithelial NF-κB activationAnti-inflammatory effectsNF-κB transcriptional activityTumor necrosis factorType 1 activityNF-κB activityAirway inflammationAllergic asthmaEndogenous glucocorticoidsLung functionCombination therapyNecrosis factorCorticosteroidsLuc activityAugments expressionAlbuterolMouse modelNF-κB
2013
The Endogenous Th17 Response in NO2-Promoted Allergic Airway Disease Is Dispensable for Airway Hyperresponsiveness and Distinct from Th17 Adoptive Transfer
Martin RA, Ather JL, Daggett R, Hoyt L, Alcorn JF, Suratt BT, Weiss DJ, Lundblad LK, Poynter ME. The Endogenous Th17 Response in NO2-Promoted Allergic Airway Disease Is Dispensable for Airway Hyperresponsiveness and Distinct from Th17 Adoptive Transfer. PLOS ONE 2013, 8: e74730. PMID: 24069338, PMCID: PMC3778003, DOI: 10.1371/journal.pone.0074730.Peer-Reviewed Original ResearchConceptsAllergic airway diseaseAirway hyperresponsivenessAirway diseaseAdoptive transferAntigen challengeCytokine productionNeutrophil recruitmentIL-1RDevelopment of AHRIL-1 receptor signalingLung cellsGlucocorticoid-resistant asthmaIL-17A neutralizationOTII T cellsAdaptive immune responsesDecreased neutrophil recruitmentAHR developmentClinical asthmaMixed Th2Antigen restimulationSevere asthmaTh17 cellsIL-17Th17 responsesAsthma severity