Laura Rose Hoyt
About
Research
Publications
2023
Metabolic fitness of IgA+ plasma cells in the gut requires DOCK8
Zhang B, Chen S, Yin X, McBride C, Gertie J, Yurieva M, Bielecka A, Hoffmann B, Hinson J, Grassmann J, Xu L, Siniscalco E, Soldatenko A, Hoyt L, Joseph J, Norton E, Uthaman G, Palm N, Liu E, Eisenbarth S, Williams A. Metabolic fitness of IgA+ plasma cells in the gut requires DOCK8. Mucosal Immunology 2023, 17: 431-449. PMID: 38159726, PMCID: PMC11571232, DOI: 10.1016/j.mucimm.2023.12.001.Peer-Reviewed Original ResearchPlasma cellsLamina propriaT cell-dependent antigensCytokinesis 8 (DOCK8) mutationsDOCK8-deficient miceMucosal IgA productionRecurrent gastrointestinal infectionGut lamina propriaPoor antibody responseIgA class switchingAntigen-specific IgAEarly B cell activationLong-term survivalB cell activationGut IgAFood antigensAntibody responseIgA productionImmune homeostasisGastrointestinal infectionsPrimary immunodeficiencyT cellsPC compartmentB cellsCell activationThe Effects of Pregnancy on the Pulmonary Immune Response in a Mouse Model of LPS-Induced Acute Lung Injury
Rieck R, Bivona J, Hoyt L, Ventrone S, Kokoszynska M, Bonney E, Suratt B. The Effects of Pregnancy on the Pulmonary Immune Response in a Mouse Model of LPS-Induced Acute Lung Injury. American Journal Of Perinatology 2023, 40: 817-824. PMID: 36796402, DOI: 10.1055/s-0043-1761916.Peer-Reviewed Original ResearchConceptsAcute lung injuryEffect of pregnancyNonpregnant miceAdhesion molecule-1Lung injuryPregnant miceNeutrophil responseImmune responseVCAM-1Mouse modelBronchoalveolar lavage fluid (BALF) differential cell countMolecule-1LPS-Induced Acute Lung InjuryPulmonary innate immune responseVascular cell adhesion molecule-1Intercellular adhesion molecule-1Cell adhesion molecule-1BALF total cellsBlood neutrophil responsesInhalation of lipopolysaccharidePulmonary immune responseVascular endothelial adhesion moleculesSevere lung diseasePeripheral blood neutrophilsBone marrow neutrophils
2022
Ketone body augmentation decreases methacholine hyperresponsiveness in mouse models of allergic asthma
Mank M, Reed L, Fastiggi V, Peña-García P, Hoyt L, Van Der Vliet K, Ather J, Poynter M. Ketone body augmentation decreases methacholine hyperresponsiveness in mouse models of allergic asthma. Journal Of Allergy And Clinical Immunology Global 2022, 1: 282-298. PMID: 36466740, PMCID: PMC9718535, DOI: 10.1016/j.jacig.2022.08.001.Peer-Reviewed Original ResearchKetone ester supplementationMethacholine hyperresponsivenessAllergic asthmaAirway epithelial cellsKetogenic dietDose-dependent mannerKetone bodiesMouse modelElicit anti-inflammatory activityAllergic asthmatic individualsBronchial smooth muscle cellsChronic allergic asthmaHuman airway epithelial cellsEpithelial cellsProinflammatory cytokine secretionIL-8 secretionAnti-inflammatory activityBHB concentrationsSmooth muscle cellsKetone body precursorsRange of mildHDM sensitizationObese asthmaCell typesCorticosteroid treatmentReply
Hoyt LR, Williams A, Eisenbarth SC. Reply. Journal Of Allergy And Clinical Immunology 2022, 150: 490. PMID: 35568592, DOI: 10.1016/j.jaci.2022.03.031.Peer-Reviewed Original ResearchInnate and Adaptive Immunity to Transfused Allogeneic RBCs in Mice Requires MyD88.
Soldatenko A, Hoyt LR, Xu L, Calabro S, Lewis SM, Gallman AE, Hudson KE, Stowell SR, Luckey CJ, Zimring JC, Liu D, Santhanakrishnan M, Hendrickson JE, Eisenbarth SC. Innate and Adaptive Immunity to Transfused Allogeneic RBCs in Mice Requires MyD88. The Journal Of Immunology 2022, 208: 991-997. PMID: 35039331, PMCID: PMC10107373, DOI: 10.4049/jimmunol.2100784.Peer-Reviewed Original ResearchConceptsPattern recognition receptorsDendritic cellsDC activationAdaptive immunityClass of PRRsNon-ABO alloantibodiesRecipient dendritic cellsSplenic dendritic cellsMouse RBCsInflammatory cytokine responseTreatment of anemiaRBC transfusion therapyTransfused RBCsAlloantibody responsesAllogeneic RBCsSerious complicationsCytokine responsesTransfusion therapyRecognition receptorsMyD88TransfusionAlloimmunizationRBCsTRIFUnknown mechanism
2021
Oral anaphylaxis to peanut in a mouse model is associated with gut permeability but not with Tlr4 or Dock8 mutations
Gertie JA, Zhang B, Liu EG, Hoyt LR, Yin X, Xu L, Long LL, Soldatenko A, Gowthaman U, Williams A, Eisenbarth SC. Oral anaphylaxis to peanut in a mouse model is associated with gut permeability but not with Tlr4 or Dock8 mutations. Journal Of Allergy And Clinical Immunology 2021, 149: 262-274. PMID: 34051223, PMCID: PMC8626534, DOI: 10.1016/j.jaci.2021.05.015.Peer-Reviewed Original ResearchMeSH KeywordsAdministration, OralAnimalsArachisDisease Models, AnimalFemaleGastrointestinal MicrobiomeGenetic Predisposition to DiseaseGuanine Nucleotide Exchange FactorsIntestinal MucosaMaleMice, Inbred C3HMice, Inbred C57BLMutationPassive Cutaneous AnaphylaxisPeanut HypersensitivityPermeabilitySpecies SpecificityToll-Like Receptor 4ConceptsC3H/HeJ miceGut permeabilityHeJ miceOral anaphylaxisPeanut challengeFood allergyMouse modelToll-like receptor 4BALB/c miceCytokinesis 8 (DOCK8) mutationsEnhanced gut permeabilityOral peanut challengesDOCK8 functionIngested allergenImmunologic mechanismsAnaphylaxis responsesImmunologic pathwaysAllergic diseasesC57BL/6 micePeanut allergyAntibody responseC miceReceptor 4DOCK8 mutationsIntraperitoneal challenge
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
2017
Mitochondrial ROS induced by chronic ethanol exposure promote hyper-activation of the NLRP3 inflammasome
Hoyt LR, Randall MJ, Ather JL, DePuccio DP, Landry CC, Qian X, Janssen-Heininger YM, van der Vliet A, Dixon AE, Amiel E, Poynter ME. Mitochondrial ROS induced by chronic ethanol exposure promote hyper-activation of the NLRP3 inflammasome. Redox Biology 2017, 12: 883-896. PMID: 28463821, PMCID: PMC5413213, DOI: 10.1016/j.redox.2017.04.020.Peer-Reviewed Original ResearchConceptsChronic ethanol exposureEthanol exposureNLRP3 inflammasomeInflammasome activationPro-inflammatory cytokines IL-1βHuman peripheral blood mononuclear cellsPeripheral blood mononuclear cellsLong-term ethanol exposureInflammation-linked diseasesNLRP3 inflammasome hyperactivationAberrant NLRP3 inflammasome activationBlood mononuclear cellsExposure of leukocytesCytokines IL-1βNLRP3 inflammasome activationIL-1β secretionNO scavenger carboxy-PTIOAlcohol use disorderMetabolism of ethanolScavenger carboxy-PTIOMouse macrophage cell lineIL-18IL-1βMononuclear cellsProlonged administration
2016
465 Protein S-Acylation in Pulmonary Disease
Randall M, Ather J, Hoyt L, Dixon A, Poynter M. 465 Protein S-Acylation in Pulmonary Disease. Free Radical Biology And Medicine 2016, 100: s193. DOI: 10.1016/j.freeradbiomed.2016.10.528.Peer-Reviewed Original ResearchHigh-fat dietHouse dust miteNasal epithelial cellsLung tissueMurine lung tissueWhole lung tissueReactive oxygen speciesEpithelial cellsPrimary nasal epithelial cellsPoor symptom controlHuman nasal epithelial cellsNon-asthmatic patientsPathophysiology of asthmaMajor risk factorFrequent exacerbationsObese asthmaticsSymptom controlComorbid diseasesObese controlsPulmonary diseaseC57BL/6 miceLung diseaseDust miteRisk factorsWestern diet
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