2021
Single-cell analysis of prostaglandin E2-induced human decidual cell in vitro differentiation: a minimal ancestral deciduogenic signal†
Stadtmauer DJ, Wagner G. Single-cell analysis of prostaglandin E2-induced human decidual cell in vitro differentiation: a minimal ancestral deciduogenic signal†. Biology Of Reproduction 2021, 106: 155-172. PMID: 34591094, PMCID: PMC8757638, DOI: 10.1093/biolre/ioab183.Peer-Reviewed Original ResearchMeSH KeywordsCell DifferentiationCell Line, TransformedCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesDeciduaDinoprostoneEndometriumFemaleFibroblastsGene ExpressionGenome-Wide Association StudyHumansMedroxyprogesterone AcetatePregnancyReceptors, Prostaglandin E, EP2 SubtypeSequence Analysis, RNASingle-Cell AnalysisConceptsPlacental mammalsCore gene regulatory networkCyclic AMP/protein kinase A (cAMP/PKA) pathwayProtein kinase A (PKA) pathwaySenescence-associated genesProgesterone-dependent activationGenome-wide studiesSingle-cell transcriptomicsGene regulatory networksProgesterone-dependent inductionMembrane-permeable cAMPKinase A PathwaySingle-cell analysisUse of PGE2Outgroup taxaCellular statesRegulatory networksPKA axisGene expressionDecidual genesPKA activationPGE2 receptor 2Progestin-dependent inductionA PathwayAdenylyl cyclase activation
2020
Calcium‐induced calcium release in proximity to hair cell BK channels revealed by PKA activation
Bai J, Xue N, Lawal O, Nyati A, Santos‐Sacchi J, Navaratnam D. Calcium‐induced calcium release in proximity to hair cell BK channels revealed by PKA activation. Physiological Reports 2020, 8: e14449. PMID: 32748549, PMCID: PMC7399380, DOI: 10.14814/phy2.14449.Peer-Reviewed Original ResearchConceptsBK channelsBK currentsCalcium-activated potassium channelsLarge-conductance calcium-activated potassium channelsCalcium-induced calcium releaseEntry of CaSlo subunitSynaptic releaseCalcium releaseChicken hair cellsPotassium channelsHair cellsIP3 receptorCICRA ActivationPKA activationActivationCritical roleImagingReleaseRyanodine
2015
Activation of Protein Kinase A in Mature Osteoblasts Promotes a Major Bone Anabolic Response
Tascau L, Gardner T, Anan H, Yongpravat C, Cardozo CP, Bauman WA, Lee FY, Oh DS, Tawfeek HA. Activation of Protein Kinase A in Mature Osteoblasts Promotes a Major Bone Anabolic Response. Endocrinology 2015, 157: 112-126. PMID: 26488807, DOI: 10.1210/en.2015-1614.Peer-Reviewed Original ResearchMeSH KeywordsAMP-Activated Protein KinasesAnimalsBone DensityCells, CulturedEnergy MetabolismEnzyme ActivationFemaleFemurLumbar VertebraeMaleMice, Inbred C57BLMice, TransgenicOsteoblastsOsteocytesOsteogenesisPoint MutationPromoter Regions, GeneticSex CharacteristicsUp-RegulationX-Ray MicrotomographyConceptsBone anabolic responseOb miceMature osteoblastsPKA activationHigher basal PKA activityControl miceAnabolic responseProtein kinase ASerum bone turnover markersBone volume/total volumeBone turnover markersBasal PKA activityFemur cortical thicknessTotal tissue areaActive PKAKinase AConstitutive activationPKA activityTurnover markersBone lossAnabolic drugsStructure model indexOsteoclast numberFemale miceBone mass
2007
NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity
Kocinsky HS, Dynia DW, Wang T, Aronson PS. NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity. American Journal Of Physiology. Renal Physiology 2007, 293: f212-f218. PMID: 17409282, DOI: 10.1152/ajprenal.00042.2007.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAnimalsCells, CulturedColforsinCyclic AMP-Dependent Protein KinasesElectrophoresis, Polyacrylamide GelKidneyKidney Tubules, ProximalMaleMicrovilliParathyroid HormonePhosphodiesterase InhibitorsPhosphorylationRatsRats, Sprague-DawleySerineSodiumSodium RadioisotopesSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersStimulation, ChemicalConceptsSerine 552NHE3 phosphorylationNHE3 activityMicrovillar membrane vesiclesPhosphorylation of NHE3Direct phosphorylationPhosphospecific antibodiesSprague-Dawley ratsExchanger type 3PKA activationMembrane vesiclesSite-specific changesPhosphorylationTransport activityOpossum kidney cellsParathyroid hormoneIntravenous infusionRat modelExchange activityKidney cellsOKP cellsNHE3 inhibitionPKACell modelExact role
2004
Involvement of Salmonella Pathogenicity Island 2 in the Up-Regulation of Interleukin-10 Expression in Macrophages: Role of Protein Kinase A Signal Pathway
Uchiya K, Groisman EA, Nikai T. Involvement of Salmonella Pathogenicity Island 2 in the Up-Regulation of Interleukin-10 Expression in Macrophages: Role of Protein Kinase A Signal Pathway. Infection And Immunity 2004, 72: 1964-1973. PMID: 15039316, PMCID: PMC375175, DOI: 10.1128/iai.72.4.1964-1973.2004.Peer-Reviewed Original ResearchConceptsSalmonella pathogenicity island 2Pathogenicity island 2Wild-type SalmonellaCyclic AMP response element binding proteinPKA activityProtein kinase A (PKA) signal pathwaySPI-2Island 2Signal transduction pathwaysProtein kinase A (PKA) inhibitor HResponse element-binding proteinA (PKA) inhibitor HElement-binding proteinFacultative intracellular bacteriaAMP response element binding proteinTransduction pathwaysSpiC genePKA activationSpiC mutantIntracellular bacteriaInhibitor HSignal pathwayCREB phosphorylationUp-RegulationPhosphorylation
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