2004
The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*
Zhang Y, Joiner WJ, Bhattacharjee A, Rassendren F, Magoski NS, Kaczmarek LK. The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*. Journal Of Biological Chemistry 2004, 279: 52324-52330. PMID: 15375169, DOI: 10.1074/jbc.m408543200.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsAplysiaCell DifferentiationCHO CellsCricetinaeCyclic AMP-Dependent Protein KinasesDNA, ComplementaryIn Vitro TechniquesLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataNeuronsPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedProtein IsoformsRecombinant ProteinsReproductionConceptsBag cell neuronsReproductive behaviorSlo geneConsensus phosphorylation sitesCell cDNA libraryProtein kinase ACell neuronsChinese hamster ovary cellsPhosphorylation sitesCatalytic subunitHamster ovary cellsAlternative transcriptsCDNA librarySplice isoformsKinase ABK channel activityMaturation of neuronsPKA inhibitorVoltage-dependent channelsOvary cellsBrief synaptic stimulationChannel activityMature neuronsIsoformsPKA
2001
Casein Kinase 2 Determines the Voltage Dependence of the Kv3.1 Channel in Auditory Neurons and Transfected Cells
Macica C, Kaczmarek L. Casein Kinase 2 Determines the Voltage Dependence of the Kv3.1 Channel in Auditory Neurons and Transfected Cells. Journal Of Neuroscience 2001, 21: 1160-1168. PMID: 11160386, PMCID: PMC6762230, DOI: 10.1523/jneurosci.21-04-01160.2001.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAuditory PathwaysBinding SitesBrain StemCasein Kinase IICDC2-CDC28 KinasesCHO CellsCricetinaeCyclin-Dependent Kinase 2Cyclin-Dependent KinasesElectric StimulationEnzyme InhibitorsIn Vitro TechniquesMembrane PotentialsNeuronsNeuropeptidesPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Voltage-GatedPrecipitin TestsProtein Kinase CProtein Serine-Threonine KinasesRatsShaw Potassium ChannelsTetradecanoylphorbol AcetateTransfectionConceptsCasein kinase 2Kinase 2Casein kinase IIProtein kinase CKv3.1 channelsChinese hamster ovary cellsHamster ovary cellsConstitutive phosphorylationPhosphatase treatmentKinase IIKinase CTransfected CellsVoltage-dependent activationOvary cellsWhole-cell conductancePhosphorylationPotassium channelsRectifier channelsBiophysical characteristicsInactivationKv3.1 potassium channelVoltage dependenceActivationKv3.1Patch-clamp recordings
1999
hSK4/hIK1, a Calmodulin-binding KCa Channel in Human T Lymphocytes ROLES IN PROLIFERATION AND VOLUME REGULATION*
Khanna R, Chang M, Joiner W, Kaczmarek L, Schlichter L. hSK4/hIK1, a Calmodulin-binding KCa Channel in Human T Lymphocytes ROLES IN PROLIFERATION AND VOLUME REGULATION*. Journal Of Biological Chemistry 1999, 274: 14838-14849. PMID: 10329683, DOI: 10.1074/jbc.274.21.14838.Peer-Reviewed Original ResearchConceptsIK currentsActivated T cell functionSecondary immune responseNaive T cellsT cell functionPromising therapeutic targetChinese hamster ovary cellsHamster ovary cellsHuman T lymphocytesVolume regulationKCa channelsT cellsT lymphocytesImmune responseTherapeutic targetIK blockHSK4Accessory moleculesHuman T lymphoblastsOvary cellsDistal C-terminusPharmacological propertiesT lymphoblastsCell functionProximal C-terminus
1997
hSK4, a member of a novel subfamily of calcium-activated potassium channels
Joiner W, Wang L, Tang M, Kaczmarek L. hSK4, a member of a novel subfamily of calcium-activated potassium channels. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11013-11018. PMID: 9380751, PMCID: PMC23566, DOI: 10.1073/pnas.94.20.11013.Peer-Reviewed Original ResearchConceptsCalcium-activated potassium channelsSK channelsSmall-conductance calcium-activated potassium channelsPotassium channelsHSK4Novel subfamilyAdult animalsPredominant expressionLeucine zipper-like domainChinese hamster ovary cellsNonexcitable tissuesHamster ovary cellsChannel polypeptideOvary cellsLow homologyC-terminusHigh affinityUnknown function
1996
Inhibition by Nystatin of Kv1.3 Channels Expressed in Chinese Hamster Ovary Cells
HAHN S, WANG L, KACZMAREK L. Inhibition by Nystatin of Kv1.3 Channels Expressed in Chinese Hamster Ovary Cells. Neuropharmacology 1996, 35: 895-901. PMID: 8938720, DOI: 10.1016/0028-3908(96)00094-9.Peer-Reviewed Original ResearchConceptsKv1.3 currentsEffect of nystatinPerforated patch recordingsChinese hamster ovary cellsPatch-clamp techniqueWhole-cell configurationConcentration-dependent reductionHamster ovary cellsRectifier potassium channelHalf-maximal inhibitionPotassium channel Kv1.3Patch recordingsMaximal inhibitionAmphotericin BOvary cellsKv1.3 channelsPotassium channelsTetraethylammoniumChannel Kv1.3Intracellular solutionInhibitionRapid blockNystatinDrugsApparent inactivation