2019
Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors
Sun L, Liu Y, Wang J, Huang L, Yang Y, Cheng X, Fan Y, Zhu M, Liang H, Tian Y, Wang H, Guo C, Yu Y. Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors. Journal Of Biological Chemistry 2019, 294: 19589-19603. PMID: 31727741, PMCID: PMC6926468, DOI: 10.1074/jbc.ra119.009959.Peer-Reviewed Original ResearchConceptsFuture transgenic studiesFull-length variantATP responseTransmembrane domainTransgenic studiesMammalian speciesP2X5 receptorsAllosteryPathological functionsSingle replacementSingle-channel recordingsSkeletal muscleExon 10Molecular modelingFunctional subtypesATPResiduesNervous systemP2X5ReceptorsDomainMammalsSpeciesTM2Lack of knowledge
2017
The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide
Yang X, Niu Y, Liu Y, Yang Y, Wang J, Cheng X, Liang H, Wang H, Hu Y, Lu X, Zhu M, Xu T, Tian Y, Yu Y. The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide. Journal Of Biological Chemistry 2017, 292: 21662-21675. PMID: 29123030, PMCID: PMC5766947, DOI: 10.1074/jbc.m117.814707.Peer-Reviewed Original ResearchConceptsDEG/ENaCDegenerin/epithelial sodium channelIon channelsAcid-sensing ion channelsMammalian acid-sensing ion channelsSodium channelsDiverse functionsKey residuesEpithelial sodium channelFMRFamide peptidesAncient featureChannel gatingActivation mechanismDistinct mechanismsSubfamiliesMammalsENaCUnitary conductancePathological processesNew insightsNonproton ligandIon selectivityEndogenous agonistSynaptic transmissionFaNaCFGF13 Selectively Regulates Heat Nociception by Interacting with Nav1.7
Yang L, Dong F, Yang Q, Yang P, Wu R, Wu Q, Wu D, Li C, Zhong Y, Lu Y, Cheng X, Xu F, Chen L, Bao L, Zhang X. FGF13 Selectively Regulates Heat Nociception by Interacting with Nav1.7. Neuron 2017, 93: 806-821.e9. PMID: 28162808, DOI: 10.1016/j.neuron.2017.01.009.Peer-Reviewed Original ResearchConceptsDorsal root gangliaAction potential firingHeat nociceptionFibroblast growth factorDRG neuronsSustained action potential firingTransient receptor potential cation channel V1Intracellular fibroblast growth factorsNoxious heat stimulationNoxious heat stimuliMouse DRG neuronsNociceptive neuronsNociceptive behaviorSodium channel NaRoot gangliaHeat stimuliNociceptionAction potentialsSodium currentHeat stimulationGrowth factorFGF13NeuronsChannel NaCurrent knowledge
2016
Long noncoding RNA glypican 3 (GPC3) antisense transcript 1 promotes hepatocellular carcinoma progression via epigenetically activating GPC3
Zhu X, Yuan J, Zhu T, Li Y, Cheng X. Long noncoding RNA glypican 3 (GPC3) antisense transcript 1 promotes hepatocellular carcinoma progression via epigenetically activating GPC3. The FEBS Journal 2016, 283: 3739-3754. PMID: 27573079, DOI: 10.1111/febs.13839.Peer-Reviewed Original ResearchMeSH KeywordsAcetylationAlpha-FetoproteinsAnimalsBiomarkers, TumorCarcinoma, HepatocellularCell Line, TumorDisease ProgressionEpigenesis, GeneticGlypicansHep G2 CellsHeterograftsHistonesHumansLiver NeoplasmsMiceMice, NudePrognosisPromoter Regions, GeneticRNA, AntisenseRNA, Long NoncodingTranscriptional ActivationUp-RegulationConceptsHCC cell proliferationBarcelona Clinic Liver Cancer stageCell proliferationTranscript 1Inhibited HCC cell proliferationLiver Cancer stageHepatocellular carcinoma screeningPotential therapeutic targetXenograft tumor growthHepatocellular carcinoma progressionP300/CBP-associated factorWorse prognosisCarcinoma screeningMicrovascular invasionTumor sizeHCC patientsCancer stageTherapeutic targetHCC progressionTumor growthCarcinoma progressionPotential biomarkersPathophysiological processesHCC tissuesSignificant upregulationExploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel*
Niu Y, Yang Y, Liu Y, Huang L, Yang X, Fan Y, Cheng X, Cao P, Hu Y, Li L, Lu X, Tian Y, Yu Y. Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel*. Journal Of Biological Chemistry 2016, 291: 7571-7582. PMID: 26867576, PMCID: PMC4817185, DOI: 10.1074/jbc.m115.710251.Peer-Reviewed Original Research
2015
ASIC3 Mediates Itch Sensation in Response to Coincident Stimulation by Acid and Nonproton Ligand
Peng Z, Li W, Huang C, Jiang Y, Wang X, Zhu M, Cheng X, Xu T. ASIC3 Mediates Itch Sensation in Response to Coincident Stimulation by Acid and Nonproton Ligand. Cell Reports 2015, 13: 387-398. PMID: 26440887, DOI: 10.1016/j.celrep.2015.09.002.Peer-Reviewed Original ResearchConceptsAcid-sensing ion channel 3Itch sensationPrimary sensory neuronsIon channel 3ASIC3 geneSL-NH2Concomitant inflammationScratching behaviorPathological changesCoincident stimulationTissue acidosisASIC3 channelsSensory neuronsAcidosisNonproton ligandPruritogensSensationIle-GlyChannel 3Arg-LeuInflammationItchMiceNeuronsDesensitizationCytotoxic T cell responses are enhanced by antigen design involving the presentation of MUC1 peptide on cholera toxin B subunit
Lu W, Qiu L, Yan Z, Lin Z, Cao M, Hu C, Wang Z, Wang J, Yu Y, Cheng X, Cao P, Li R. Cytotoxic T cell responses are enhanced by antigen design involving the presentation of MUC1 peptide on cholera toxin B subunit. Oncotarget 2015, 6: 34537-34548. PMID: 26417929, PMCID: PMC4741471, DOI: 10.18632/oncotarget.5307.Peer-Reviewed Original ResearchMeSH KeywordsAdjuvants, ImmunologicAnimalsAntigen PresentationBlotting, WesternCancer VaccinesCholera ToxinDisease Models, AnimalEpitopes, B-LymphocyteFemaleFluorescent Antibody TechniqueLymphocyte ActivationMiceMice, Inbred C57BLMinisatellite RepeatsMucin-1Polymerase Chain ReactionT-Lymphocytes, CytotoxicVaccines, SubunitConceptsCytotoxic T lymphocytesMUC1-specific cytotoxic T lymphocytesElicit cytotoxic T lymphocyteCytotoxic T cell responsesT cell responsesCancer vaccine designCholera toxin B subunitToxin B subunitB-cell epitopesMUC1 vaccineTumor burdenCancer vaccinesTh1 cellsT cellsT lymphocytesMouse modelCell epitopesTumor growthCell responsesTumor tissueVaccine designTumor MUC1Antigen designVaccineMUC1 peptide
2014
Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation
Zhao W, Wang J, Ma X, Yang Y, Liu Y, Huang L, Fan Y, Cheng X, Chen H, Wang R, Yu Y. Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation. Nature Communications 2014, 5: 4189. PMID: 24943126, DOI: 10.1038/ncomms5189.Peer-Reviewed Original ResearchConceptsAllosteric changesChannel gatingLeft flipperP2X4 receptorDorsal fin domainAllosteric eventsP2X4 receptor activationPhysiological functionsResidues leadFin domainHydrophobic interactionsEssential roleExtracellular ATPFundamental processesZinc bridgesChannel activationReceptor activationDorsal finP2X receptorsReceptorsGatingDomainActivationL217V291Inherent Dynamics of Head Domain Correlates with ATP-Recognition of P2X4 Receptors: Insights Gained from Molecular Simulations
Huang L, Fan Y, Tian Y, Yang Y, Liu Y, Wang J, Zhao W, Zhou W, Cheng X, Cao P, Lu X, Yu Y. Inherent Dynamics of Head Domain Correlates with ATP-Recognition of P2X4 Receptors: Insights Gained from Molecular Simulations. PLOS ONE 2014, 9: e97528. PMID: 24878662, PMCID: PMC4039465, DOI: 10.1371/journal.pone.0097528.Peer-Reviewed Original Research
2011
CaV1.2 Channel N-terminal Splice Variants Modulate Functional Surface Expression in Resistance Size Artery Smooth Muscle Cells*
Bannister J, Thomas-Gatewood C, Neeb Z, Adebiyi A, Cheng X, Jaggar J. CaV1.2 Channel N-terminal Splice Variants Modulate Functional Surface Expression in Resistance Size Artery Smooth Muscle Cells*. Journal Of Biological Chemistry 2011, 286: 15058-15066. PMID: 21357696, PMCID: PMC3083159, DOI: 10.1074/jbc.m110.182816.Peer-Reviewed Original ResearchConceptsArterial smooth muscle cellsSmooth muscle cellsMuscle cellsSurface expressionIntravascular pressureSmooth muscle-specific expressionArtery smooth muscle cellsDepolarization-induced vasoconstrictionHuman cerebral arteriesWhole-cell currentsReduced surface expressionLarge vasodilationCerebral arteryInflux pathwayVariety of stimuliCardiovascular systemFunctional surface expressionVasodilationProximal N-terminusReduced expressionMuscle-specific expressionE1CAuxiliary subunitsKnockdownPhysiological functions
2009
Alternative splicing of Cav1.2 channel exons in smooth muscle cells of resistance-size arteries generates currents with unique electrophysiological properties
Cheng X, Pachuau J, Blaskova E, Asuncion-Chin M, Liu J, Dopico A, Jaggar J. Alternative splicing of Cav1.2 channel exons in smooth muscle cells of resistance-size arteries generates currents with unique electrophysiological properties. AJP Heart And Circulatory Physiology 2009, 297: h680-h688. PMID: 19502562, PMCID: PMC2724194, DOI: 10.1152/ajpheart.00109.2009.Peer-Reviewed Original ResearchAlternative SplicingAmino Acid SequenceAnimalsBase SequenceCalcium Channels, L-TypeCells, CulturedCerebral ArteriesCerebrovascular CirculationExonsMolecular Sequence DataMuscle, Smooth, VascularMyocytes, Smooth MusclePatch-Clamp TechniquesProtein Structure, TertiaryRatsRats, Sprague-DawleyVascular Resistance
2007
A Novel CaV1.2 N Terminus Expressed in Smooth Muscle Cells of Resistance Size Arteries Modifies Channel Regulation by Auxiliary Subunits*
Cheng X, Liu J, Asuncion-Chin M, Blaskova E, Bannister J, Dopico A, Jaggar J. A Novel CaV1.2 N Terminus Expressed in Smooth Muscle Cells of Resistance Size Arteries Modifies Channel Regulation by Auxiliary Subunits*. Journal Of Biological Chemistry 2007, 282: 29211-29221. PMID: 17699517, PMCID: PMC2276565, DOI: 10.1074/jbc.m610623200.Peer-Reviewed Original ResearchConceptsExon 1cN-terminusExon 1bAuxiliary subunitsRich N-terminusCysteine-rich N-terminusNovel alternative splicingResistance-size cerebral arteriesPlasma membrane insertionExon 1Arterial myocytesMultiple vascular functionsIsoform-dependent differencesWhole-cell current densityN-terminal variantsAlternative splicingMembrane insertionChannel regulationExon 1AMolecular identityHuman diseasesSubunitsTerminusEntry pathwaySmooth muscle cells
2006
Genetic ablation of caveolin-1 modifies Ca2+ spark coupling in murine arterial smooth muscle cells
Cheng X, Jaggar J. Genetic ablation of caveolin-1 modifies Ca2+ spark coupling in murine arterial smooth muscle cells. AJP Heart And Circulatory Physiology 2006, 290: h2309-h2319. PMID: 16428350, PMCID: PMC1698957, DOI: 10.1152/ajpheart.01226.2005.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBariumCadmiumCalcium SignalingCaveolin 1ElectrophysiologyEnzyme InhibitorsFluorescent DyesFura-2IndolesMiceMice, KnockoutMicroscopy, ConfocalMicroscopy, ElectronMuscle, Smooth, VascularMyocytes, Smooth MuscleNitroargininePatch-Clamp TechniquesRyanodine Receptor Calcium Release ChannelConceptsCerebral artery smooth muscle cellsSmooth muscle cellsArtery smooth muscle cellsMuscle cellsMurine arterial smooth muscle cellsGenetic ablationNitric oxide synthase activityVoltage-dependent calcium channelsArterial smooth muscle cellsOxide synthase activitySmooth muscle contractilityChannel blockersMuscle contractilityCalcium channelsCav-1-deficient cellsSpark regulationL-typeElevated intracellularSpark frequencyPotassium channelsSarcoplasmic reticulumCurrent activationCav-1Control cellsRelease channel
2002
Carbon Monoxide Dilates Cerebral Arterioles by Enhancing the Coupling of Ca2+ Sparks to Ca2+-Activated K+ Channels
Jaggar J, Leffler C, Cheranov S, Tcheranova D, E S, Cheng X. Carbon Monoxide Dilates Cerebral Arterioles by Enhancing the Coupling of Ca2+ Sparks to Ca2+-Activated K+ Channels. Circulation Research 2002, 91: 610-617. PMID: 12364389, DOI: 10.1161/01.res.0000036900.76780.95.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArteriolesCalcium Channel BlockersCalcium SignalingCarbon MonoxideCells, CulturedCerebral ArteriesCulture TechniquesElectric ConductivityHemeKineticsLysineMuscle, Smooth, VascularPotassium Channels, Calcium-ActivatedRyanodineRyanodine Receptor Calcium Release ChannelSignal TransductionSwineVasodilationVasodilator AgentsConceptsCerebral arteriolesArteriole smooth muscle cellsRelease channel blockerSmooth muscle cellsLarge-conductance Ca2Ryanodine-sensitive Ca2Enzyme heme oxygenasePial arteriolesCerebral circulationChannel blockersCoupling of Ca2Cellular signaling mechanismsPotent effectsArteriolesMuscle cellsHeme oxygenaseVasodilatorsPotent activatorControl conditionDilationPresent studySignaling mechanismCa2Source of controversyPercentage of Ca2Effect of Zinc Ions on Caffeine-Induced Contracture in Vascular Smooth Muscle and Skeletal Mu-scle of Rat
Cheng X, Chen K, Zhang X, Zhu P. Effect of Zinc Ions on Caffeine-Induced Contracture in Vascular Smooth Muscle and Skeletal Mu-scle of Rat. Cellular Physiology And Biochemistry 2002, 12: 119-126. PMID: 12077557, DOI: 10.1159/000063788.Peer-Reviewed Original ResearchConceptsVascular smooth muscleSmooth muscleCaffeine contractureCaffeine exposureSkeletal muscleCaffeine-induced contracturesDose-dependent mannerAortic stripsContractureIntracellular Ca2MuscleActivation dependenceMin intervalsRatsCaffeine concentrationsDepressionExposureMicroMPossible mechanismPotentiationSmall bundles
2001
Inhibition of Ryanodine Binding to Sarcoplasmic Reticulum Vesicles of Cardiac Muscle by Zn2+ Ions
Wang H, Wei Q, Cheng X, Chen K, Zhu P. Inhibition of Ryanodine Binding to Sarcoplasmic Reticulum Vesicles of Cardiac Muscle by Zn2+ Ions. Cellular Physiology And Biochemistry 2001, 11: 83-92. PMID: 11275686, DOI: 10.1159/000047795.Peer-Reviewed Original ResearchConceptsInhibitory effectCardiac muscleModulators of RyRSarcoplasmic reticulumSkeletal muscleSarcoplasmic reticulum vesiclesMuscleScatchard analysisRyanodine receptorRyanodine bindingRyRsThiol-reducing agentsPhysiological significanceReticulum vesiclesHill coefficientObvious changeActivation siteMM dithiothreitol
2000
Biphasic modulation of ryanodine binding to sarcoplasmic reticulum vesicles of skeletal muscle by Zn2+ ions
XIA R, CHENG X, Hui W, CHEN K, WEI Q, ZHANG X, ZHU P. Biphasic modulation of ryanodine binding to sarcoplasmic reticulum vesicles of skeletal muscle by Zn2+ ions. Biochemical Journal 2000, 345: 279-286. PMID: 10620505, PMCID: PMC1220757, DOI: 10.1042/bj3450279.Peer-Reviewed Original ResearchConceptsSarcoplasmic reticulum vesiclesReticulum vesiclesBiphasic modulationSkeletal muscle ryanodine receptorPeak bindingInhibitory effectMuscle ryanodine receptorHeavy sarcoplasmic reticulum vesiclesSkeletal muscleScatchard analysisRyanodine receptorBiphasic time courseRyanodine bindingTime courseMicroMThiol-reducing agentsPhysiological significanceInactivation site