2009
Maitotoxin converts the plasmalemmal Ca2+ pump into a Ca2+-permeable nonselective cation channel
Sinkins W, Estacion M, Prasad V, Goel M, Shull G, Kunze D, Schilling W. Maitotoxin converts the plasmalemmal Ca2+ pump into a Ca2+-permeable nonselective cation channel. American Journal Of Physiology - Cell Physiology 2009, 297: c1533-c1543. PMID: 19794142, PMCID: PMC2793065, DOI: 10.1152/ajpcell.00252.2009.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAnimals, Genetically ModifiedCalciumCation Transport ProteinsCationsCell MembraneCells, CulturedDown-RegulationElectric ConductivityFibroblastsHumansIon ChannelsKidneyMarine ToxinsMiceOxocinsPermeabilityPlasma Membrane Calcium-Transporting ATPasesRNA, Small InterferingSpodopteraUp-RegulationConceptsPermeable nonselective cation channelNonselective cation channelsCation channelsSpodoptera frugiperda (Sf9) insect cellsHEK cellsMouse embryonic fibroblastsHuman embryonic kidney 293 cellsEmbryonic kidney 293 cellsKidney 293 cellsInsect cellsEmbryonic fibroblastsWhole-cell membrane currentsMolecular identityCell membrane currentsCell typesPMCACytosolic freeMarine toxinsEnhanced expressionWhole-cell currentsPlasmalemmal Ca2PalytoxinATPaseCellsMaitotoxin
2001
Regulation of Drosophila transient receptor potential‐like (TrpL) channels by phospholipase C‐dependent mechanisms
Estacion M, Sinkins W, Schilling W. Regulation of Drosophila transient receptor potential‐like (TrpL) channels by phospholipase C‐dependent mechanisms. The Journal Of Physiology 2001, 530: 1-19. PMID: 11136854, PMCID: PMC2278390, DOI: 10.1111/j.1469-7793.2001.0001m.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviridaeCalciumCalmodulin-Binding ProteinsCell LineCHO CellsCricetinaeDrosophilaDrosophila ProteinsFluorescent DyesFura-2Indicators and ReagentsMembrane PotentialsMembrane ProteinsOocytesPatch-Clamp TechniquesPhosphatidylinositol 4,5-DiphosphateSpodopteraTransient Receptor Potential ChannelsType C PhospholipasesXenopusConceptsPhospholipase CPhospholipase DDrosophila TRPL channelsTRPL channel activitySf9 insect cellsBacterial PI-PLCsPLC-dependent mechanismChannel activityFura-2 assayReceptor stimulationHydrolysis of PIP2Generation of diacylglycerolPoly-unsaturated fatty acidsTRPL channelsReceptor-mediated activationAddition of phosphatidylinositolInsect cellsExogenous applicationPI-PLCTransient receptor potential-like channelPC-PLCPIP2Spontaneous channel activityTRPLDiacylglycerol
1998
Functional expression of TrpC1: a human homologue of the Drosophila Trp channel
SINKINS W, ESTACION M, SCHILLING W. Functional expression of TrpC1: a human homologue of the Drosophila Trp channel. Biochemical Journal 1998, 331: 331-339. PMID: 9512497, PMCID: PMC1219356, DOI: 10.1042/bj3310331.Peer-Reviewed Original ResearchConceptsStore-operated channelsPost-infection timesBasal cytosolic free Ca2Mammalian cellsExpression of TRPC1Whole-cell membrane currentsSf9 cellsNon-selective cation channelsCytosolic free Ca2Drosophila TRP channelsSf9 insect cellsInternal Ca2Baculovirus expression systemPlasmalemmal Ca2Basal Ba2TRPC1Free Ca2TRP channelsCation channelsGluconate solutionMembrane currentsInsect cellsAdditional subunitsHuman homologueCytoplasmic factors