2006
Palytoxin-induced cell death cascade in bovine aortic endothelial cells
Schilling W, Snyder D, Sinkins W, Estacion M. Palytoxin-induced cell death cascade in bovine aortic endothelial cells. American Journal Of Physiology - Cell Physiology 2006, 291: c657-c667. PMID: 16672692, DOI: 10.1152/ajpcell.00063.2006.Peer-Reviewed Original ResearchMeSH KeywordsAcrylamidesAnimalsAortaCalciumCattleCell DeathCells, CulturedCnidarian VenomsComputer SystemsDose-Response Relationship, DrugDrug Administration ScheduleEndothelial CellsEthidiumFluorescent DyesGreen Fluorescent ProteinsIntracellular MembranesMicroscopy, VideoOsmolar ConcentrationOuabainPertussis ToxinPropidiumConceptsAortic endothelial cellsBovine aortic endothelial cellsEndothelial cellsConcentration-dependent increaseCell deathAddition of ouabainMonovalent cation channelCell death cascadeCell lysisMarine toxin palytoxinCation channelsOuabainOncotic cell deathEB uptakeATPase pumpDeath cascadeTime-lapse video microscopyPropidium iodideDeathYO-PRO-1ExtracellularEthidium bromideDownstream eventsRapid uptake
2002
Blockade of maitotoxin-induced oncotic cell death reveals zeiosis
Estacion M, Schilling W. Blockade of maitotoxin-induced oncotic cell death reveals zeiosis. BMC Physiology 2002, 2: 2. PMID: 11825342, PMCID: PMC65053, DOI: 10.1186/1472-6793-2-2.Peer-Reviewed Original Research
2001
Maitotoxin-induced membrane blebbing and cell death in bovine aortic endothelial cells
Estacion M, Schilling W. Maitotoxin-induced membrane blebbing and cell death in bovine aortic endothelial cells. BMC Physiology 2001, 1: 2. PMID: 11231888, PMCID: PMC32181, DOI: 10.1186/1472-6793-1-2.Peer-Reviewed Original ResearchRegulation 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
1999
Maitotoxin activates a nonselective cation channel and a P2Z/P2X7-like cytolytic pore in human skin fibroblasts
Schilling W, Sinkins W, Estacion M. Maitotoxin activates a nonselective cation channel and a P2Z/P2X7-like cytolytic pore in human skin fibroblasts. American Journal Of Physiology 1999, 277: c755-c765. PMID: 10516106, DOI: 10.1152/ajpcell.1999.277.4.c755.Peer-Reviewed Original ResearchConceptsEffects of maitotoxinConcentration-dependent increaseNonselective cation channelsCation channelsHuman skin fibroblastsPlasmalemmal permeabilitySkin fibroblastsUptake of ethidiumIntracellular fura-2Cytolytic poreYO-PRO-1Permeable cation channelFura-2Receptor stimulationTypes of cellsCytosolic freeLactate dehydrogenaseMembrane currentsPotent cytolytic agentCytolytic agentsMaitotoxinCell typesPresent studyCell levelSingle-cell level