2019
Reduction in SNAP-23 Alters Microfilament Organization in Myofibrobastic Hepatic Stellate Cells.
Eubanks HB, Lavoie EG, Goree J, Kamykowski JA, Gokden N, Fausther M, Dranoff JA. Reduction in SNAP-23 Alters Microfilament Organization in Myofibrobastic Hepatic Stellate Cells. Gene Expression 2019, 20: 25-37. PMID: 31757226, PMCID: PMC7284106, DOI: 10.3727/105221619x15742818049365.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsActinsAnimalsCarbon TetrachlorideCell LineCell MovementCell SeparationGene Knockdown TechniquesHepatic Stellate CellsHumansLiverLiver CirrhosisMiceMyofibroblastsQb-SNARE ProteinsQc-SNARE ProteinsRho-Associated KinasesRNA InterferenceRNA, Small InterferingSignal TransductionStress FibersWound HealingConceptsSNAP-23T-SNARE proteinsSpecific SNARE proteinsMyofibroblastic hepatic stellate cellsSNARE proteinsActin cytoskeletonActin dynamicsHepatic stellate cellsCytoskeletal reorganizationCell movementPlasma membraneHomologous proteinsExtracellular environmentMicrofilament organizationSNAP-25HSC phenotypeReceptor proteinProteinStellate cellsQuiescent hepatic stellate cellsPhenotypeCellsCritical effector cellsCytoskeletonVivo
2005
The Anti-apoptotic Protein Mcl-1 Inhibits Mitochondrial Ca2+ Signals*
Minagawa N, Kruglov EA, Dranoff JA, Robert ME, Gores GJ, Nathanson MH. The Anti-apoptotic Protein Mcl-1 Inhibits Mitochondrial Ca2+ Signals*. Journal Of Biological Chemistry 2005, 280: 33637-33644. PMID: 16027162, DOI: 10.1074/jbc.m503210200.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaAniline CompoundsAntibodies, MonoclonalApoptosisBile Duct NeoplasmsCalcium SignalingCarbocyaninesCell LineCell Line, TumorCell NucleusFluorescent Antibody Technique, IndirectFluorescent DyesHeterocyclic Compounds, 3-RingHumansHydrazinesImmunohistochemistryMicroscopy, ConfocalMitochondriaModels, BiologicalMyeloid Cell Leukemia Sequence 1 ProteinNeoplasm ProteinsProto-Oncogene Proteins c-bcl-2Signal TransductionTissue DistributionXanthenesConceptsAnti-apoptotic proteinsMcl-1Mitochondrial Ca2Mcl-1 expressionApoptotic stimuliEndoplasmic reticulum Ca2Trisphosphate receptorCell growthNovel mechanismApoptosisMechanism of actionProteinExpressionDevelopment of neoplasiaCa2Reticulum Ca2CellsMitochondriaInositolRegulationPathwayMechanismSignalsReceptorsRegeneration
1999
Short‐term regulation of bile acid uptake by microfilament‐dependent translocation of rat ntcp to the plasma membrane
Dranoff J, McClure M, Burgstahler A, Denson L, Crawford A, Crawford J, Karpen S, Nathanson M. Short‐term regulation of bile acid uptake by microfilament‐dependent translocation of rat ntcp to the plasma membrane. Hepatology 1999, 30: 223-229. PMID: 10385660, DOI: 10.1002/hep.510300136.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonAnimalsBase SequenceBile Acids and SaltsBiological TransportCarcinoma, HepatocellularCarrier ProteinsCell MembraneCyclic AMPCytochalasin DGreen Fluorescent ProteinsHumansKineticsLiver NeoplasmsLuminescent ProteinsMembrane Transport ProteinsModels, MolecularMolecular Sequence DataOpen Reading FramesOrganic Anion Transporters, Sodium-DependentProtein Structure, SecondaryRatsRecombinant Fusion ProteinsSymportersTaurocholic AcidTransfectionTritiumTumor Cells, CulturedConceptsPlasma membraneGreen fluorescence proteinGFP fluorescenceNTCP-GFPPlasma membrane fluorescenceMembrane fluorescenceRat NtcpInhibitor of microfilamentsSecond messenger adenosinePrimary transporterFluorescence proteinNocodazole removalCytochalasin DTransporter activityShort-term regulationAcid uptakeConfocal video microscopyMicrotubule inhibitorsHepG2 cellsTaurocholate cotransportMembraneProteinMicrofilamentsCellsVideo microscopy