2015
Canalicular membrane MRP2/ABCC2 internalization is determined by Ezrin Thr567 phosphorylation in human obstructive cholestasis
Chai J, Cai SY, Liu X, Lian W, Chen S, Zhang L, Feng X, Cheng Y, He X, He Y, Chen L, Wang R, Wang H, Boyer JL, Chen W. Canalicular membrane MRP2/ABCC2 internalization is determined by Ezrin Thr567 phosphorylation in human obstructive cholestasis. Journal Of Hepatology 2015, 63: 1440-1448. PMID: 26212029, PMCID: PMC4686151, DOI: 10.1016/j.jhep.2015.07.016.Peer-Reviewed Original ResearchMeSH KeywordsAdultBile CanaliculiCase-Control StudiesCholestasisCytoskeletal ProteinsFemaleGallstonesGene Knockdown TechniquesHep G2 CellsHumansLiverMaleMembrane ProteinsMiddle AgedModels, BiologicalMultidrug Resistance-Associated Protein 2Multidrug Resistance-Associated ProteinsPhosphorylationProtein Kinase CReceptors, Autocrine Motility FactorRNA, MessengerThreonineConceptsObstructive cholestasisCholestatic liverMRP2 expressionMrp2 internalizationHepG2 cellsHuman obstructive cholestasisMRP2 protein expressionMembrane expressionHepatic MRP2 expressionNon-cholestatic controlsExpression of PKCαTotal protein levelsBile ductCholestatic patientsCholestasisBile acidsPatientsAbstractTextHuman liverProtein expressionProtein levelsLiverMRP2JaundiceAIMS
1999
Modulation of protein kinase C by taurolithocholic acid in isolated rat hepatocytes
Beuers U, Probst I, Soroka C, Boyer J, Kullak‐Ublick G, Paumgartner G. Modulation of protein kinase C by taurolithocholic acid in isolated rat hepatocytes. Hepatology 1999, 29: 477-482. PMID: 9918925, DOI: 10.1002/hep.510290227.Peer-Reviewed Original Research
1996
Tauroursodeoxycholic acid activates protein kinase C in isolated rat hepatocytes
Beuers U, Throckmorton D, Anderson, Isales C, Thasler W, Kullak-Ublick G, Sauter G, Koebe H, Paumgartner G, Boyer J. Tauroursodeoxycholic acid activates protein kinase C in isolated rat hepatocytes. Gastroenterology 1996, 110: 1553-1563. PMID: 8613063, DOI: 10.1053/gast.1996.v110.pm8613063.Peer-Reviewed Original ResearchConceptsEffect of TUDCATauroursodeoxycholic acidProtein kinase CHepatocellular Ca2Chronic cholestatic liver diseaseCholestatic liver diseaseAlpha-PKCPKC activityLiver diseaseLiver functionRadioenzymatic techniqueExperimental cholestasisPhorbol ester phorbolActivation of PKCKinase CTaurocholic acidImmunofluorescence techniqueAbstractTextMembrane-associated PKC activitySignificant increaseAIMSStimulation of exocytosisUnknown mechanismParticulate membrane fractionHepatocytes
1994
Effects of protein kinase C and cytosolic Ca2+ on exocytosis in the isolated perfused rat liver
Bruck R, Nathanson M, Roelofsen H, Boyer J. Effects of protein kinase C and cytosolic Ca2+ on exocytosis in the isolated perfused rat liver. Hepatology 1994, 20: 1032-1040. PMID: 7927205, DOI: 10.1002/hep.1840200436.Peer-Reviewed Original ResearchConceptsProtein kinase CKinase CApical exocytosisRegulation of exocytosisProtein kinase C inhibitor HHorseradish peroxidase concentrationCytosolic Ca2ExocytosisCell typesInhibitor HProtein kinase C activator phorbol dibutyrateHorseradish peroxidase excretionPhorbol dibutyrateCa2Rat liverRelative importanceNet excretionPeroxidase concentrationsHepatocytes
1989
Protein kinase C agonists inhibit bile secretion independently of effects on the microcirculation in the isolated perfused rat liver
Corasanti J, Smith N, Gordon E, Boyer J. Protein kinase C agonists inhibit bile secretion independently of effects on the microcirculation in the isolated perfused rat liver. Hepatology 1989, 10: 8-13. PMID: 2737605, DOI: 10.1002/hep.1840100103.Peer-Reviewed Original ResearchConceptsBile flowPerfusion pressureBile secretionVehicle dimethyl sulfoxideReversible decreaseConstant perfusate flowPhorbol dibutyrateVenous effluent concentrationsInactive phorbol ester 4Rat liver systemVascular redistributionHepatic microvasculaturePhorbol esterPhorbol ester 4Vasoactive agentsRole of hormonesPerfusate flowTrypan blue dyeAntagonist HProtein kinase C agonistsGm liverActive phorbol estersLiver systemRat liverOxygen consumption