2009
Reducing Extracellular pH Sensitizes the Acinar Cell to Secretagogue-Induced Pancreatitis Responses in Rats
Bhoomagoud M, Jung T, Atladottir J, Kolodecik TR, Shugrue C, Chaudhuri A, Thrower EC, Gorelick FS. Reducing Extracellular pH Sensitizes the Acinar Cell to Secretagogue-Induced Pancreatitis Responses in Rats. Gastroenterology 2009, 137: 1083-1092. PMID: 19454288, PMCID: PMC2736307, DOI: 10.1053/j.gastro.2009.05.041.Peer-Reviewed Original ResearchConceptsAcinar cellsAcute pancreatitisPancreatic acinar cellsSecretagogue-induced pancreatitisAcid loadAcid challengeAcute acid loadKey early eventPancreatic edemaClinical studiesCell injuryPancreatitisAmylase secretionIsolated aciniAbstractTextPhe effectTrypsinogen activationInjuryPancreatitis responsesZymogen activationAIMSEarly eventsRatsActivationRelevant concentrations
2006
Vesicle-associated membrane protein 7 is expressed in intestinal ER
Siddiqi SA, Mahan J, Siddiqi S, Gorelick FS, Mansbach CM. Vesicle-associated membrane protein 7 is expressed in intestinal ER. Journal Of Cell Science 2006, 119: 943-950. PMID: 16495485, PMCID: PMC2828367, DOI: 10.1242/jcs.02803.Peer-Reviewed Original Research
2004
Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell
Chaudhuri A, Kolodecik TR, Gorelick FS. Effects of increased intracellular cAMP on carbachol-stimulated zymogen activation, secretion, and injury in the pancreatic acinar cell. AJP Gastrointestinal And Liver Physiology 2004, 288: g235-g243. PMID: 15458924, PMCID: PMC2975016, DOI: 10.1152/ajpgi.00334.2004.Peer-Reviewed Original ResearchConceptsPancreatic acinar cellsSecretion of amylaseAcinar cellsCell injuryIntracellular cAMPForms of pancreatitisParameters of injuryAcinar cell injuryCholinergic agonist carbacholEnzyme secretionRat pancreatic acinar cellsAcute pancreatitisZymogen activationAgonist carbacholSupraphysiological concentrationsCellular injuryCarbacholInjuryPancreatic aciniCAMP productionUnstimulated aciniSecretionCellular cAMPPhysiological concentrationsPancreatitis
2003
Effect of ligands that increase cAMP on caerulein-induced zymogen activation in pancreatic acini
Lu Z, Kolodecik TR, Karne S, Nyce M, Gorelick F. Effect of ligands that increase cAMP on caerulein-induced zymogen activation in pancreatic acini. AJP Gastrointestinal And Liver Physiology 2003, 285: g822-g828. PMID: 12881228, PMCID: PMC2830556, DOI: 10.1152/ajpgi.00213.2003.Peer-Reviewed Original ResearchConceptsCCK analogue caeruleinEffect of CCKAcinar cellsSupraphysiological concentrationsPancreatic aciniCell cAMP levelsRat pancreatic aciniRp-8-BrPancreatic acinar cellsPathological activationCell-permeable cAMP analogCAMP levelsPhysiological concentrationsPancreatitisCell cAMPCCKZymogen activationActivationCAMP analogPhysiological ligandsAciniCells
1998
Telenzepine-sensitive muscarinic receptors on rat pancreatic acinar cells
Schmid S, Modlin I, Tang L, Stoch A, Rhee S, Nathanson M, Scheele G, Gorelick F. Telenzepine-sensitive muscarinic receptors on rat pancreatic acinar cells. American Journal Of Physiology 1998, 274: g734-g741. PMID: 9575856, DOI: 10.1152/ajpgi.1998.274.4.g734.Peer-Reviewed Original ResearchConceptsPancreatic acinar cellsAmylase secretionRat pancreatic acinar cellsMuscarinic receptorsAcinar cellsDifferent muscarinic receptor antagonistsM2 antagonist methoctramineMaximal amylase secretionMuscarinic receptor antagonistIsolated rat pancreatic aciniRat pancreatic aciniAntagonist methoctramineM3 subtypeM1 antagonistMuscarinic subtypesReceptor antagonistZymogen processingAntagonist sensitivityPancreatic aciniSecretionAntagonistSubtypesPotent inhibitorReceptorsDistinct patterns
1996
Effect of ethanol on cholecystokinin-stimulated zymogen conversion in pancreatic acinar cells
Katz M, Carangelo R, Miller LJ, Gorelick F. Effect of ethanol on cholecystokinin-stimulated zymogen conversion in pancreatic acinar cells. American Journal Of Physiology 1996, 270: g171-g175. PMID: 8772515, DOI: 10.1152/ajpgi.1996.270.1.g171.Peer-Reviewed Original ResearchConceptsPancreatic acinar cellsEffects of ethanolAbility of ethanolAcinar cellsHigh dosesLow dose cholecystokininCholecystokinin receptor antagonistDose of ethanolReceptor antagonistCholecystokininSmall intestineCholecystokinin receptorsEthanol treatmentActive formCarbamylcholineZymogen conversionIntracellular conversionDosesPancreatic zymogensCellsAntagonistDoseIntestine
1993
Characterization of cAMP‐dependent protein kinase activation by CCK in rat pancreas
Marino C, Leach S, Schaefer J, Miller L, Gorelick F. Characterization of cAMP‐dependent protein kinase activation by CCK in rat pancreas. FEBS Letters 1993, 316: 48-52. PMID: 7678554, PMCID: PMC2830555, DOI: 10.1016/0014-5793(93)81734-h.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAnimalsCholecystokininCyclic AMPEnzyme ActivationIn Vitro TechniquesMalePancreasProtein KinasesRatsRats, Sprague-DawleyConceptsCAMP-dependent protein kinase activityProtein kinase activityKinase activityCAMP second messenger cascadeCAMP-dependent protein kinase activationProtein kinase activationSecond messenger cascadesCellular cAMP levelsKinase activationCAMP cascadeTreatment of aciniMessenger cascadesCellular cAMPCAMP levelsEnzyme secretionCascadeNew sensitive assayRat pancreatic aciniSensitive assayPancreatic aciniActivityHigh concentrationsAciniCellsActivation
1990
Rabbit ileal villus cell brush border Na+/H+ exchange is regulated by Ca2+/calmodulin-dependent protein kinase II, a brush border membrane protein.
Cohen ME, Reinlib L, Watson AJ, Gorelick F, Rys-Sikora K, Tse M, Rood RP, Czernik AJ, Sharp GW, Donowitz M. Rabbit ileal villus cell brush border Na+/H+ exchange is regulated by Ca2+/calmodulin-dependent protein kinase II, a brush border membrane protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 8990-8994. PMID: 2174171, PMCID: PMC55086, DOI: 10.1073/pnas.87.22.8990.Peer-Reviewed Original ResearchConceptsDependent protein kinase IIProtein kinase IIKinase IIMembrane proteinsSynapsin IDependent protein kinase activityDependent protein kinaseBrush border membranePhosphorylation of sitesProtein kinase activityInhibitor peptideCaM kinase IIBrush border membrane proteinsBorder membraneSpecific inhibitor peptidePhosphopeptide mappingBrush borderProtein kinaseMicrovillus membrane proteinsKinase activityIleal brush-border membraneVillus cell brush border membraneApical membraneKinaseVesicle preparations
1986
Phytohemagglutinin from red kidney bean (Phaseolus vulgaris) inhibits sodium and chloride absorption in the rabbit ileum
Dobbins J, Laurenson J, Gorelick F, Banwell J. Phytohemagglutinin from red kidney bean (Phaseolus vulgaris) inhibits sodium and chloride absorption in the rabbit ileum. Gastroenterology 1986, 90: 1907-1913. PMID: 3009261, DOI: 10.1016/0016-5085(86)90260-x.Peer-Reviewed Original ResearchConceptsRabbit ileumTissue conductanceCyclic guanosine monophosphateEffects of phytohemagglutininIndicator of absorptionAmino acid absorptionSerosal calciumMucosal levelSerosal additionCyclic adenosine monophosphatePhytohemagglutininControl tissuesChloride absorptionCrypt cellsAcid absorptionIleumRabbit colonDietary lectinsGuanosine monophosphateEpithelial surfaceVillus cellsElectrolyte transportLuminal borderNet NaMucosal solution