2012
Cerulein hyperstimulation decreases AMP-activated protein kinase levels at the site of maximal zymogen activation
Shugrue C, Alexandre M, de Villalvilla A, Kolodecik TR, Young LH, Gorelick FS, Thrower EC. Cerulein hyperstimulation decreases AMP-activated protein kinase levels at the site of maximal zymogen activation. AJP Gastrointestinal And Liver Physiology 2012, 303: g723-g732. PMID: 22821946, PMCID: PMC3468535, DOI: 10.1152/ajpgi.00082.2012.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAminoimidazole CarboxamideAMP-Activated Protein KinasesAnimalsCells, CulturedCeruletideCyclic AMP-Dependent Protein KinasesEnzyme PrecursorsGene Expression RegulationMaleMetforminOctoxynolPancreasPhosphorylationPyrazolesPyrimidinesRatsRats, Sprague-DawleyRibonucleotidesSodium Dodecyl SulfateConceptsAdenosine monophosphate-activated protein kinaseZymogen activationAMPK activityPancreatic acinar cellsMonophosphate-activated protein kinaseVacuolar ATPase activityAMPK levelsDigestive enzyme zymogensAMPK effectsProtein kinaseProtein kinase levelsE subunitAcinar cellsTime-dependent translocationCompound CCellular modelPancreatitis responsesATPase activityDifferential centrifugationPremature activationChymotrypsin activityActivationInitiating eventSoluble fractionCerulein hyperstimulation
2007
Cyclic AMP-dependent protein kinase and Epac mediate cyclic AMP responses in pancreatic acini
Chaudhuri A, Husain SZ, Kolodecik TR, Grant WM, Gorelick FS. Cyclic AMP-dependent protein kinase and Epac mediate cyclic AMP responses in pancreatic acini. AJP Gastrointestinal And Liver Physiology 2007, 292: g1403-g1410. PMID: 17234888, PMCID: PMC2975017, DOI: 10.1152/ajpgi.00478.2005.Peer-Reviewed Original ResearchConceptsProtein kinaseZymogen activationCAMP-dependent protein kinaseStimulation of PKACyclic AMP-dependent protein kinasePancreatic acinar cellsAMP-dependent protein kinaseApical actin cytoskeletonCAMP-binding proteinsRole of PKAMuscarinic agonist carbacholIntracellular zymogen activationSupraphysiological concentrationsCAMP-dependent pathwayActin cytoskeletonApical cytoskeletonPhenotypic responsesPKA responseAgonist carbacholCarbachol-induced activationAcinar cellsDecreased secretionEpacCAMP pathwayPancreatic acini
1995
Calmodulin-dependent protein kinases in rat glioblastoma.
Cheng EH, Gorelick FS, Czernik AJ, Bagaglio DM, Hait WN. Calmodulin-dependent protein kinases in rat glioblastoma. Molecular Cancer Research 1995, 6: 615-21. PMID: 7647041.Peer-Reviewed Original ResearchConceptsCaM-dependent protein kinaseProtein kinaseKinase II activitySignal transductionCaM kinase II activityKinase IICalmodulin-dependent protein kinaseCalcium-dependent signal transductionCaM-dependent protein kinase IIExogenous synapsin ICell cycle regulationII activityCaM kinase IIIElongation factor 2Protein kinase IICell linesCaM kinase IINumerous malignant cell linesSpecific peptide substratePhosphopeptide mappingKinase IIIAbnormal cell growthCycle regulationKinase activityKinase
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
1987
Calcium-calmodulin-stimulated protein kinase in developing pancreas
Gorelick FS, Chang A, Jamieson JD. Calcium-calmodulin-stimulated protein kinase in developing pancreas. American Journal Of Physiology 1987, 253: g469-g476. PMID: 3116856, DOI: 10.1152/ajpgi.1987.253.4.g469.Peer-Reviewed Original ResearchConceptsCalmodulin-dependent protein kinaseProtein kinase activityCDPK activityProtein kinaseKinase activityEndogenous proteinsType II calmodulin-dependent protein kinaseType II Ca2Adult pancreasCaM-binding proteinsRelative molecular weightEmbryonic pancreasPancreatic developmentPancreatic acinar cellsGel filtration chromatographySecretagogue responsivenessCalcium-calmodulinExogenous substratesKinaseSynapsin IPancreatic maturationProteinPancreatic supernatantPhosphorylationSecretory processPurification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas
Cohn J, Kinder B, Jamieson J, Delahunt N, Gorelick F. Purification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas. Biochimica Et Biophysica Acta 1987, 928: 320-331. PMID: 3105599, DOI: 10.1016/0167-4889(87)90192-3.Peer-Reviewed Original ResearchConceptsCalmodulin protein kinaseCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseProtein kinaseMultifunctional calcium/calmodulin-dependent protein kinaseTwo-dimensional gel electrophoresisRibosomal proteinsThreonine residuesLarge subunitCellular functionsRibosomal substratesSubstrate specificityKinaseProteolytic degradationSubunitsGel electrophoresisHydrophobic chromatographyAffinity chromatographyPolyacrylamide gelsCalmodulinPurification procedureGel filtrationEnzyme preparationAutophosphorylationTissueCalcium-Calmodulin-Dependent Protein Kinase in Hyperplastic Human Parathyroid Glands
KINDER BK, DELAHUNT NG, JAMIESON JD, GORELICK FS. Calcium-Calmodulin-Dependent Protein Kinase in Hyperplastic Human Parathyroid Glands. Endocrinology 1987, 120: 170-177. PMID: 3096699, DOI: 10.1210/endo-120-1-170.Peer-Reviewed Original Research