2003
Calcium/calmodulin dependent protein kinase II constitutively binds and regulates the ileal BB Na+/H+ exchanger NHE3
Zizak M, Bartonicek D, Cha B, Murtazina R, Kim J, Lee-Kwon W, Gorelick F, Tse M, Donowitz M. Calcium/calmodulin dependent protein kinase II constitutively binds and regulates the ileal BB Na+/H+ exchanger NHE3. Gastroenterology 2003, 124: a471. DOI: 10.1016/s0016-5085(03)82384-3.Peer-Reviewed Original Research
1996
Co-distribution of calmodulin-dependent protein kinase II and inositol trisphosphate receptors in an apical domain of gastrointestinal mucosal cells.
Matovcik LM, Maranto AR, Soroka CJ, Gorelick FS, Smith J, Goldenring JR. Co-distribution of calmodulin-dependent protein kinase II and inositol trisphosphate receptors in an apical domain of gastrointestinal mucosal cells. Journal Of Histochemistry & Cytochemistry 1996, 44: 1243-1250. PMID: 8918899, DOI: 10.1177/44.11.8918899.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium ChannelsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCell PolarityDigestive SystemFluorescent Antibody Technique, IndirectInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsIntestinal MucosaMaleRabbitsRatsRats, Sprague-DawleyReceptors, Cytoplasmic and NuclearConceptsType 3 InsP3 receptorCaM kinase IICalmodulin-dependent protein kinase IIKinase IIProtein kinase IIInsP3 receptorPotential phosphorylation sitesCalcium/calmodulin-dependent protein kinase IIType 3 inositolPhosphorylation sitesApical domainSubcellular localizationCytoskeletal domainTrisphosphate receptorPancreatic acinar cellsImmunofluorescence microscopyPhysiologic substratesGastrointestinal tissuesRabbit gastric glandsF-actin domainsGastrointestinal mucosal cellsIntestinal enterocytesApical regionAcinar cellsInositol
1995
Ca2+/calmodulin-dependent protein kinase II activation and regulation of adrenal glomerulosa Ca2+ signaling
Fern RJ, Hahm MS, Lu HK, Liu LP, Gorelick FS, Barrett PQ. Ca2+/calmodulin-dependent protein kinase II activation and regulation of adrenal glomerulosa Ca2+ signaling. American Journal Of Physiology 1995, 269: f751-f760. PMID: 8594869, DOI: 10.1152/ajprenal.1995.269.6.f751.Peer-Reviewed Original ResearchConceptsCaMKII activityBovine adrenal glomerulosa cellsDepolarization-induced increaseAdrenal glomerulosa cellsDepolarization-induced Ca2Voltage-gated Ca2Independent CaMKII activityElevated extracellular potassiumDependent protein kinase II (CaMKII) activationCaMKII inhibitor peptideAgonist-induced stimulationAldosterone secretagoguesAngiotensin IIGlomerulosa cellsKinase activityExtracellular potassiumImportance of CaMKIIIntracellular Ca2Dependent protein kinase IIProtein kinase IICell treatmentKN-62Calmodulin antagonistsCell-permeable inhibitorChannel activityCalmodulin-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
1994
Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells.
Matovcik LM, Karapetian O, Czernik AJ, Marino CR, Kinder BK, Gorelick FS. Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells. European Journal Of Cell Biology 1994, 65: 327-40. PMID: 7536673.Peer-Reviewed Original ResearchConceptsClone 9 cellsEndocytic compartmentsPotential substrate proteinsDependent protein kinase IISynapsin ISmall intracellular vesiclesProtein kinase IIRat liver endosomesSubstrate proteinsPhosphorylation sequenceNon-neuronal cellsCLIP-170Intracellular vesiclesKinase IILarge endosomesPostnuclear supernatantEndosomesSensitive compartmentLiver endosomesProteinConfocal microscopyCell linesVesiclesIntestinal enterocytesCompartmentsCalcium/calmodulin-dependent protein kinase-II activation in rat pituitary cells in the presence of thyrotropin-releasing hormone and dopamine
Cui ZJ, Gorelick FS, Dannies PS. Calcium/calmodulin-dependent protein kinase-II activation in rat pituitary cells in the presence of thyrotropin-releasing hormone and dopamine. Endocrinology 1994, 134: 2245-2250. PMID: 8156928, DOI: 10.1210/endo.134.5.8156928.Peer-Reviewed Original ResearchConceptsPulses of TRHPRL releaseCaM kinase IIPituitary cellsAnterior pituitary cellsCaM kinase II activityThyrotropin-releasing hormoneRat pituitary cellsCalmodulin-dependent protein kinase II activationCalcium/calmodulin-dependent protein kinase II (CaMKII) activationKinase IICalcium/calmodulin-dependent protein kinase IIPretreatment of cellsCalmodulin-dependent protein kinase IIBasal valuesKinase II activityLack of responsivenessKinase activityIntracellular Ca2TRHProtein kinase IIRat lactotrophsDopamineTRH pulsesLactotrophsCell cycle-dependent and kinase-specific regulation of the apical Na/H exchanger and the Na,K-ATPase in the kidney cell line LLC-PK1 by calcitonin.
Chakraborty M, Chatterjee D, Gorelick FS, Baron R. Cell cycle-dependent and kinase-specific regulation of the apical Na/H exchanger and the Na,K-ATPase in the kidney cell line LLC-PK1 by calcitonin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 2115-2119. PMID: 8134357, PMCID: PMC43320, DOI: 10.1073/pnas.91.6.2115.Peer-Reviewed Original ResearchConceptsNa/H exchangerApical Na/H exchangerH exchangerAmiloride-sensitive 22Na uptakeCell line LLC-PK1Potent natriuretic effectKidney tubulesNa transport systemLLC-PK1K-ATPaseCa/calmodulin-dependent protein kinase IINatriuretic effectSerum calciumCalmodulin-dependent protein kinase IIProximal kidney tubuleCalcitoninCell cycle-specific activationProtein kinase IIReabsorptionTubulesSame cellsKinase IICellsApical exchangerS phase
1993
Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes
Matovcik LM, Haimowitz B, Goldenring JR, Czernik AJ, Gorelick FS. Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes. American Journal Of Physiology 1993, 264: c1029-c1036. PMID: 8386447, DOI: 10.1152/ajpcell.1993.264.4.c1029.Peer-Reviewed Original ResearchConceptsProtein kinase IIDependent protein kinase IIKinase IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDependent kinase activityRelative molecular massSpecific peptide inhibitorWide tissue distributionTerminal web regionIntestinal epithelial cellsEpithelial cytoskeletonKinase activityMyosin IISoluble subcellular fractionMolecular massRat ilealRat ileumMultiple substratesEnterocyte cytoskeletonImmunoreactive proteinMajor effectorPeptide inhibitorEpithelial cellsTissue distribution
1992
Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I
Benfenati F, Valtorta F, Rubenstein J, Gorelick F, Greengard P, Czernik A. Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature 1992, 359: 417-420. PMID: 1328883, DOI: 10.1038/359417a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesChromatography, High Pressure LiquidElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicMolecular Sequence DataPhosphorylationProtein KinasesRatsReceptors, NeurotransmitterSubstrate SpecificitySynapsinsSynaptic VesiclesConceptsDependent protein kinase IIProtein kinase IIC-terminal regionKinase IISynapsin ISynaptic vesicle-associated phosphoproteinsAmino-terminal regionCarboxy-terminal regionKinase functionRegulatory domainProtein componentsMembrane phospholipidsProteinPhosphoproteinVesiclesEnzymeRegionBindingPhospholipidsDomainSynaptic
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
1989
Presence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain
Walaas S, Gorelick F, Greengard P. Presence of calcium/calmodulin‐dependent protein Kinase II in Nerve terminals of rat brain. Synapse 1989, 3: 356-362. PMID: 2545012, DOI: 10.1002/syn.890030409.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinase IICalmodulin-dependent protein kinase IISubstantia nigraProtein kinase IINerve terminalsRat brainSynapsin INerve terminal markersLesion-induced degenerationLesion-induced changesCalcium/calmodulin-dependent protein kinase type IIPrevious immunocytochemical studiesKinase IIStriatonigral tractCorticostriatal tractPresynaptic terminalsNeuronal populationsCalmodulin-dependent protein kinase type IIMammalian brainCell bodiesImmunocytochemical studyTerminal markersBrainNeostriatumLesions
1988
Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals.
Gorelick FS, Wang JK, Lai Y, Nairn AC, Greengard P. Autophosphorylation and activation of Ca2+/calmodulin-dependent protein kinase II in intact nerve terminals. Journal Of Biological Chemistry 1988, 263: 17209-17212. PMID: 2846557, DOI: 10.1016/s0021-9258(19)77816-8.Peer-Reviewed Original ResearchConceptsDependent protein kinase IIKinase IIAlpha subunitProtein kinase IIKinase II activityTwo-dimensional phosphopeptide mapsII activityState of phosphorylationAutophosphorylation mechanismThreonine residuesPhosphothreonine contentPhosphopeptide mapsTransient phosphorylationIndependent speciesPhosphoserine contentIntact nerve terminalsBeta subunitEnhanced phosphorylationSubunitsPhosphorylationAutophosphorylationIntact synaptosomesBasal incubation conditionsPhosphopeptidesDepolarization of synaptosomesCell-specific localization of the α-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum
Walaas S, Lai Y, Gorelick F, DeCamilli P, Moretti M, Greengard P. Cell-specific localization of the α-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum. Brain Research 1988, 4: 233-242. DOI: 10.1016/0169-328x(88)90029-0.Peer-Reviewed Original ResearchCalmodulin-dependent protein kinase type IICalcium/calmodulin-dependent protein kinase type IIProtein kinase type IIKinase type IIΑ-subunitΒ-subunitCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDistinct isozymic formsProtein kinase IINormal rat cerebellumNon-Purkinje cellsKinase IICell-specific localizationRestricted localizationRodent cerebellumIsozymic formsPurkinje cellsDifferent cellsImmunocytochemical analysisMutant miceSubunitsCellsCerebellar mutantsType IICell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum.
Walaas SI, Lai Y, Gorelick FS, DeCamilli P, Moretti M, Greengard P. Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum. Brain Research 1988, 464: 233-42. PMID: 2850084, DOI: 10.1016/0169-328x(88)90029-0.Peer-Reviewed Original ResearchConceptsCalmodulin-dependent protein kinase type IICalcium/calmodulin-dependent protein kinase type IIProtein kinase type IIKinase type IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDistinct isozymic formsProtein kinase IINormal rat cerebellumPurkinje cellsBeta/betaNon-Purkinje cellsKinase IIAlpha subunitCell-specific localizationRestricted localizationRodent cerebellumIsozymic formsDifferent cellsImmunocytochemical analysisMutant miceSubunitsType IICellsCerebellumCa2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity.
Thiel G, Czernik AJ, Gorelick F, Nairn AC, Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 6337-6341. PMID: 2842767, PMCID: PMC281965, DOI: 10.1073/pnas.85.17.6337.Peer-Reviewed Original ResearchConceptsBeta/beta' subunitsAlpha subunitThr-286Beta subunitDependent protein kinase IIProtein kinase IIAutophosphorylation sitesThreonine residuesMajor phosphopeptideNaDodSO4/PAGEPhosphorylated residuesCyanogen bromide peptidesConsensus sequenceKinase IIIndependent activityThermolytic phosphopeptidesPrimary structureGas-phase Edman degradationGeneration of Ca2Edman degradationAutophosphorylationSubunitsThreonine-286Amino acidsAsp-XaaDevelopment of Secretagogue Responsiveness in the Pancreas
Jamieson JD, Gorelick FS, Chang A. Development of Secretagogue Responsiveness in the Pancreas. Scandinavian Journal Of Gastroenterology 1988, 23: 98-103. PMID: 2852401, DOI: 10.3109/00365528809095920.Peer-Reviewed Original ResearchConceptsSecretory pathwaySecretory proteinsPancreatic acinar cellsEpithelial cell polarityDependent protein kinase IIRegulated secretory pathwayConstitutive secretory pathwayAcinar cellsProtein kinase IICell polarityMembrane proteinsPhosphorylated substratesRegulated secretionBasolateral domainCell biologyPlasmalemmal domainsPlasma membraneKinase IISecond messengerSecretagogue responsivenessFunctional specializationProteinEpithelial cellsPathwayZymogen granules