2019
Recent Insights Into the Pathogenic Mechanism of Pancreatitis: Role of Acinar Cell Organelle Disorders.
Gukovskaya AS, Gorelick FS, Groblewski GE, Mareninova OA, Lugea A, Antonucci L, Waldron RT, Habtezion A, Karin M, Pandol SJ, Gukovsky I. Recent Insights Into the Pathogenic Mechanism of Pancreatitis: Role of Acinar Cell Organelle Disorders. Pancreas 2019, 48: 459-470. PMID: 30973461, PMCID: PMC6461375, DOI: 10.1097/mpa.0000000000001298.Peer-Reviewed Original ResearchConceptsOrganelle dysfunctionCell death responseSecretion of proteinsAcinar cell homeostasisOrganelle disordersNascent proteinsDysfunctional organellesDeath responseAccessory proteinsVesicular compartmentsEndosomal pathwayCell homeostasisAcute pancreatitisEndoplasmic reticulumProtein synthesisCells triggersPancreatic acinar cellsLethal inflammatory diseaseDigestive enzymesCell constituentsRecent insightsDistinct mechanismsProteinOrganellesAcinar cell injury
2015
Chronic Nicotine Exposure In Vivo and In Vitro Inhibits Vitamin B1 (Thiamin) Uptake by Pancreatic Acinar Cells
Srinivasan P, Thrower EC, Loganathan G, Balamurugan AN, Subramanian VS, Gorelick FS, Said HM. Chronic Nicotine Exposure In Vivo and In Vitro Inhibits Vitamin B1 (Thiamin) Uptake by Pancreatic Acinar Cells. PLOS ONE 2015, 10: e0143575. PMID: 26633299, PMCID: PMC4669105, DOI: 10.1371/journal.pone.0143575.Peer-Reviewed Original ResearchConceptsHuman pancreatic acinar cellsPancreatic acinar cellsNormal cellular functionThiamin uptakeTHTR-1Chronic exposureMurine pancreatic acinar cellsThiamin uptake processCellular functionsAcinar cellsThiamin pyrophosphokinaseMolecular biologyThiamin transporter-1Mouse pancreatic acinar cellsSpecific carrier-mediated processMitochondrial dysfunctionTHTR-2Chronic nicotine exposureTransporter 1Oxidative stressProteinExpressionNicotine impairsUptake processNicotine exposure
2012
Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell
Gorelick F, Jamieson J. Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell. 2012, 1341-1360. DOI: 10.1016/b978-0-12-382026-6.00049-x.Peer-Reviewed Original ResearchProtein synthesisZymogen granulesAcinar cellsSecretion of enzymesStructure-function relationshipsNascent proteinsVesicular transportCell signalingEnzyme precursorsGolgi complexEndoplasmic reticulumPancreatic acinar cellsDigestive enzymesEnzymeModel systemExport protein synthesisVectorial mannerApical regionProteinCellsHormonal routesGranulesDigestionDietary proteinExocytosis
2002
COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle
Siddiqi SA, Gorelick FS, Mahan JT, Mansbach CM. COPII proteins are required for Golgi fusion but not for endoplasmic reticulum budding of the pre-chylomicron transport vesicle. Journal Of Cell Science 2002, 116: 415-427. PMID: 12482926, DOI: 10.1242/jcs.00215.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesApolipoprotein B-48Apolipoproteins BCells, CulturedChylomicronsCOP-Coated VesiclesEndoplasmic ReticulumEpithelial CellsGolgi ApparatusIntestinal AbsorptionIntestinal MucosaLipid MetabolismMaleMembrane FusionMicroscopy, ElectronMonomeric GTP-Binding ProteinsProtein TransportRatsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsConceptsPre-chylomicron transport vesicleCOPII proteinsEndoplasmic reticulumTransport vesiclesBudding of vesiclesSucrose density centrifugationNascent proteinsCargo proteinsProtein vesiclesMembrane proteinsGolgi complexProteinase K treatmentProteinSec24VesiclesGolgiSar1Intestinal GolgiDensity centrifugationReticulumK treatmentTriton XSec13/31Rbet1COPII
1999
Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat
Shugrue C, Kolen E, Peters H, Czernik A, Kaiser C, Matovcik L, Hubbard A, Gorelick F. Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat. Journal Of Cell Science 1999, 112: 4547-4556. PMID: 10574704, PMCID: PMC5567750, DOI: 10.1242/jcs.112.24.4547.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell LineCloning, MolecularCOP-Coated VesiclesDNA, ComplementaryFungal ProteinsGTPase-Activating ProteinsHumansMembrane ProteinsMolecular Sequence DataNuclear Pore Complex ProteinsPhosphoproteinsRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidVesicular Transport ProteinsConceptsMammalian orthologuesCOPII coatSequential column chromatographyTwo-hybrid analysisIntracellular vesicular traffickingSmall punctate structuresVesicle-associated proteinLiver cDNA libraryCultured cell linesRat liver cDNA libraryVesicular buddingVesicular traffickingNovel proteinSignificant homologyTarget membraneCDNA libraryPunctate structuresSec13pSec31pIntact cellsP137ProteinOrthologuesCell linesColumn chromatography
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 enterocytesCompartments
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
1991
Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor
Klueppelberg UG, Gates LK, Gorelick FS, Miller LJ. Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor. Journal Of Biological Chemistry 1991, 266: 2403-2408. PMID: 1989991, DOI: 10.1016/s0021-9258(18)52258-4.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCarbacholCell FractionationChromatography, AffinityChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelEnzyme ActivationKineticsMalePancreasPhosphorylationProtein Kinase CRatsRats, Inbred StrainsReceptors, CholecystokininSincalideSolubilityTetradecanoylphorbol AcetateConceptsC activationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsProtein kinase C activationPlasma membrane glycoproteinsPhosphorylated MrKinase C activationSulfate-polyacrylamide gelsSerine residuesRegulated mannerAffinity-labeled proteinsMembrane glycoproteinsPhosphorylationReceptor proteinProteinNative formATP poolAffinity resinLectin affinity chromatographyConcentration-dependent mannerDirect activationPancreatic cholecystokinin receptorSubsequent solubilizationReceptorsActivation
1990
Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland
Marino CR, Castle JD, Gorelick FS. Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland. American Journal Of Physiology 1990, 259: g70-g77. PMID: 1695488, DOI: 10.1152/ajpgi.1990.259.1.g70.Peer-Reviewed Original ResearchConceptsSecretory granule membrane proteinsIntegral membrane proteinsMembrane proteinsGranule membrane proteinProtein phosphorylation eventsGranule membrane fractionExocrine secretory granulesPhosphorylation eventsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisRat parotid glandRegulated phosphorylationSulfate-polyacrylamide gel electrophoresisSitu phosphorylationIntact cellsMembrane fractionTime-dependent mannerPhosphorylationProteinSecretory granule fractionParotid lobulesGel electrophoresisProtein antiserumSecretory granulesPhosphoprotein
1988
Development 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
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 process