2006
Phospholipase D1 corrects impaired βAPP trafficking and neurite outgrowth in familial Alzheimer’s disease-linked presenilin-1 mutant neurons
Cai D, Zhong M, Wang R, Netzer WJ, Shields D, Zheng H, Sisodia SS, Foster DA, Gorelick FS, Xu H, Greengard P. Phospholipase D1 corrects impaired βAPP trafficking and neurite outgrowth in familial Alzheimer’s disease-linked presenilin-1 mutant neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 1936-1940. PMID: 16449385, PMCID: PMC1413666, DOI: 10.1073/pnas.0510710103.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkOverexpression of PLD1Mutant neuronsPhospholipase D1Beta-amyloid precursor proteinIntracellular traffickingPS1-deficient cellsPLD enzymatic activityTherapeutic targetNeuronal functionPS1 mutationsOverexpression of WTBetaAPPPrecursor proteinMutant cellsSubcellular localizationNeurite outgrowthPLD1 activitySurface deliveryNeuronsOutgrowth capacityCellsTraffickingEnzymatic activityOverexpressionPresenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation
Cai D, Netzer WJ, Zhong M, Lin Y, Du G, Frohman M, Foster DA, Sisodia SS, Xu H, Gorelick FS, Greengard P. Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 1941-1946. PMID: 16449386, PMCID: PMC1413665, DOI: 10.1073/pnas.0510708103.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesCell LineEndopeptidasesGene Expression RegulationHumansMembrane ProteinsMiceMice, KnockoutPhospholipase DPresenilin-1Protein BindingProtein Processing, Post-TranslationalProtein TransportTrans-Golgi Network
2005
Zymogen activation in a reconstituted pancreatic acinar cell system
Thrower EC, de Villalvilla A, Kolodecik TR, Gorelick FS. Zymogen activation in a reconstituted pancreatic acinar cell system. AJP Gastrointestinal And Liver Physiology 2005, 290: g894-g902. PMID: 16339296, PMCID: PMC2830560, DOI: 10.1152/ajpgi.00373.2005.Peer-Reviewed Original Research
2001
Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment.
Bustos R, Kolen E, Braiterman L, Baines A, Gorelick F, Hubbard A. Synapsin I is expressed in epithelial cells: localization to a unique trans-Golgi compartment. Journal Of Cell Science 2001, 114: 3695-704. PMID: 11707521, DOI: 10.1242/jcs.114.20.3695.Peer-Reviewed Original ResearchConceptsSynapsin ITrans-Golgi compartmentSynaptic vesicle exocytosisProtein kinase ANon-neuronal cell linesBrain synapsin IEpithelial cellsNorthern blot analysisTrafficking pathwaysVesicle exocytosisVesicular compartmentsKinase AMyosin IIGolgi complexLimited proteolysisAnti-synapsin antibodiesPre-synaptic terminalsPeptide mapsBlot analysisCell linesCompartmentsCellsNeural tissueLiver cellsCytoskeleton
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
1998
Codistribution of TAP and the granule membrane protein GRAMP-92 in rat caerulein-induced pancreatitis
Otani T, Chepilko S, Grendell J, Gorelick F. Codistribution of TAP and the granule membrane protein GRAMP-92 in rat caerulein-induced pancreatitis. American Journal Of Physiology 1998, 275: g999-g1009. PMID: 9815030, DOI: 10.1152/ajpgi.1998.275.5.g999.Peer-Reviewed Original ResearchConceptsAcinar cell compartmentNumber of vesiclesRecycling endosomesSupranuclear compartmentPancreatic acinar cellsTime-dependent mannerProcessing siteCell compartmentTrypsinogen processingPhysiological levelsZymogen granulesImmunofluorescence studiesCaerulein-induced pancreatitisAcinar cellsActivation peptideTrypsinogen activation peptidePathological activationCompartmentsActivation
1995
Effect of cerulein hyperstimulation on the paracellular barrier of rat exocrine pancreas
Fallon M, Gorelick F, Anderson J, Mennone A, Saluja A, Steer M. Effect of cerulein hyperstimulation on the paracellular barrier of rat exocrine pancreas. Gastroenterology 1995, 108: 1863-1872. PMID: 7539388, DOI: 10.1016/0016-5085(95)90151-5.Peer-Reviewed Original Research
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
Scientific advances in cystic fibrosis
Marino C, Gorelick F. Scientific advances in cystic fibrosis. Gastroenterology 1992, 103: 681-693. PMID: 1378805, DOI: 10.1016/0016-5085(92)90866-w.Peer-Reviewed Original Research
1991
Localization of the cystic fibrosis transmembrane conductance regulator in pancreas.
Marino CR, Matovcik LM, Gorelick FS, Cohn JA. Localization of the cystic fibrosis transmembrane conductance regulator in pancreas. Journal Of Clinical Investigation 1991, 88: 712-716. PMID: 1713921, PMCID: PMC295422, DOI: 10.1172/jci115358.Peer-Reviewed Original ResearchConceptsCF transmembrane conductance regulatorCystic fibrosisTransmembrane conductance regulatorCFTR peptidesPancreatic secretory functionDouble-label immunofluorescence studiesConductance regulatorDuct epithelial cellsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorPancreatic insufficiencyIntralobular duct cellsSecretory functionHuman pancreasCFTR moleculesChloride transportMonoclonal antibodiesApical domainDuct cellsAntibodiesEpithelial cellsAcinar cellsCFTR proteinImmunofluorescence studiesProtein products
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 preparationsRegulated 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