2015
Early to Late Endosome Trafficking Controls Secretion and Zymogen Activation in Rodent and Human Pancreatic Acinar Cells
Messenger SW, Thomas D, Cooley MM, Jones EK, Falkowski MA, August BK, Fernandez LA, Gorelick FS, Groblewski GE. Early to Late Endosome Trafficking Controls Secretion and Zymogen Activation in Rodent and Human Pancreatic Acinar Cells. Cellular And Molecular Gastroenterology And Hepatology 2015, 1: 695-709. PMID: 26618189, PMCID: PMC4657148, DOI: 10.1016/j.jcmgh.2015.08.002.Peer-Reviewed Original ResearchEarly endosomesRecycling endosomesEndosomal traffickingLate endosomesDominant-negative Rab11a mutantCellular damage responseAssociated membrane proteinLysosome-Associated Membrane ProteinsPIKfyve inhibitionApical traffickingPIKfyve activityEndosomal systemCCK-8Damage responseMembrane proteinsPlasma membraneAcinar cellsPIKfyvePharmacological inhibitorsPancreatic acinar cellsTraffickingEndosomesZymogen activationAdenoviral overexpressionCellular death
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
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
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