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 ResearchMeSH KeywordsAcinar CellsAcute DiseaseAutophagyEndoplasmic ReticulumEndosomesHomeostasisHumansLysosomesPancreatitisSecretory VesiclesConceptsOrganelle 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
2010
Adaptive Unfolded Protein Response Attenuates Alcohol-Induced Pancreatic Damage
Lugea A, Tischler D, Nguyen J, Gong J, Gukovsky I, French SW, Gorelick FS, Pandol SJ. Adaptive Unfolded Protein Response Attenuates Alcohol-Induced Pancreatic Damage. Gastroenterology 2010, 140: 987-997.e8. PMID: 21111739, PMCID: PMC3057335, DOI: 10.1053/j.gastro.2010.11.038.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalAnimalsApoptosisApoptosis Regulatory ProteinsDisease Models, AnimalDNA-Binding ProteinsEndoplasmic ReticulumEthanolMaleMiceMice, Inbred BALB CMice, KnockoutPancreas, ExocrinePancreatitis, AlcoholicProtein Disulfide-IsomerasesRatsRats, WistarRegulatory Factor X Transcription FactorsStress, PhysiologicalTissue Culture TechniquesTranscription FactorsUnfolded Protein ResponseX-Box Binding Protein 1ConceptsProtein disulfide isomeraseX-box binding protein 1ER stressUPR regulatorOxidation of PDIER protein foldingDisulfide bond formationBinding protein 1Reticulum stress responseDisulfide isomeraseProtein foldingER functionProapoptotic signalsStress responseHuman disordersXBP1 deficiencyAcinar cell deathER dysfunctionCell deathXBP1 levelsAlcohol-induced ER stressPDI levelsProtein 1UPRWild-type miceMolecular and cellular mechanisms of pancreatic injury
Thrower EC, Gorelick FS, Husain SZ. Molecular and cellular mechanisms of pancreatic injury. Current Opinion In Gastroenterology 2010, 26: 484-489. PMID: 20651589, PMCID: PMC3023172, DOI: 10.1097/mog.0b013e32833d119e.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisEndoplasmic ReticulumHumansPancreasPancreatitis, Acute NecrotizingPancreatitis, ChronicTrypsinTrypsinogenConceptsPancreatic injuryCellular mechanismsFibroblast growth factor 21Antiapoptotic effectGrowth factor 21Ameliorate injuryEndoplasmic reticulum stressChronic pancreatitisFactor 21Immune cellsExendin-4Endogenous trypsin inhibitorBile acidsDisease severityInjuryPancreatitisCausative factorsSensitizing factorTrypsinogen activationProtein CReticulum stressTrypsinogen mutationsBcl-2Intracellular eventsUpregulation of proteinsAlcohol Abuse, Endoplasmic Reticulum Stress and Pancreatitis
Pandol SJ, Gorelick FS, Gerloff A, Lugea A. Alcohol Abuse, Endoplasmic Reticulum Stress and Pancreatitis. Digestive Diseases 2010, 28: 776-782. PMID: 21525762, PMCID: PMC3211518, DOI: 10.1159/000327212.Peer-Reviewed Original ResearchMeSH KeywordsAlcoholismEndoplasmic ReticulumHumansPancreatitisSmokingStress, PhysiologicalUnfolded Protein ResponseConceptsX-box binding protein 1Alcohol abuseChronic pancreatitisEthanol feedingUnfolded protein responseER stressSignificant pathological responseAcinar cellsAfrican American ethnicityEndoplasmic reticulum stressPancreatic manifestationAlcoholic pancreatitisAdaptive unfolded protein responseMinority of individualsChronic inflammationMost individualsPathological responseCommon causePancreatic diseaseApparent diseasePancreatitisBinding protein 1Heavy drinkersExocrine pancreasPancreas
2007
Development and Physiological Regulation of Intestinal Lipid Absorption. II. Dietary lipid absorption, complex lipid synthesis, and the intracellular packaging and secretion of chylomicrons
Mansbach CM, Gorelick F. Development and Physiological Regulation of Intestinal Lipid Absorption. II. Dietary lipid absorption, complex lipid synthesis, and the intracellular packaging and secretion of chylomicrons. AJP Gastrointestinal And Liver Physiology 2007, 293: g645-g650. PMID: 17627968, DOI: 10.1152/ajpgi.00299.2007.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChylomicronsDietary FatsEndoplasmic ReticulumHumansIntestinal AbsorptionLipid MetabolismTriglyceridesConceptsLipid absorptionSecretion of chylomicronsEpidemic of obesityDietary lipid absorptionDietary fat absorptionIntestinal lipid absorptionFatty acid transportersFatty acid uptakeDiscovery of familiesLiver fatty acidEndoplasmic reticulumAcid transportersClinical importanceFat absorptionPhysiological functionsIntracellular packagingComplex lipid synthesisLipid synthesisChylomicronsAcid uptakePhysiological regulationRecent advancesAcyltransferasesGolgiObesity
2006
The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle*
Siddiqi SA, Siddiqi S, Mahan J, Peggs K, Gorelick FS, Mansbach CM. The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle*. Journal Of Biological Chemistry 2006, 281: 20974-20982. PMID: 16735505, PMCID: PMC2833420, DOI: 10.1074/jbc.m601401200.Peer-Reviewed Original ResearchVesicle-associated membrane protein 7 is expressed in intestinal ER
Siddiqi SA, Mahan J, Siddiqi S, Gorelick FS, Mansbach CM. Vesicle-associated membrane protein 7 is expressed in intestinal ER. Journal Of Cell Science 2006, 119: 943-950. PMID: 16495485, PMCID: PMC2828367, DOI: 10.1242/jcs.02803.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesBiological TransportChylomicronsEndoplasmic ReticulumGolgi ApparatusIn Vitro TechniquesIntestine, SmallRatsR-SNARE ProteinsTriglycerides
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
2001
Exiting the endoplasmic reticulum
Gorelick F, Shugrue C. Exiting the endoplasmic reticulum. Molecular And Cellular Endocrinology 2001, 177: 13-18. PMID: 11377815, DOI: 10.1016/s0303-7207(01)00438-5.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumNascent proteinsCOPII coatCoat protein complexCis-Golgi regionVesicular transport processesDifferent adaptor proteinsTrans-Golgi regionSite of synthesisCOPII vesiclesNascent vesiclesVesicle biogenesisCargo selectionCOPII proteinsExtracellular destinationsCOPI coatomerGolgi traffickingBudding vesicleCytoplasmic coatRetrograde trafficProtein complexesAdaptor proteinDonor membranesLysosome biogenesisTarget membrane