2014
Lactate Reduces Liver and Pancreatic Injury in Toll-Like Receptor– and Inflammasome-Mediated Inflammation via GPR81-Mediated Suppression of Innate Immunity
Hoque R, Farooq A, Ghani A, Gorelick F, Mehal WZ. Lactate Reduces Liver and Pancreatic Injury in Toll-Like Receptor– and Inflammasome-Mediated Inflammation via GPR81-Mediated Suppression of Innate Immunity. Gastroenterology 2014, 146: 1763-1774. PMID: 24657625, PMCID: PMC4104305, DOI: 10.1053/j.gastro.2014.03.014.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory AgentsArrestinsBeta-Arrestin 2Beta-ArrestinsCarrier ProteinsCell LineCeruletideChemical and Drug Induced Liver InjuryCytoprotectionDisease Models, AnimalDose-Response Relationship, DrugDown-RegulationGalactosamineHumansImmunity, InnateInflammasomesInjections, IntraperitonealInterleukin-1betaLipopolysaccharidesLiverMacrophagesMaleMiceMice, Inbred C57BLMonocytesNF-kappa BNLR Family, Pyrin Domain-Containing 3 ProteinPancreasPancreatitisReceptors, G-Protein-CoupledRNA InterferenceRNA, Small InterferingSignal TransductionSodium LactateToll-Like Receptor 4Toll-Like ReceptorsTransfectionConceptsToll-like receptorsRelease of IL1βAdministration of lipopolysaccharideOrgan injuryNF-κBCaspase-1TLR inductionAcute pancreatitisPyrin domain-containing protein 3Administration of lactatePromising immunomodulatory therapyAcute liver injuryAcute organ injuryMacrophages of miceDomain-containing protein 3Production of IL1βRAW 264.7 cellsConcentration of lactateAcute hepatitisImmunomodulatory therapyImmune hepatitisPancreatic injuryLactate receptorLiver injuryNLRP3 inflammasome
2011
TLR9 and the NLRP3 Inflammasome Link Acinar Cell Death With Inflammation in Acute Pancreatitis
Hoque R, Sohail M, Malik A, Sarwar S, Luo Y, Shah A, Barrat F, Flavell R, Gorelick F, Husain S, Mehal W. TLR9 and the NLRP3 Inflammasome Link Acinar Cell Death With Inflammation in Acute Pancreatitis. Gastroenterology 2011, 141: 358-369. PMID: 21439959, PMCID: PMC3129497, DOI: 10.1053/j.gastro.2011.03.041.Peer-Reviewed Original ResearchMeSH KeywordsAcute DiseaseAnimalsAnti-Inflammatory AgentsApoptosisApoptosis Regulatory ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCaspase 1CeruletideCytoskeletal ProteinsDisease Models, AnimalDNAInflammasomesInterleukin-1MacrophagesMaleMiceMice, Inbred C57BLMice, KnockoutNecrosisNeutrophil InfiltrationNLR Family, Pyrin Domain-Containing 3 ProteinPancreasPancreatitisPneumoniaProtein PrecursorsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X7RNA, MessengerSeverity of Illness IndexSignal TransductionTaurolithocholic AcidToll-Like Receptor 9ConceptsToll-like receptor 9Acute pancreatitisWild-type miceAcinar cell deathPancreatic edemaTaurolithocholic acidDamage-associated molecular pattern receptorsResident immune cellsCell deathImmune cell populationsDevelopment of inflammationInitiation of inflammationCell populationsNew therapeutic strategiesMolecular pattern receptorsDAMP receptorsLung inflammationInflammatory infiltrateTLR9 expressionImmune cellsPancreatic necrosisReceptor 9TLR9 antagonistInflammasome activationPurinergic receptors
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
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
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