2017
Bidirectional regulation of Aβ levels by Presenilin 1
Bustos V, Pulina MV, Kelahmetoglu Y, Sinha SC, Gorelick FS, Flajolet M, Greengard P. Bidirectional regulation of Aβ levels by Presenilin 1. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 7142-7147. PMID: 28533411, PMCID: PMC5502639, DOI: 10.1073/pnas.1705235114.Peer-Reviewed Original ResearchConceptsAmyloid precursor proteinAβ levelsΓ-secretase complexAlzheimer's diseasePresenilin 1Pathogenesis of ADAβ peptidesEndogenous kinaseΒ-amyloid peptidePS1 functionIntramembranous proteinsCatalytic subunitΓ-secretase activityPlaque loadC-terminal fragmentAutophagic degradationPotential therapySer367Selective phosphorylationSequential proteolysisTransgenic micePhosphorylationCultured cellsΒ-secretaseDisease
2016
Inhibition of renalase expression and signaling has antitumor activity in pancreatic cancer
Guo X, Hollander L, MacPherson D, Wang L, Velazquez H, Chang J, Safirstein R, Cha C, Gorelick F, Desir GV. Inhibition of renalase expression and signaling has antitumor activity in pancreatic cancer. Scientific Reports 2016, 6: 22996. PMID: 26972355, PMCID: PMC4789641, DOI: 10.1038/srep22996.Peer-Reviewed Original ResearchMeSH KeywordsAdultAgedAged, 80 and overAnimalsAntibodiesApoptosisCarcinoma, Pancreatic DuctalCell Cycle CheckpointsCell Line, TumorFemaleGene Expression Regulation, NeoplasticHumansImmunohistochemistryKaplan-Meier EstimateMaleMice, NudeMiddle AgedMonoamine OxidasePancreatic NeoplasmsPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionXenograft Model Antitumor AssaysConceptsRenalase expressionPancreatic cancerPancreatic ductal adenocarcinoma growthCohort of patientsPancreatic cancer tissuesPancreatic ductal adenocarcinomaPancreatic ductal adenocarcinoma cellsXenograft mouse modelAttractive therapeutic targetDuctal adenocarcinoma cellsTumor cell apoptosisOverall survivalPathogenic roleCell cycle arrestDuctal adenocarcinomaPrognostic makerTumor massMouse modelTherapeutic targetCellular injuryCancer tissuesRenalaseCancerAdenocarcinoma cellsGrowth factor
2011
The vacuolar-ATPase modulates matrix metalloproteinase isoforms in human pancreatic cancer
Chung C, Mader CC, Schmitz J, Atladottir J, Fitchev P, Cornwell M, Koleske AJ, Crawford SE, Gorelick F. The vacuolar-ATPase modulates matrix metalloproteinase isoforms in human pancreatic cancer. Laboratory Investigation 2011, 91: 732-743. PMID: 21339745, PMCID: PMC3084324, DOI: 10.1038/labinvest.2011.8.Peer-Reviewed Original ResearchConceptsPancreatic ductal adenocarcinomaMMP-9 activityHuman pancreatic cancerPancreatic cancerPanIN lesionsHigh-grade PanIN lesionsHuman pancreatic ductal adenocarcinomaPancreatic intraepithelial neoplasmsCancer cellsLow-grade PanIN lesionsMatrix metalloproteinase activationMMP-2 activityPancreatic cancer cellsHuman cancer tissuesShort hairpin RNAPancreatic histologyIntraepithelial neoplasmDuctal adenocarcinomaNormal ductsMMP releaseCancer tissuesMMP-2Metalloproteinase activationInvasive propertiesSpecific MMPs
1993
Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes
Matovcik LM, Haimowitz B, Goldenring JR, Czernik AJ, Gorelick FS. Distribution of calcium/calmodulin-dependent protein kinase II in rat ileal enterocytes. American Journal Of Physiology 1993, 264: c1029-c1036. PMID: 8386447, DOI: 10.1152/ajpcell.1993.264.4.c1029.Peer-Reviewed Original ResearchConceptsProtein kinase IIDependent protein kinase IIKinase IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDependent kinase activityRelative molecular massSpecific peptide inhibitorWide tissue distributionTerminal web regionIntestinal epithelial cellsEpithelial cytoskeletonKinase activityMyosin IISoluble subcellular fractionMolecular massRat ilealRat ileumMultiple substratesEnterocyte cytoskeletonImmunoreactive proteinMajor effectorPeptide inhibitorEpithelial cellsTissue distribution
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
1988
Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum.
Walaas SI, Lai Y, Gorelick FS, DeCamilli P, Moretti M, Greengard P. Cell-specific localization of the alpha-subunit of calcium/calmodulin-dependent protein kinase II in Purkinje cells in rodent cerebellum. Brain Research 1988, 464: 233-42. PMID: 2850084, DOI: 10.1016/0169-328x(88)90029-0.Peer-Reviewed Original ResearchConceptsCalmodulin-dependent protein kinase type IICalcium/calmodulin-dependent protein kinase type IIProtein kinase type IIKinase type IICalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IIDistinct isozymic formsProtein kinase IINormal rat cerebellumPurkinje cellsBeta/betaNon-Purkinje cellsKinase IIAlpha subunitCell-specific localizationRestricted localizationRodent cerebellumIsozymic formsDifferent cellsImmunocytochemical analysisMutant miceSubunitsType IICellsCerebellum