2013
Reduction of Synaptojanin 1 Accelerates Aβ Clearance and Attenuates Cognitive Deterioration in an Alzheimer Mouse Model*
Zhu L, Zhong M, Zhao J, Rhee H, Caesar I, Knight E, Volpicelli-Daley L, Bustos V, Netzer W, Liu L, Lucast L, Ehrlich M, Robakis N, Gandy S, Cai D. Reduction of Synaptojanin 1 Accelerates Aβ Clearance and Attenuates Cognitive Deterioration in an Alzheimer Mouse Model*. Journal Of Biological Chemistry 2013, 288: 32050-32063. PMID: 24052255, PMCID: PMC3814799, DOI: 10.1074/jbc.m113.504365.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsCell Line, TumorDisease Models, AnimalDown-RegulationGene Knockdown TechniquesHippocampusHumansLysosomesMiceMice, TransgenicMutationPeptide FragmentsPhosphatidylinositol 4,5-DiphosphatePhosphoric Monoester HydrolasesPresenilin-1ConceptsAmyloid precursor proteinNovel mechanismSwedish mutant amyloid precursor proteinSynaptojanin 1Aβ clearanceC-terminal fragmentΓ-secretase cleavageMouse modelIntracellular Aβ levelsCellular degradationAlzheimer's Disease Transgenic Mouse ModelFull-length amyloid precursor proteinSYNJ1Cellular clearanceMutant amyloid precursor proteinN2a cellsAlzheimer mouse modelPrecursor proteinTransgenic mouse modelReduced expressionPlaque loadAβ42 levelsAβ levelsTransgenic miceCognitive deteriorationB-Raf and the inhibitors: from bench to bedside
Huang T, Karsy M, Zhuge J, Zhong M, Liu D. B-Raf and the inhibitors: from bench to bedside. Journal Of Hematology & Oncology 2013, 6: 30. PMID: 23617957, PMCID: PMC3646677, DOI: 10.1186/1756-8722-6-30.Peer-Reviewed Original Research
2006
Presenilin-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 NetworkPhospholipase 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 activityOverexpression
2003
Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells
Zhong M, Shen Y, Zheng Y, Joseph T, Jackson D, Foster D. Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells. Biochemical And Biophysical Research Communications 2003, 302: 615-619. PMID: 12615079, DOI: 10.1016/s0006-291x(03)00229-8.Peer-Reviewed Original ResearchConceptsHuman breast cancer cell linesSerum withdrawalBreast cancer cell linesMDA-MB-231 breast cancer cellsMDA-MB-231 cellsPLD activityBreast cancer cellsElevated PLD activityCancer cell linesTyrosine kinaseRat fibroblastsElevated expressionElevated levelsCancer cellsPhospholipase D activityCell linesWithdrawalApoptosisOncogenic signalsUndergo apoptosisD activityCellsFibroblastsApoptotic insultsPhospholipase D
2002
Elevated phospholipase D activity induces apoptosis in normal rat fibroblasts
Zhong M, Joseph T, Jackson D, Beychenok S, Foster D. Elevated phospholipase D activity induces apoptosis in normal rat fibroblasts. Biochemical And Biophysical Research Communications 2002, 298: 474-477. PMID: 12408976, DOI: 10.1016/s0006-291x(02)02495-6.Peer-Reviewed Original ResearchConceptsElevated PLD expressionPLD expressionPhospholipase DRat fibroblastsElevated expressionProtein kinase C deltaNormal rat fibroblastsElevated phospholipase D activityInducible expression systemCytochrome c releaseMitochondrial apoptosis pathwayADP-ribose polymerasePhospholipase D activityC deltaApoptotic insultsC releaseExpression systemTyrosine kinase expressionTransient transfectionTyrosine kinaseApoptosis pathwayCell transformationPLD activityAbsence of serumCaspase-3Downregulating PKC δ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression
Zhong M, Lu Z, Foster D. Downregulating PKC δ provides a PI3K/Akt-independent survival signal that overcomes apoptotic signals generated by c-Src overexpression. Oncogene 2002, 21: 1071-1078. PMID: 11850824, DOI: 10.1038/sj.onc.1205165.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCaspase 9CaspasesCell LineCell Line, TransformedCell SurvivalCulture Media, Serum-FreeCytochrome c GroupDown-RegulationIsoenzymesPhosphatidylinositol 3-KinasesProtein Kinase CProtein Kinase C-deltaProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktProto-Oncogene Proteins pp60(c-src)RatsSignal TransductionTetradecanoylphorbol AcetateConceptsSurvival signalsSerum withdrawalPKC δApoptotic signalsTyrosine kinase c-SrcProtein kinase C δC-Src overexpressionKinase c-SrcCaspase-9 pathwayV-SrcRenders cellsApoptotic phenotypeApoptotic stressC-SrcSurvival pathwaysRat fibroblastsDownregulationApoptosisCellsPathwayOverexpressionPhenotypeFibroblastsSignals
2001
Transformation of Cells Overexpressing a Tyrosine Kinase by Phospholipase D1 and D2
Joseph T, Wooden R, Bryant A, Zhong M, Lu Z, Foster D. Transformation of Cells Overexpressing a Tyrosine Kinase by Phospholipase D1 and D2. Biochemical And Biophysical Research Communications 2001, 289: 1019-1024. PMID: 11741292, DOI: 10.1006/bbrc.2001.6118.Peer-Reviewed Original ResearchConceptsEpidermal growth factor receptorTransformation of cellsTyrosine kinaseElevated tyrosine kinase activityElevated expressionTyrosine kinase activityGTPase cascadeMembrane microdomainsPhospholipase D activityTransform cellsPLD genesGrowth factor receptorC-SrcMitogenic signalsGene productsDownstream targetsKinase activityOncogenic signalingPhospholipase D1PLD2Common genetic alterationsHuman cancersKinaseMalignant phenotypeGenetic alterationsNovel tumor-promoting property of tamoxifen.
Zhong M, Lu Z, Abbas T, Hornia A, Chatakondu K, Barile N, Kaplan P, Foster D. Novel tumor-promoting property of tamoxifen. Molecular Cancer Research 2001, 12: 187-92. PMID: 11331247.Peer-Reviewed Original ResearchConceptsTumor-promoting capabilitiesEstrogen antagonist propertiesEstrogen-mimetic effectsEffect of tamoxifenBreast cancer patientsYears of treatmentTumor-promoting phorbol ester TPATumor-promoting propertiesC-Src overexpressionEndometrial cancerCancer patientsRat fibroblastsTamoxifenPhorbol ester TPA
2000
Phospholipase D and RalA Cooperate with the Epidermal Growth Factor Receptor To Transform 3Y1 Rat Fibroblasts
Lu Z, Hornia A, Joseph T, Sukezane T, Frankel P, Zhong M, Bychenok S, Xu L, Feig L, Foster D. Phospholipase D and RalA Cooperate with the Epidermal Growth Factor Receptor To Transform 3Y1 Rat Fibroblasts. Molecular And Cellular Biology 2000, 20: 462-467. PMID: 10611224, PMCID: PMC85102, DOI: 10.1128/mcb.20.2.462-467.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DivisionCell LineCell Transformation, NeoplasticEnzyme ActivationEpidermal Growth FactorErbB ReceptorsFibroblastsGene ExpressionGenes, DominantGTP PhosphohydrolasesJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein KinasesMutationPhenotypePhospholipase DRal GTP-Binding ProteinsRas ProteinsRatsSignal TransductionTransfectionConceptsEGFR cellsAbsence of EGFEpidermal growth factor receptorGrowth factor receptorRas-dependent activationElevated phospholipase D activityEGF-induced activationOverexpression of PLD1Factor receptorRat fibroblastsDownstream effector moleculesRalA mutantsActivation of PLDPhospholipase D activityJun kinaseSmall GTPaseEGF receptorRalA.PLD activityPhospholipase DRalAEffector moleculesPLD1EGFMitogenic stimuli
1999
Antagonistic Effects of Protein Kinase C α and δ on Both Transformation and Phospholipase D Activity Mediated by the Epidermal Growth Factor Receptor
Hornia A, Lu Z, Sukezane T, Zhong M, Joseph T, Frankel P, Foster D. Antagonistic Effects of Protein Kinase C α and δ on Both Transformation and Phospholipase D Activity Mediated by the Epidermal Growth Factor Receptor. Molecular And Cellular Biology 1999, 19: 7672-7680. PMID: 10523655, PMCID: PMC84804, DOI: 10.1128/mcb.19.11.7672.Peer-Reviewed Original ResearchMeSH KeywordsAcetophenonesAnimalsBenzopyransCarbazolesCell Transformation, NeoplasticCells, CulturedCrosses, GeneticEpidermal Growth FactorErbB ReceptorsIndolesIsoenzymesModels, GeneticMutagenesis, InsertionalPhospholipase DProtein Kinase CProtein Kinase C-alphaProtein Kinase C-deltaRatsRecombinant ProteinsTetradecanoylphorbol Acetate