2010
Anti-tumor effects of adenovirus containing human growth hormone sequences in a mouse model of human ovarian cancer
Zhu Y, Fariña JB, Meshack S, Santoveña A, Patel S, Oliva A, Llabrés M, Hodsdon ME, Booth CJ, Dannies PS. Anti-tumor effects of adenovirus containing human growth hormone sequences in a mouse model of human ovarian cancer. Endocrine 2010, 37: 430-439. PMID: 20960164, DOI: 10.1007/s12020-010-9333-5.Peer-Reviewed Original ResearchConceptsHuman ovarian cancerOvarian cancerPeritoneal cavityMouse modelTumor cell injectionImmunodeficient SCID miceGrowth hormone releaseHuman ovarian cancer cellsAnti-tumor effectsOvarian cancer cellsReplication-deficient adenovirusLower survival rateLiver metastasesMedian survivalControl miceLung metastasesIntraperitoneal injectionPeritoneal fibrosisLiver toxicitySCID miceHormone releaseHepatocellular changesSurvival rateCell injectionGrowth hormonePharmacokinetics analysis of sustained release hGH biodegradable implantable tablets using a mouse model of human ovarian cancer
Santoveña A, Fariña JB, Llabrés M, Zhu Y, Dannies P. Pharmacokinetics analysis of sustained release hGH biodegradable implantable tablets using a mouse model of human ovarian cancer. International Journal Of Pharmaceutics 2010, 388: 175-180. PMID: 20060456, DOI: 10.1016/j.ijpharm.2009.12.054.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell ProliferationDelayed-Action PreparationsDisease Models, AnimalDrug CarriersDrug ImplantsDrug StabilityFemaleHuman Growth HormoneHumansLactic AcidLikelihood FunctionsMiceMice, SCIDOvarian NeoplasmsPolyglycolic AcidPolylactic Acid-Polyglycolic Acid CopolymerSurvival RateTabletsTime FactorsConceptsSerum levelsSurvival timeMouse modelOvarian cancer mouse modelHormone serum levelsImmunodeficient female micePopulation pharmacokinetic modelHuman ovarian cancer cellsHuman ovarian cancerCancer mouse modelEffect of hGHOvarian cancer cellsFemale miceOvarian cancerHormone releaseOrbital vesselsTumoral cell proliferationPeritoneal cavityPharmacokinetic analysisHigh doseHormone loadSustained release devicesPharmacokinetic modelCancer cellsPharmacokinetic study
2004
Aggregation and Lack of Secretion of Most Newly Synthesized Proinsulin in Non-β-Cell Lines
Zhu YL, Abdo A, Gesmonde JF, Zawalich KC, Zawalich W, Dannies PS. Aggregation and Lack of Secretion of Most Newly Synthesized Proinsulin in Non-β-Cell Lines. Endocrinology 2004, 145: 3840-3849. PMID: 15117881, DOI: 10.1210/en.2003-1512.Peer-Reviewed Original ResearchIs there structural specificity in the reversible protein aggregates that are stored in secretory granules?
Keeler C, Hodsdon ME, Dannies PS. Is there structural specificity in the reversible protein aggregates that are stored in secretory granules? Journal Of Molecular Neuroscience 2004, 22: 43-49. PMID: 14742909, DOI: 10.1385/jmn:22:1-2:43.Peer-Reviewed Original ResearchConceptsSecretory granule proteinsMembrane proteinsGranule functionGranule proteinsAmino acid residuesSecretory granulesExcess membraneProtein aggregatesSecretory proteinsAcid residuesProteinStructural specificityResiduesSurface motifsGranulesAggregation processMembraneReversible aggregationSpecificityMotifNMR spectroscopyAggregationAggregatesCellsAccumulationPeptide Hormones, Segregation Mechanism
Dannies P. Peptide Hormones, Segregation Mechanism. 2004, 573-574. DOI: 10.1016/b0-12-475570-4/01000-3.Peer-Reviewed Original ResearchPeptide Hormones, Subcellular Structure
Dannies P. Peptide Hormones, Subcellular Structure. 2004, 575-578. DOI: 10.1016/b0-12-475570-4/01001-5.Peer-Reviewed Original ResearchPeptide Hormones, Regulated Secretion
Dannies P. Peptide Hormones, Regulated Secretion. 2004, 561-565. DOI: 10.1016/b0-12-475570-4/00998-7.Peer-Reviewed Original ResearchMembrane fusionSecretory granulesMembrane fusion processVesicular trafficSecretory pathwayProtein hormonesRegulated secretionPlasma membraneLarge dense-core vesiclesDense-core vesiclesVesiclesNeuroendocrine cellsExtracellular spaceCytosolic Ca2Release of hormonesPeptide hormonesMembraneGranulesCellsFusionYeastFusion processCytosolCa2Hormone
2003
Manipulating the Reversible Aggregation of Protein Hormones in Secretory Granules
Dannies P. Manipulating the Reversible Aggregation of Protein Hormones in Secretory Granules. BioDrugs 2003, 17: 315-324. PMID: 14498762, DOI: 10.2165/00063030-200317050-00002.Peer-Reviewed Original ResearchConceptsSecretory granule proteinsSecretory granule formationCell typesSecretory granulesGranule formationGranule proteinsDense-core secretory granulesSecretory cell typesFormation of aggregatesMembrane-permeable chelatorCorrect assemblyProtein aggregationProtein aggregatesProtein interfacesSecretory proteinsMonomeric proteinInsoluble aggregatesNative conformationProtein hormonesExact residuesMacromolecular crowdingProtein preparationsProteinHuman prolactinNeuroendocrine cellsThe Tertiary Structure and Backbone Dynamics of Human Prolactin
Keeler C, Dannies PS, Hodsdon ME. The Tertiary Structure and Backbone Dynamics of Human Prolactin. Journal Of Molecular Biology 2003, 328: 1105-1121. PMID: 12729745, DOI: 10.1016/s0022-2836(03)00367-x.Peer-Reviewed Original ResearchConceptsFour-dimensional heteronuclear NMR spectroscopyTertiary structureBackbone dynamicsFour-helical bundleN-terminal loopSecretory granulesHeteronuclear NMR spectroscopyExtrapituitary prolactinNMR relaxation phenomenaThird helixFirst helixSecond helixGolgi complexFunctional bindingHematopoietic cytokinesBundle topologyDiscrete structural differencesFemale reproductive systemHuman prolactinProlactin receptorReversible oligomerizationHelixShort loopsReproductive systemGrowth factor
2002
New GH-1 gene mutations: expanding the spectrum of causes of isolated growth hormone deficiency.
Mullis PE, Deladoëy J, Dannies PS. New GH-1 gene mutations: expanding the spectrum of causes of isolated growth hormone deficiency. Journal Of Pediatric Endocrinology And Metabolism 2002, 15 Suppl 5: 1301-10. PMID: 12510984.Peer-Reviewed Original ResearchConceptsSecretory pathwayDNA/RNA levelIGHD type IIGH-1 gene alterationsCellular biological mechanismsBasis of inheritanceDistinct familial typesPhenotype resultsGH-1 gene mutationsMolecular analysisGenetic causeBiological mechanismsRNA levelsGene alterationsGene mutationsPathwaySame familyType IIFamilyMutationsInheritanceFamilial typePossible mechanismWide varietyMechanismProlonged Retention after Aggregation into Secretory Granules of Human R183H-Growth Hormone (GH), a Mutant that Causes Autosomal Dominant GH Deficiency Type II
Zhu YL, Conway-Campbell B, Waters MJ, Dannies PS. Prolonged Retention after Aggregation into Secretory Granules of Human R183H-Growth Hormone (GH), a Mutant that Causes Autosomal Dominant GH Deficiency Type II. Endocrinology 2002, 143: 4243-4248. PMID: 12399418, DOI: 10.1210/en.2002-220575.Peer-Reviewed Original ResearchAggregation of Human Wild-Type and H27A-Prolactin in Cells and in Solution: Roles of Zn2+, Cu2+, and pH
Sankoorikal B, Zhu Y, Hodsdon M, Lolis E, Dannies P. Aggregation of Human Wild-Type and H27A-Prolactin in Cells and in Solution: Roles of Zn2+, Cu2+, and pH. Endocrinology 2002, 143: 1302-1309. DOI: 10.1210/en.143.4.1302.Peer-Reviewed Original ResearchAtT20 cellsSecretory granulesFormation of secretory granulesHuman prolactinZn2+-binding siteTransfected AtT20 cellsCores of secretory granulesHuman wild-typeWild-type prolactinAcidic pHCOS cellsRecombinant human prolactinIntracellular compartmentsWild-typeBinding sitesRat prolactinCu2+Neutral pHProlactinRatio of Zn2Concentrations of hormonesAtT20Cells
2001
A serum prolactin-binding protein: implications for growth hormone
Dannies P. A serum prolactin-binding protein: implications for growth hormone. Trends In Endocrinology And Metabolism 2001, 12: 427-428. PMID: 11701331, DOI: 10.1016/s1043-2760(01)00497-0.Peer-Reviewed Original ResearchMisfolded growth hormone causes fragmentation of the Golgi apparatus and disrupts endoplasmic reticulum-to-Golgi traffic.
Graves T, Patel S, Dannies P, Hinkle P. Misfolded growth hormone causes fragmentation of the Golgi apparatus and disrupts endoplasmic reticulum-to-Golgi traffic. Journal Of Cell Science 2001, 114: 3685-94. PMID: 11707520, DOI: 10.1242/jcs.114.20.3685.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAnti-Bacterial AgentsBiomarkersCarrier ProteinsChromatinCoatomer ProteinCOS CellsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGolgi ApparatusGreen Fluorescent ProteinsHeat-Shock ProteinsHuman Growth HormoneHumansIndicators and ReagentsLuminescent ProteinsMembrane ProteinsMicrotubule-Organizing CenterMicrotubulesMolecular ChaperonesProlactinProtein FoldingProtein TransportQb-SNARE ProteinsReceptors, Thyrotropin-Releasing HormoneTunicamycinConceptsWild-type growth hormoneUnfolded protein responseGolgi trafficEndoplasmic reticulumBeta-COPProtein responseGolgi apparatusWild-type human growth hormonePlasma membrane proteinsGolgi marker beta-COPMicrotubule-organizing centerAmino acids 32Thyrotropin-releasing hormone receptorGolgi fragmentationMembrane proteinsSubcellular localizationGolgi markersCOS7 cellsBiP mRNASecretory proteinsReceptor traffickingHost cellsMembrinMicrotubular arrangementTraffickingConcentrating hormones into secretory granules: layers of control
Dannies P. Concentrating hormones into secretory granules: layers of control. Molecular And Cellular Endocrinology 2001, 177: 87-93. PMID: 11377824, DOI: 10.1016/s0303-7207(01)00437-3.Peer-Reviewed Original ResearchConceptsTransport of proteinsCisternal maturation modelSecretory granule proteinsSecretory granulesLayer of controlSecretory pathwayGolgi complexSoluble proteinSmall vesiclesGranule proteinsProteinPassive aggregationMaturation modelProtein hormonesSelective retentionGranulesMajor roleAggregationVesiclesHormonePathwaySortingCellsAcquisition of Lubrol Insolubility, a Common Step for Growth Hormone and Prolactin in the Secretory Pathway of Neuroendocrine Cells*
Lee M, Zhu Y, Chang J, Dannies P. Acquisition of Lubrol Insolubility, a Common Step for Growth Hormone and Prolactin in the Secretory Pathway of Neuroendocrine Cells*. Journal Of Biological Chemistry 2001, 276: 715-721. PMID: 11024038, DOI: 10.1074/jbc.m008530200.Peer-Reviewed Original ResearchAnimalsAnti-Bacterial AgentsBrefeldin AChloroquineCOS CellsDinitrobenzenesEndoplasmic ReticulumEpidermal Growth FactorEstradiolHuman Growth HormoneHydrogen-Ion ConcentrationInsulinMacrolidesMutationPituitary GlandPolyethylene GlycolsProlactinProtein TransportRatsSecretory VesiclesSolubilitySubstrate SpecificityTumor Cells, CulturedUltracentrifugation
2000
Accumulation of Synaptosomal-Associated Protein of 25 kDa (SNAP-25) and Other Proteins Associated with the Secretory Pathway in GH4C1 Cells Upon Treatment with Estradiol, Insulin, and Epidermal Growth Factor
Lee M, Zhu Y, Sun Z, Rhee H, Jeromin A, Roder J, Dannies P. Accumulation of Synaptosomal-Associated Protein of 25 kDa (SNAP-25) and Other Proteins Associated with the Secretory Pathway in GH4C1 Cells Upon Treatment with Estradiol, Insulin, and Epidermal Growth Factor. Endocrinology 2000, 141: 3485-3492. PMID: 10965922, DOI: 10.1210/endo.141.9.7647.Peer-Reviewed Original ResearchConceptsSecretory pathwayEpidermal growth factorSynaptotagmin IIICyclophilin BGH4C1 cellsInduction of proteinsGrowth factorGlucose-regulated protein 94Rat pituitary GH4C1 cellsSecretory granulesSynaptosomal-associated proteinMessenger RNA accumulationMembrane proteinsPituitary GH4C1 cellsSynaptosomal associated proteinRNA accumulationPlasma membraneProtein AssociatedSpecific proteinsSynaptotagmin IHormone-treated cellsSNAP-25Protein 94Secretory granule accumulationCoordinate eventAccumulation of Synaptosomal-Associated Protein of 25 kDa (SNAP-25) and Other Proteins Associated with the Secretory Pathway in GH4C1 Cells Upon Treatment with Estradiol, Insulin, and Epidermal Growth Factor*
Lee M, Zhu Y, Sun Z, Rhee H, Jeromin A, Roder J, Dannies P. Accumulation of Synaptosomal-Associated Protein of 25 kDa (SNAP-25) and Other Proteins Associated with the Secretory Pathway in GH4C1 Cells Upon Treatment with Estradiol, Insulin, and Epidermal Growth Factor*. Endocrinology 2000, 141: 3485-3492. DOI: 10.1210/en.141.9.3485.Peer-Reviewed Original ResearchSNAP-25Secretory pathwaySynaptosomal-associated proteinSynaptotagmin IIIEpidermal growth factorCyclophilin BTreatment of GH4C1 cellsSecretory granulesSecretory granule accumulationGH4C1 cellsGlucose-regulated protein 94Rat pituitary GH4C1 cellsHormone-treated cellsInduction of proteinsPituitary GH4C1 cellsSynaptotagmin IRNA accumulationPlasma membraneSynaptotagminMessenger RNA accumulationInduced accumulationCell surfaceGranule accumulationProteinGrowth factorArgl83His, a New Mutational "Hot-Spot" in the Growth Hormone Gene
Wajnrajch M, Gertner J, Mullis P, Deladoey J, Cogan J, Lekhakula S, Kim S, Dannies P, Saenger P, Moshang T, Phillips J, Leibel R. Argl83His, a New Mutational "Hot-Spot" in the Growth Hormone Gene. International Journal On Disability And Human Development 2000, 1: 125-136. DOI: 10.1515/ijdhd.2000.1.3.125.Peer-Reviewed Original ResearchAutosomal Dominant Growth Hormone (GH) Deficiency Type II: The Del32–71-GH Deletion Mutant Suppresses Secretion of Wild-Type GH
Lee M, Wajnrajch M, Kim S, Plotnick L, Wang J, Gertner J, Leibel R, Dannies P. Autosomal Dominant Growth Hormone (GH) Deficiency Type II: The Del32–71-GH Deletion Mutant Suppresses Secretion of Wild-Type GH. Endocrinology 2000, 141: 883-890. PMID: 10698162, DOI: 10.1210/endo.141.3.7380.Peer-Reviewed Original ResearchConceptsWild-type GHSecretory pathway functionNeuroendocrine cell lineGH deficiency type IISuppression of accumulationPathway functionTransient transfectionIntracellular stabilityCHO cellsAutosomal dominant formCell linesDecreased stabilityNormal allelePosttranslational effectGeneral suppressionCoexpressionProtein