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 spectroscopyAggregationAggregatesCellsAccumulation
2001
Misfolded 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 eventProtein folding and deficiencies caused by dominant-negative mutants of hormones
Dannies P. Protein folding and deficiencies caused by dominant-negative mutants of hormones. Vitamins & Hormones 2000, 58: 1-26. PMID: 10668393, DOI: 10.1016/s0083-6729(00)58019-4.Peer-Reviewed Original Research
1999
Protein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting*
Dannies P. Protein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting*. Endocrine Reviews 1999, 20: 3-21. PMID: 10047971, DOI: 10.1210/edrv.20.1.0354.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSecretory granule proteinsMembrane proteinsGranule proteinsSecretory granule membrane proteinsPossible recognition siteGranule membrane proteinSecretory granule membranesThree-dimensional electron microscopyTransport vesiclesCell biologyConstitutive pathwayRegulated pathwayMembrane lipidsGranule formationGranule membranesSorting mechanismHormone aggregationProteinDense core granulesProcess of aggregationRecognition sitesSame cellsNeuroendocrine cellsSecretory granulesProtein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting
Dannies P. Protein Hormone Storage in Secretory Granules: Mechanisms for Concentration and Sorting. Endocrine Reviews 1999, 20: 3-21. DOI: 10.1210/er.20.1.3.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSecretory granule proteinsMembrane proteinsGranule proteinsSecretory granule membrane proteinsPossible recognition siteGranule membrane proteinSecretory granule membranesThree-dimensional electron microscopyTransport vesiclesCell biologyConstitutive pathwayRegulated pathwayMembrane lipidsGranule formationGranule membranesSorting mechanismHormone aggregationProteinDense core granulesProcess of aggregationRecognition sitesSame cellsNeuroendocrine cellsSecretory granules
1998
Stabilization of the receptor protein tyrosine phosphatase-like protein ICA512 in GH4C1 cells upon treatment with estradiol, insulin, and epidermal growth factor.
Lee M, Dirkx R, Solimena M, Dannies P. Stabilization of the receptor protein tyrosine phosphatase-like protein ICA512 in GH4C1 cells upon treatment with estradiol, insulin, and epidermal growth factor. Endocrinology 1998, 139: 2727-33. PMID: 9607778, DOI: 10.1210/endo.139.6.6039.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantigensCytoplasmic GranulesDrug StabilityEpidermal Growth FactorEstradiolImmunoblottingImmunologic TechniquesInsulinMembrane ProteinsMicroscopy, ConfocalPeptide FragmentsPrecipitin TestsProtein PrecursorsProtein Tyrosine PhosphatasesRatsReceptor-Like Protein Tyrosine Phosphatases, Class 8Time FactorsTumor Cells, Cultured
1997
Editorial: A New Releasing Factor? with Biotechnology and a Little Bit of Luck
Dannies P. Editorial: A New Releasing Factor? with Biotechnology and a Little Bit of Luck. Endocrinology 1997, 138: 5085-5086. PMID: 9389485, DOI: 10.1210/endo.138.12.5710.Peer-Reviewed Original ResearchInefficient secretion of human H27A-prolactin, a mutant that does not bind Zn2+.
Sun Z, Lee M, Rhee H, Arrandale J, Dannies P. Inefficient secretion of human H27A-prolactin, a mutant that does not bind Zn2+. Endocrinology 1997, 11: 1544-51. PMID: 9280069, DOI: 10.1210/mend.11.10.0002.Peer-Reviewed Original Research
1996
Properties of human prolactin (PRL) and H27A-PRL, a mutant that does not bind Zn++.
Sun Z, Li P, Dannies P, Lee J. Properties of human prolactin (PRL) and H27A-PRL, a mutant that does not bind Zn++. Endocrinology 1996, 10: 265-71. PMID: 8833655, DOI: 10.1210/mend.10.3.8833655.Peer-Reviewed Original ResearchKN-62, a calcium/calmodulin-dependent protein kinase II inhibitor, inhibits high potassium-stimulated prolactin secretion and intracellular calcium increases in anterior pituitary cells
Cui Z, Hidaka H, Dannies P. KN-62, a calcium/calmodulin-dependent protein kinase II inhibitor, inhibits high potassium-stimulated prolactin secretion and intracellular calcium increases in anterior pituitary cells. Biochimica Et Biophysica Acta 1996, 1310: 343-347. PMID: 8599613, DOI: 10.1016/0167-4889(95)00170-0.Peer-Reviewed Original ResearchMeSH Keywords1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCells, CulturedEnzyme InhibitorsFemaleIsoquinolinesKineticsPiperazinesPituitary Gland, AnteriorPotassiumPotassium ChlorideProlactinRatsRats, Sprague-DawleyThyrotropin-Releasing HormoneTime FactorsConceptsAnterior pituitary cellsProlactin secretionCalcium/calmodulin-dependent protein kinase IIPituitary cellsCalmodulin-dependent protein kinase IIKN-04KN-62Rat anterior pituitary cellsVoltage-dependent calcium channelsProtein kinase IICalmodulin-dependent protein kinase II inhibitorKCl-stimulated increasesIntracellular calcium increaseCalcium/calmodulin-dependent protein kinase II inhibitorKinase II inhibitorCalcium channelsCalcium increaseIntracellular Ca2Kinase IISecretionInhibits activationII inhibitorsIC50InhibitorsCells
1995
Biological activity and immunological reactivity of human prolactin mutants
Rhee H, Sun Z, Kim S, Goffin V, Martial J, Dannies P. Biological activity and immunological reactivity of human prolactin mutants. Endocrinology 1995, 136: 4990-4995. PMID: 7588233, DOI: 10.1210/endo.136.11.7588233.Peer-Reviewed Original ResearchConceptsSerine 90Cystine loopBiological activityRat pituitary cell lineHuman PRLPituitary cell lineWild typeCertain fishPRL-3MutantsTryptophan fluorescenceCell linesMutationsFishT mutationCell assayPRL storageImmunological reactivityImmunological propertiesSerineConcentration of ureaActivityConservationSpacial requirementsLoopLack of correlation of distribution of prolactin (PRL) charge isoforms with induction of PRL storage
Mastro R, Dannies P. Lack of correlation of distribution of prolactin (PRL) charge isoforms with induction of PRL storage. Endocrinology 1995, 136: 69-74. PMID: 7828559, DOI: 10.1210/endo.136.1.7828559.Peer-Reviewed Original ResearchConceptsEpidermal growth factorNormal lactotrophsGH4C1 cellsGrowth factorForms of PRLFemale rat pituitary glandsNM epidermal growth factorRat pituitary glandDense core granulesRat pituitary tumor cellsPRL storagePituitary tumor cellsNM estradiolTotal PRLPituitary glandPRLTumor cellsCore granulesInsulinNM insulinLack of correlationLactotrophs
1994
Inhibition of rat prolactin (PRL) storage by coexpression of human PRL.
Arrandale J, Dannies P. Inhibition of rat prolactin (PRL) storage by coexpression of human PRL. Endocrinology 1994, 8: 1083-1090. PMID: 7997234, DOI: 10.1210/mend.8.8.7997234.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAsparagineBiological TransportCell CompartmentationCytoplasmic GranulesEpidermal Growth FactorEstradiolGene ExpressionHumansInsulinModels, MolecularPituitary NeoplasmsProlactinProtein ConformationRatsRecombinant Fusion ProteinsSerineSpecies SpecificityTransfectionTumor Cells, CulturedConceptsHuman PRLRat PRLGH4C1 cellsReceptor-mediated mechanismNM epidermal growth factorSecretory granulesNM estradiolDense-core secretory granulesEpidermal growth factorHormone treatmentPRL storageProlactin storagePRLGrowth factorNM insulinMore ratsUntransfected cellsRatsRegulated pathwayControl culturesCellsInhibitionMarked specificityRegulation of Parathyroid Hormone‐Related Peptide Gene Expression by Estrogen in GH4C1 Rat Pituitary Cells Has the Pattern of a Primary Response Gene
Holt E, Lu C, Dreyer B, Dannies P, Broadus A. Regulation of Parathyroid Hormone‐Related Peptide Gene Expression by Estrogen in GH4C1 Rat Pituitary Cells Has the Pattern of a Primary Response Gene. Journal Of Neurochemistry 1994, 62: 1239-1246. PMID: 8133258, DOI: 10.1046/j.1471-4159.1994.62041239.x.Peer-Reviewed Original ResearchConceptsGH4C1 rat pituitary cellsRat pituitary cellsPituitary cellsParathyroid hormone-related peptide gene expressionPTHrP mRNA expressionPrimary response geneParathyroid hormone-related peptide genePTHrP gene transcriptionPeptide gene expressionResponse genesPharmacological controlMRNA responseMRNA expressionTransient increaseGrowth factorGene transcriptionPlateau responsePeak response