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
Is 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
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 Research
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 roleAggregationVesiclesHormonePathwaySortingCells
2000
Autosomal 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 suppressionCoexpressionProteinProtein 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
1997
Inefficient 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 Research
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 requirementsLoop
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 specificity
1993
Rapid stimulation of rhodamine 123 efflux from multidrug-resistant KB cells by progesterone
Jancis E, Hong-xing C, Carbone R, Hochberg R, Dannies P. Rapid stimulation of rhodamine 123 efflux from multidrug-resistant KB cells by progesterone. Biochemical Pharmacology 1993, 46: 1613-1619. PMID: 7902090, DOI: 10.1016/0006-2952(93)90331-p.Peer-Reviewed Original ResearchConceptsRhodamine 123 effluxMultidrug resistance pumpRhodamine 123Efflux of daunomycinRapid stimulationMultidrug-resistant KB cellsAbsence of progesteroneNon-genomic mechanismsCause of retentionKB cellsMicroM progesteroneProgesteroneCarcinoma cellsPump activityActive steroidsMCF7 cellsStimulationIntracellular bindingEffluxCellsMitochondrial dyeDesoxycorticosteronePromegestoneVerapamilTestosterone
1991
Regulation of prolactin storage
Reaves B, Dannies P. Regulation of prolactin storage. Cell Biochemistry And Biophysics 1991, 19: 109. PMID: 1726881, DOI: 10.1007/bf02989884.Peer-Reviewed Original Research