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 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, 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
Aggregation 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
Concentrating 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
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 factor
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
Cell Biology of Secretion
Dannies P. Cell Biology of Secretion. 1998, 3-22. DOI: 10.1002/cphy.cp070101.Peer-Reviewed Original ResearchDocking/fusionCorrect membraneEndocrine cellsMembrane buddingCell biologyMembrane fusionIntracellular transportSynaptic vesiclesDense core granulesSecretory granulesVesiclesEndocytosisNeurotransmitter releaseReconstituted systemExocytosisCore granulesCellsFusion mechanismClathrinYeastCalcium dependenceBuddingBiologyGranulesFusionStabilization 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: 2727-2733. DOI: 10.1210/en.139.6.2727.Peer-Reviewed Original ResearchSecretory granule membranesEpidermal growth factorGTP-binding protein Rab3Granule membranesSecretory granule accumulationSecretory granule compartmentAssociated with secretory granule membranesTyrosine phosphatase-like proteinPhosphatase-like proteinGH4C1 cellsProlactin storageGH4C1 rat pituitary tumor cellsIncreased transcriptionPulse-chase procedureMature formRat pituitary tumor cellsSecretory granulesGranule compartmentGranule accumulationTreated cellsGrowth factorUntreated cellsPituitary tumor cellsMessenger RNAICA512
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
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
1990
Comparison of the Regulation of Carboxypeptidase E and Prolactin in GH4C1 Cells, a Rat Pituitary Cell Line
Flicker L, Reaves B, Das B, Dannies P. Comparison of the Regulation of Carboxypeptidase E and Prolactin in GH4C1 Cells, a Rat Pituitary Cell Line. Neuroendocrinology 1990, 51: 658-663. PMID: 2114002, DOI: 10.1159/000125407.Peer-Reviewed Original ResearchConceptsGH4C1 cellsPituitary cell lineEpidermal growth factorNM thyrotropin-releasing hormoneCarboxypeptidase ECell linesCPE activityGrowth factorThyrotropin-releasing hormoneLevels of prolactinCPE mRNAAnterior pituitary cell lineIntracellular levelsSecretory granulesRat anterior pituitary cell lineRat pituitary cell lineGH4C1 cell lineProlactinControl valuesIntracellular prolactinTreatmentNorthern blot analysisBlot analysisEstradiolInsulin
1986
Hormonal Induction of Secretory Granules in a Pituitary Tumor Cell Line*
SCAMMELL J, BURRAGE T, DANNIES P. Hormonal Induction of Secretory Granules in a Pituitary Tumor Cell Line*. Endocrinology 1986, 119: 1543-1548. PMID: 3530721, DOI: 10.1210/endo-119-4-1543.Peer-Reviewed Original ResearchConceptsGH4C1 cellsIntracellular PRLSecretory granulesCombination of estradiolNumber of granulesPituitary tumor cell linePRL accumulationHormone regimenTumor cell strainsEpidermal growth factorHormone treatmentTumor cell linesPRLGrowth factorControl levelsOccasional granulesCell linesHormonal inductionGHCell strainsCellsGranule numberTreatmentCellular contentStorage granules
1984
Spiperone: evidence for uptake into secretory granules.
Dannies P, Rudnick M, Fishkes H, Rudnick G. Spiperone: evidence for uptake into secretory granules. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 1867-1870. PMID: 6584920, PMCID: PMC345023, DOI: 10.1073/pnas.81.6.1867.Peer-Reviewed Original ResearchConceptsSerotonin receptorsSecretory granulesRat pituitary tumor cellsMicroM reserpinePlatelet dense granulesPituitary tumor cellsDopamine antagonistsIntracellular storage organellesSpiperoneTumor cellsSerotonin transportDense granulesBiogenic amine transportReceptorsCell strainsDopamineEquimolar concentrationsSpecific ligandsAmine transportStorage organellesPlasma membrane transport systemsReserpineAntagonistMinNeurons