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 arrangementTraffickingAcquisition 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
Protein 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 ResearchMeSH KeywordsAnimalsEndoplasmic ReticulumHormonesHuman Growth HormoneHumansMutationNeurosecretory SystemsProlactinProtein FoldingVasopressins
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 ResearchMeSH KeywordsAnimalsBiological TransportCytoplasmic GranulesEndoplasmic ReticulumGolgi ApparatusHormonesHumansHydrolasesLysosomesNeurosecretory SystemsProteinsConceptsTrans-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 ResearchMeSH KeywordsAnimalsBiological TransportCytoplasmic GranulesEndoplasmic ReticulumGolgi ApparatusHormonesHumansHydrolasesLysosomesNeurosecretory SystemsProteinsConceptsTrans-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
1982
Prolactin: Multiple intracellular processing routes plus several potential mechanisms for regulation
Dannies P. Prolactin: Multiple intracellular processing routes plus several potential mechanisms for regulation. Biochemical Pharmacology 1982, 31: 2845-2849. PMID: 6291547, DOI: 10.1016/0006-2952(82)90253-2.Peer-Reviewed Original ResearchAnimalsBromocriptineCalciumCyclic AMPEndoplasmic ReticulumProlactinRatsThyrotropin-Releasing Hormone