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 varietyMechanism
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 arrangementTrafficking
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
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 ResearchMeSH KeywordsAnimalsCell LineCircular DichroismHumansProlactinProtein BindingProtein ConformationProtein FoldingZinc