1997
Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert D. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6210-6215. PMID: 9177196, PMCID: PMC21028, DOI: 10.1073/pnas.94.12.6210.Peer-Reviewed Original ResearchMeSH KeywordsAdultCalcium-Binding ProteinsCalnexinCalreticulinCell DifferentiationCells, CulturedCoculture TechniquesEndoplasmic ReticulumEnzyme PrecursorsHumansInfant, NewbornKineticsMelanocytesMelanomaMolecular ChaperonesMolecular WeightMonophenol MonooxygenasePhenotypeRibonucleoproteinsSkin NeoplasmsTime FactorsTumor Cells, CulturedConceptsEndoplasmic reticulumNormal melanocytesER chaperone calnexinMelanin synthesisMalignant melanocytesMelanoma cellsChaperone bindingAberrant retentionChaperone calnexinGolgi compartmentSubcellular localizationAmelanotic melanoma cell lineKey enzymeMelanoma cell linesMaturation of tyrosinaseAmelanotic melanoma cellsKinetics of synthesisInhibitor sensitivityDedifferentiated phenotypeProteolytic degradationCell linesProteasome inhibitorsEnzymeProteasomeImmature forms
1996
Characterization and Subcellular Localization of Human Pmel 17/silver, a 100-kDa (Pre)Melanosomal Membrane Protein Associated With 5,6,-Dihydroxyindole-2-Carboxylic Acid (DHICA) Converting Activity
Lee Z, Hou L, Moellmann G, Kuklinska E, Antol K, Fraser M, Halaban R, Kwon B. Characterization and Subcellular Localization of Human Pmel 17/silver, a 100-kDa (Pre)Melanosomal Membrane Protein Associated With 5,6,-Dihydroxyindole-2-Carboxylic Acid (DHICA) Converting Activity. Journal Of Investigative Dermatology 1996, 106: 605-610. PMID: 8617992, DOI: 10.1111/1523-1747.ep12345163.Peer-Reviewed Original ResearchConceptsPmel 17Baculovirus expression vectorCo-precipitated proteinsElectron transfer chainPigmentation lociCytosolic vesiclesInsect cellsComplexed proteinsSubcellular localizationPolyclonal antibodiesProtein AssociatedMelanin biosynthesisPigment cellsExpression vectorPrimary structureTransfer chainApproximate molecular sizeHuman melanoma cellsProteinNatural proteinsOxidoreductive enzymesMelanoma cellsUltrastructural locationElectron microscopic cytochemistryCells
1991
Fibroblast Growth Factors in Normal and Malignant Melanocytesa
Halaban R, Funasaka Y, Lee P, Rubin J, Ron D, Birnbaum D. Fibroblast Growth Factors in Normal and Malignant Melanocytesa. Annals Of The New York Academy Of Sciences 1991, 638: 232-243. PMID: 1723854, DOI: 10.1111/j.1749-6632.1991.tb49034.x.Peer-Reviewed Original Research
1988
Tyrosinases of murine melanocytes with mutations at the albino locus.
Halaban R, Moellmann G, Tamura A, Kwon BS, Kuklinska E, Pomerantz SH, Lerner AB. Tyrosinases of murine melanocytes with mutations at the albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7241-7245. PMID: 3140237, PMCID: PMC282161, DOI: 10.1073/pnas.85.19.7241.Peer-Reviewed Original ResearchConceptsAlbino locusTrans-Golgi networkWild-type melanocytesWild-type strainAbnormal posttranslational modificationsSynthesis of melaninDiminished pigmentationStructural genePosttranslational modificationsMurine melanocytesLocus mutantsKey enzymeLevels of mRNAMutantsKinetics of activationProteolytic cleavageUnstable enzymeEnzymeLociMelanocytesReduced levelsMutationsConfer susceptibilityTyrosinaseLittle enzyme