2003
Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*
Francis E, Wang N, Parag H, Halaban R, Hebert DN. Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*. Journal Of Biological Chemistry 2003, 278: 25607-25617. PMID: 12724309, DOI: 10.1074/jbc.m303411200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalnexinCalreticulinCells, CulturedCentrifugation, Density GradientCHO CellsCricetinaeCross-Linking ReagentsDimerizationDogsElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumLectinsMelanocytesMembrane GlycoproteinsMiceMicrosomesMonophenol MonooxygenaseMutationOxidoreductasesPancreasPlasmidsPolysaccharidesProtein BindingProtein BiosynthesisProtein FoldingProtein TransportProteinsRabbitsSucroseTime FactorsTranscription, GeneticTrypsinConceptsMelanocyte-specific factorsSemipermeabilized cellsEndoplasmic reticulum retentionLectin chaperones calnexinMelanocyte-specific proteinsTyrosinase-related protein 1Wild-type tyrosinaseSynthesis of melaninChaperone interactionsChaperone calnexinTyrosinase maturationMouse melanocytesTrypsin-resistant stateProtein 1Human tyrosinaseTranslation systemOligomerizationPersistent interactionsMaturationMelanocytesTyrosinaseCellsCalnexinMisfoldingER
2002
COMMENTARY Pigmentation in Melanomas: Changes Manifesting Underlying Oncogenic and Metabolic Activities
Halaban R. COMMENTARY Pigmentation in Melanomas: Changes Manifesting Underlying Oncogenic and Metabolic Activities. Oncology Research Featuring Preclinical And Clinical Cancer Therapeutics 2002, 13: 3-8. PMID: 12201672, DOI: 10.3727/096504002108747908.Peer-Reviewed Original ResearchConceptsMelanocyte-specific gene expressionTranscription factor MITFDownregulation of tyrosinaseEpigenetic levelV-ATPaseRate-limiting enzymeTranscriptional activityGene expressionAcidified microenvironmentsAmelanotic melanoma cellsC-MycActivity of tyrosinaseEnhanced glycolysisMelanin synthesisExtracellular acidificationMelanoma tumorsTYR activityMelanoma cellsMetabolic activityPigmentationAnaerobic conditionsTyrosinase activityMetastatic melanocytic lesionsMetabolic changesTyrosinase
1990
Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity.
Halaban R, Moellmann G. Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 4809-4813. PMID: 1693779, PMCID: PMC54207, DOI: 10.1073/pnas.87.12.4809.Peer-Reviewed Original ResearchConceptsPigmentation genesRapid proteolytic degradationMelanosomal glycoproteinLocus proteinBrown locusCatalase BB mutationsProteolytic degradationB locusMelanogenic activityGenesMelanin precursorsLociProteinMutationsGlycoproteinCatalase activityTyrosinaseHydrogen peroxideHydroperoxidaseMelanogenesisGp75ActivityMurinePigmentation
1989
Molecular basis of mouse Himalayan mutation
Kwon B, Halaban R, Chintamaneni C. Molecular basis of mouse Himalayan mutation. Biochemical And Biophysical Research Communications 1989, 161: 252-260. PMID: 2567165, DOI: 10.1016/0006-291x(89)91588-x.Peer-Reviewed Original ResearchConceptsAmino acid 420Histidine residuesAmino acidsTemperature-sensitive tyrosinaseCDNA libraryHimalayan miceMouse tyrosinaseInteresting mutantsNucleotide sequenceB proteinMolecular basisTyrosinase geneTyrosinase cDNAArginine residuesTyrosinase moleculesHuman tyrosinaseG changeResiduesMutationsTyrosinaseMutantsCDNAGenesMiceTyrosinase inhibitors
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
1987
Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus.
Kwon BS, Haq AK, Pomerantz SH, Halaban R. Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 7473-7477. PMID: 2823263, PMCID: PMC299318, DOI: 10.1073/pnas.84.21.7473.Peer-Reviewed Original ResearchConceptsCDNA clonesMelanocyte cDNA libraryRelated mRNA speciesHuman tyrosinaseAmino acid sequenceSouthern blot analysisStructural geneCDNA libraryNucleotide sequenceMRNA speciesAcid sequenceGlycosylation sitesCDNA insertDeletion mutationsCell typesAmino acidsCopper bindingBlot analysisClonesMalignant melanocytesLociSequenceTyrosinaseApproximate lengthKilobases
1983
Regulation of tyrosinase in human melanocytes grown in culture.
Halaban R, Pomerantz S, Marshall S, Lambert D, Lerner A. Regulation of tyrosinase in human melanocytes grown in culture. Journal Of Cell Biology 1983, 97: 480-488. PMID: 6411733, PMCID: PMC2112541, DOI: 10.1083/jcb.97.2.480.Peer-Reviewed Original ResearchConceptsHuman melanocytesApparent molecular weightMalignant human melanocytesTyrosinase activityMajor biochemical eventsExpression of tyrosinaseSynthesis of melaninRegulation of tyrosinasePosttranslational modificationsImmunoprecipitation experimentsO-glycosylationBiochemical eventsNormal melanocytesMelanocytesMolecular weightProteinEnzymeTyrosinaseTunicamycinAbundanceActivityRegulationHigh levelsLow levelsCulture