2004
Novel tyramide‐based tyrosinase assay for the detection of melanoma cells in cytological preparations
Angeletti C, Khomitch V, Halaban R, Rimm DL. Novel tyramide‐based tyrosinase assay for the detection of melanoma cells in cytological preparations. Diagnostic Cytopathology 2004, 31: 33-37. PMID: 15236262, DOI: 10.1002/dc.20051.Peer-Reviewed Original ResearchCarbohydrates act as sorting determinants in ER-associated degradation of tyrosinase
Svedine S, Wang T, Halaban R, Hebert DN. Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. Journal Of Cell Science 2004, 117: 2937-2949. PMID: 15161941, DOI: 10.1242/jcs.01154.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalnexinCarbohydrate MetabolismCells, CulturedEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGlucoseHeat-Shock ProteinsMannoseMelanocytesMiceMolecular ChaperonesMonophenol MonooxygenaseMutationProteasome Endopeptidase ComplexProtein Disulfide-IsomerasesProtein TransportConceptsLectin chaperonesMutant tyrosinaseEndoplasmic reticulum (ER) quality control machineryQuality control machineryProtein disulfide isomeraseDegradation of tyrosinaseERAD substratesChaperone interactionsNon-native substratesER organizationProtein maturationER retentionER lumenDisulfide isomeraseAberrant proteinsProteasomal degradationGlucose trimmingProtein degradationProtein aggregatesTyrosinase degradationSubsequent degradationChaperonesIntact melanocytesMaturation processProteasome
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
Coexpression of Wild-Type Tyrosinase Enhances Maturation of Temperature-Sensitive Tyrosinase Mutants
Halaban R, Cheng E, Hebert DN. Coexpression of Wild-Type Tyrosinase Enhances Maturation of Temperature-Sensitive Tyrosinase Mutants. Journal Of Investigative Dermatology 2002, 119: 481-488. PMID: 12190874, DOI: 10.1046/j.1523-1747.2002.01824.x.Peer-Reviewed Original ResearchMeSH KeywordsAlbinism, OculocutaneousAnimalsCells, CulturedDihydroxyphenylalanineEnzyme StabilityGlycosylationHumansMiceMonophenol MonooxygenaseMutationPigmentationTemperatureTyrosineConceptsWild-type proteinTyrosinase mutantsMutant proteinsGlycosylation-deficient mutantsGlycosylation-deficient formsOculocutaneous albinism 1Wild-type tyrosinaseDevelopment of pigmentsDifferent mutant allelesType I membraneActivity-dependent mannerNonpermissive temperatureMutant allelesEndoplasmic reticulumTypes of mutationsMutantsFunction mutationsCarbohydrate processingMelanin synthesisProteinCoexpressionMelanocytesTyrosinase activityMutationsMaturationAbnormal Acidification of Melanoma Cells Induces Tyrosinase Retention in the Early Secretory Pathway*
Halaban R, Patton RS, Cheng E, Svedine S, Trombetta ES, Wahl ML, Ariyan S, Hebert DN. Abnormal Acidification of Melanoma Cells Induces Tyrosinase Retention in the Early Secretory Pathway*. Journal Of Biological Chemistry 2002, 277: 14821-14828. PMID: 11812790, DOI: 10.1074/jbc.m111497200.Peer-Reviewed Original ResearchCOMMENTARY 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 ResearchMeSH KeywordsGene Expression Regulation, NeoplasticHumansMelanomaMonophenol MonooxygenaseSkin NeoplasmsSkin PigmentationConceptsMelanocyte-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
2000
Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*
Halaban R, Cheng E, Svedine S, Aron R, Hebert D. Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*. Journal Of Biological Chemistry 2000, 276: 11933-11938. PMID: 11124258, DOI: 10.1074/jbc.m008703200.Peer-Reviewed Original ResearchMeSH KeywordsCells, CulturedDihydroxyphenylalanineEndoplasmic ReticulumGolgi ApparatusHumansMicroscopy, FluorescenceMonophenol MonooxygenaseProtein FoldingProtein TransportTyrosineConceptsWild-type tyrosinaseEndoplasmic reticulumProper foldingWild-type proteinMelanoma cellsLoss of pigmentationTyrosinase-positive melanoma cellsGolgi transportType proteinAlbino mutantS proteasomeSubsequent retranslocationMutant formsCatalytic stateEnzymatic activityProteolytic degradationNative formReticulumFoldingProteinTumor-derived antigenic peptidesTyrosinase activitySuppress tyrosinase activityCellsMetabolic changesTranslation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*
Újvári A, Aron R, Eisenhaure T, Cheng E, Parag H, Smicun Y, Halaban R, Hebert D. Translation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*. Journal Of Biological Chemistry 2000, 276: 5924-5931. PMID: 11069924, DOI: 10.1074/jbc.m009203200.Peer-Reviewed Original ResearchConceptsTranslation rateCell-free systemProtein translation ratesType I membrane glycoproteinsNormal melanocytesHuman tyrosinaseSemi-permeabilized cellsMelanoma cellsUbiquitin-proteasomal pathwayRate of translationSite-directed mutagenesisWild-type tyrosinaseProtein synthesis inhibitor cycloheximideInefficient glycosylationGlycosylation efficiencyAberrant retentionProtein translationCotranslational eventsConsensus sitesCore glycanDegradative fateProtein doubletEndoplasmic reticulumMaturation eventsAmelanotic melanoma cellsEndoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism
Halaban R, Svedine S, Cheng E, Smicun Y, Aron R, Hebert D. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 5889-5894. PMID: 10823941, PMCID: PMC18529, DOI: 10.1073/pnas.97.11.5889.Peer-Reviewed Original ResearchMeSH KeywordsAlbinism, OculocutaneousAmino Acid SubstitutionAnimalsCalcium-Binding ProteinsCalnexinCalreticulinCells, CulturedEndoplasmic ReticulumGolgi ApparatusHumansMelanocytesMelanosomesMiceMice, Mutant StrainsMicroscopy, FluorescenceMonophenol MonooxygenasePoint MutationProtein BindingProtein FoldingRecombinant Fusion ProteinsRibonucleoproteinsTransfection
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
1993
Molecular analyses of a tyrosinase-negative albino family.
Park K, Chintamaneni C, Halaban R, Witkop C, Kwon B. Molecular analyses of a tyrosinase-negative albino family. American Journal Of Human Genetics 1993, 52: 406-13. PMID: 8430701, PMCID: PMC1682201.Peer-Reviewed Original ResearchMeSH KeywordsAlbinism, OculocutaneousBase SequenceBlotting, NorthernBlotting, SouthernChildDNA Mutational AnalysisElectrophoresis, Polyacrylamide GelFemaleFrameshift MutationGene LibraryGlycosylationHumansMaleMelanocytesMolecular Sequence DataMonophenol MonooxygenaseMutationPedigreePoint MutationPolymerase Chain ReactionPrecipitin TestsSequence DeletionConceptsAmino acid changesAcid changesPutative amino acid changesPremature termination signalTwo-nucleotide deletionSingle base substitutionTermination signalGel electrophoretic analysisN-glycosylationCDNA libraryBase pair deletionCodon 355Genomic DNAHomologous allelesNucleotide substitutionsSequence analysisMolecular analysisMissense mutationsTwo-base deletionExon 1Electrophoretic analysisCodon 226Exon 3AllelesTyrosinase-negative oculocutaneous albinism
1991
A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism.
Chintamaneni C, Halaban R, Kobayashi Y, Witkop C, Kwon B. A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 5272-5276. PMID: 1711223, PMCID: PMC51854, DOI: 10.1073/pnas.88.12.5272.Peer-Reviewed Original Research
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 peroxideHydroperoxidaseMelanogenesisGp75ActivityMurinePigmentationRecent Advances in the Molecular Biology of Pigmentation: Mouse Models
Halaban R, Moellmann G. Recent Advances in the Molecular Biology of Pigmentation: Mouse Models. Pigment Cell & Melanoma Research 1990, 3: 67-78. PMID: 1409441, DOI: 10.1111/j.1600-0749.1990.tb00352.x.Peer-Reviewed Original Research
1989
Isolation, Chromosomal Mapping, and Expression of the Mouse Tyrosinase Gene
Kwon B, Haq A, Wakulchik M, Kestler D, Barton D, Francke U, Lamoreux M, Whitney J, Halaban R. Isolation, Chromosomal Mapping, and Expression of the Mouse Tyrosinase Gene. Journal Of Investigative Dermatology 1989, 93: 589-594. PMID: 2507645, DOI: 10.1111/1523-1747.ep12319693.Peer-Reviewed Original ResearchConceptsMouse tyrosinaseTyrosinase geneMouse chromosome 7Mouse tyrosinase geneSomatic cell hybridsSouthern blot analysisChromosomal mappingGenomic clonesCell hybridsPromoter sequencesTATA elementAlbino locusChromosome 7Melanoma cell linesCDNA probeNormal melanocytesTyrosinase mRNABackcross miceBlot analysisFarthest upstreamCell linesDeletion miceGenesLociCloudman SMolecular 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 enzymeSequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression
Kwon B, Wakulchik M, Haq A, Halaban R, Kestler D. Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression. Biochemical And Biophysical Research Communications 1988, 153: 1301-1309. PMID: 3134020, DOI: 10.1016/s0006-291x(88)81370-6.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAcid sequenceTyrosinase cDNAPotential N-glycosylation sitesMouse genomic cloneHistidine-rich regionMouse tyrosinase geneN-glycosylation sitesLevels of transcriptsCopper-binding siteMouse tyrosinase cDNADeduced proteinGenomic clonesTransmembrane sequenceHuman tyrosinase cDNACDNA clonesMouse tyrosinaseTyrosinase geneGene expressionSequence analysisAmino acidsHuman tyrosinaseClonesCDNAMelanoma cellsCloning and characterization of a human tyrosinase cDNA.
Kwon B, Haq A, Kim G, Pomerantz S, Halaban R. Cloning and characterization of a human tyrosinase cDNA. Progress In Clinical And Biological Research 1988, 256: 273-82. PMID: 2835779.Peer-Reviewed Original Research
1987
A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine.
Kwon B, Halaban R, Kim G, Usack L, Pomerantz S, Haq A. A melanocyte-specific complementary DNA clone whose expression is inducible by melanotropin and isobutylmethyl xanthine. Molecular Biology & Medicine 1987, 4: 339-55. PMID: 2449595.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAnimalsAntibodies, MonoclonalCatechol OxidaseDNAGene Expression RegulationGlycoproteinsHumansMelaninsMelanocyte-Stimulating HormonesMelanocytesMelanomaMelanoma, ExperimentalMiceMonophenol MonooxygenaseNeoplasm ProteinsPigmentationSpecies SpecificityTheophyllineTumor Cells, CulturedConceptsPmel 17CDNA clonesLambda gt11 cDNA libraryComplementary DNA cloneHuman tyrosinase geneNormal human melanocytesSingle geneDNA clonesCDNA libraryStimulation of humanMRNA speciesTyrosinase geneMurine melanocytesMurine DNAMurine melanoma cellsRestriction fragmentsHuman melanocytesRepresentative clonesGenesClonesImmunological homologyCDNAMelanoma cellsMelanocytesSpecies