2019
A novel anti-melanoma SRC-family kinase inhibitor
Halaban R, Bacchiocchi A, Straub R, Cao J, Sznol M, Narayan D, Allam A, Krauthammer M, Mansour TS. A novel anti-melanoma SRC-family kinase inhibitor. Oncotarget 2019, 10: 2237-2251. PMID: 31040916, PMCID: PMC6481345, DOI: 10.18632/oncotarget.26787.Peer-Reviewed Original ResearchSrc family kinase inhibitorMAPK inhibitorTranscription factor MITFPatient-derived melanoma cellsPI3K activityKinase inhibitorsSynergistic growth inhibitionGrowth arrestMelanoma cell linesK activityProteolytic degradationCell linesERBB2 inhibitionOncogene expressionMelanoma therapyTumor growthDrug resistanceMelanoma cellsGrowth inhibitionAlternative targetsActivity leadInhibitorsPP2ASHP2Inhibition
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 ResearchConceptsWild-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 changes
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
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