2011
Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma
Tworkoski K, Singhal G, Szpakowski S, Zito CI, Bacchiocchi A, Muthusamy V, Bosenberg M, Krauthammer M, Halaban R, Stern DF. Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma. Molecular Cancer Research 2011, 9: 801-812. PMID: 21521745, PMCID: PMC3117976, DOI: 10.1158/1541-7786.mcr-10-0512.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell Line, TumorCell MovementCell ProliferationErbB ReceptorsGene Expression Regulation, NeoplasticGene Knockdown TechniquesHEK293 CellsHumansInfant, NewbornMelanocytesMelanomaPhosphoproteinsPhosphorylationProteomicsReceptor Protein-Tyrosine KinasesReceptor, IGF Type 2RNA, Small InterferingSignal TransductionSkin NeoplasmsSTAT3 Transcription FactorConceptsTherapeutic targetReceptor tyrosine kinasesMelanoma cellsPotential therapeutic targetIdentifies potential therapeutic targetsActive receptor tyrosine kinasesTyrosine kinaseMelanoma cell migrationReceptor expressionBreast cancerAxl knockdownAutocrine circuitTherapeutic interventionsCancer subtypesReceptor tyrosine kinase activationTyrosine kinase activationNovel targetActivated receptorsAxlRNA knockdownMelanomaCell migrationHER3KnockdownIGF1R
1997
Suppression of autocrine cell proliferation and tumorigenesis of human melanoma cells and fibroblast growth factor transformed fibroblasts by a kinase-deficient FGF receptor 1: evidence for the involvement of Src-family kinases
Yayon A, Ma Y, Safran M, Klagsbrun M, Halaban R. Suppression of autocrine cell proliferation and tumorigenesis of human melanoma cells and fibroblast growth factor transformed fibroblasts by a kinase-deficient FGF receptor 1: evidence for the involvement of Src-family kinases. Oncogene 1997, 14: 2999-3009. PMID: 9223663, DOI: 10.1038/sj.onc.1201159.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCell DivisionCell Line, TransformedFibroblast Growth Factor 2FibroblastsFilaggrin ProteinsGenes, DominantHumansMelanomaMicePhenotypeProtein-Tyrosine KinasesReceptor Protein-Tyrosine KinasesReceptor, Fibroblast Growth Factor, Type 1Receptors, Fibroblast Growth FactorRecombinant ProteinsSrc Homology DomainsTumor Cells, CulturedConceptsSrc family kinasesFGF receptor 1FGF receptorsTyrosyl-phosphorylated proteinsHuman melanoma cellsMelanoma cellsImmune kinase assayIntracellular kinase domainDominant negative mutantActivated FGF receptorCell proliferationMetastatic melanoma cellsMelanoma tumor progressionGrowth factorTransmembrane domainKinase assaysSrc familyKinase domainDownstream targetsReceptor 1Fibroblast growth factorBasic fibroblast growth factorGrowth advantageNormal melanocytesAutocrine activation
1995
VEGF121, a Vascular Endothelial Growth Factor (VEGF) Isoform Lacking Heparin Binding Ability, Requires Cell-surface Heparan Sulfates for Efficient Binding to the VEGF Receptors of Human Melanoma Cells*
Cohen T, Gitay-Goren H, Sharon R, Shibuya M, Halaban R, Levi B, Neufeld G. VEGF121, a Vascular Endothelial Growth Factor (VEGF) Isoform Lacking Heparin Binding Ability, Requires Cell-surface Heparan Sulfates for Efficient Binding to the VEGF Receptors of Human Melanoma Cells*. Journal Of Biological Chemistry 1995, 270: 11322-11326. PMID: 7744769, DOI: 10.1074/jbc.270.19.11322.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingBinding SitesCell DivisionCell LineCell MembraneCross-Linking ReagentsEndothelial Growth FactorsGene ExpressionGenetic VariationHeparinHeparitin SulfateHumansKineticsLymphokinesMelanomaReceptor Protein-Tyrosine KinasesReceptors, Growth FactorReceptors, MitogenReceptors, Vascular Endothelial Growth FactorRNA, MessengerTumor Cells, CulturedVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsHuman melanoma cellsVEGF receptorsMelanoma cellsCell surface heparan sulfateVEGF receptor Flt-1VEGF receptor KDR/flkVascular endothelial growth factor isoformsHeparan sulfateReceptor KDR/flkReceptor Flt-1Growth factor isoformsCell surface heparin-like moleculesKDR/FlkVascular endothelial growth factor (VEGF) splice variantsHeparin-like moleculesAddition of heparin