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J. Biol. Chem., Vol. 266, Issue 23, 14964-14969, Aug, 1991
MP Carroll, JL Spivak, M McMahon, N Weich, UR Rapp and WS May
Erythropoietin mediates the rapid phosphorylation of Raf-1 in the murine
cell lines HCD-57 and FDC-P1/ER, which proliferate in response to this
cytokine. Phosphorylation occurs at both serine and tyrosine residues and
as such is similar to the Raf-1 phosphorylation seen after interleukin-3
(IL-3), granulocyte-macrophage colony-stimulating factor, and interleukin-2
stimulation in other murine cell lines. Such data suggest that these growth
factors may share a common mechanism(s) of Raf-1 phosphorylation.
Furthermore, in association with Raf-1 phosphorylation, erythropoietin
induces a 2-3-fold increase in Raf-1 kinase activity as measured in immune
complex kinase assays in vitro. Finally, a c-raf antisense
oligodeoxyribonucleotide, which specifically decreases intracellular Raf-1
levels, also substantially inhibits both erythropoietin and IL-3-directed
DNA synthesis. Together, these results provide evidence that activated
Raf-1 is a necessary component of erythropoietin and IL-3 growth signaling
pathways.
Erythropoietin induces Raf-1 activation and Raf-1 is required for erythropoietin-mediated proliferation
Johns Hopkins Oncology Center, Johns Hopkins University School of Medicine, Baltimore, Maryland 21231.
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