Abstract
The molecular mechanism of erythroid differentiation has been still ill-defined. In this study, we introduced a human interleukin-2 receptor (IL-2R) beta chain cDNA into ELM-I-1 cells which differentiated into hemoglobin-positive cells in the presence of erythropoietin (Epo), and established the transformant which expressed IL-2R beta chain. In this transformant, we revealed that IL-2 induced erythroid differentiation and the same pattern of tyrosine phosphorylation as Epo. These data suggest that tyrosine phosphorylation is involved in signal transduction pathway of erythroid differentiation. It is also implicated that the Epo and IL-2 receptor system share a common signal transduction pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Differentiation / drug effects*
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Erythropoietin / pharmacology
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Humans
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Interleukin-2 / pharmacology*
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Kinetics
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Leukemia, Erythroblastic, Acute
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Macromolecular Substances
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Mice
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Molecular Weight
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Phosphoproteins / isolation & purification
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Phosphoproteins / metabolism
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Phosphorylation
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Phosphotyrosine
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Receptors, Interleukin-2 / drug effects
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Receptors, Interleukin-2 / genetics
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Receptors, Interleukin-2 / physiology*
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Recombinant Proteins / pharmacology
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Transfection
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Tumor Cells, Cultured
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Tyrosine / analogs & derivatives
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Tyrosine / analysis
Substances
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Interleukin-2
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Macromolecular Substances
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Phosphoproteins
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Receptors, Interleukin-2
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Recombinant Proteins
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Erythropoietin
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Phosphotyrosine
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Tyrosine