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Interleukin-3, GM-CSF, and TPA induce distinct phosphorylation events in an
interleukin 3-dependent multipotential cell line
PH Sorensen, AL Mui, SC Murthy and G Krystal
Terry Fox Laboratory, B.C. Cancer Research Centre, Vancouver, Canada.
The mechanism of action of the hemopoietic growth factor, murine
interleukin-3 (mIL-3), was investigated using an mIL-3-dependent
multipotential hematopoietic cell line, B6SUtA1. Murine granulocyte-
macrophage colony-stimulating factor (mGM-CSF) was as potent as mIL-3 in
stimulating these cells. In addition, sodium orthovanadate, an inhibitor of
phosphotyrosine phosphatase, and 12-O-tetradecanoyl- phorbol-13-acetate
(TPA), a known activator of protein kinase C, also stimulated DNA synthesis
in these cells, suggesting that protein phosphorylation might be involved
in the mechanism of action of mIL-3 and mGM-CSF. To assess this
possibility, intact B6SUtA1 cells exposed for brief periods to mIL-3,
mGM-CSF, and TPA were analyzed for changes in phosphorylation patterns
using metabolic 32P-labeling and antibodies to phosphotyrosine. Both mIL-3
and mGM-CSF induced the serine-specific phosphorylation of a 68-Kd
cytosolic protein, whereas all three agents stimulated the serine-specific
phosphorylation of a 68-Kd membrane protein. Furthermore, mIL-3 stimulated
tyrosine phosphorylation of the 68-Kd membrane protein, as well as of 140-,
90-, 55, and 40-Kd proteins. The 90-Kd protein was also tyrosine
phosphorylated in response to mGM-CSF. These phosphotyrosine containing
proteins were not detected in TPA-treated cells. These results indicate
that protein phosphorylations on tyrosine and serine residues occur in
B6SUtA1 cells following short-term incubation with mIL-3 or mGM-CSF and
that most of these phosphorylation events are mediated by kinases other
than protein kinase C (PkC).
Volume 73,
Issue 2,
pp. 406-418,
02/01/1989
Copyright © 1989 by The American Society of Hematology
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