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Granulocyte-macrophage colony-stimulating factor, interleukin-3, and steel
factor induce rapid tyrosine phosphorylation of p42 and p44 MAP kinase
K Okuda, JS Sanghera, SL Pelech, Y Kanakura, M Hallek, JD Griffin and BJ Druker
Dana-Farber Cancer Institute, Boston, MA 02115.
Granulocyte-macrophage colony-stimulating factor (GM-CSF), Interleukin- 3
(IL-3), and Steel Factor (SF) induce proliferation of hematopoietic cells
through binding to specific, high-affinity, cell surface receptors.
However, little is known about postreceptor signal transduction pathways.
In previous studies, we noted that each of these three factors could
independently support proliferation of the human MO7 cell line, and also
that each factor induced a rapid increase in protein-tyrosyl
phosphorylation. Although the proteins phosphorylated on tyrosine by GM-CSF
and IL-3 are similar or identical in MO7 cells, many of the proteins that
are phosphorylated on tyrosine after SF are different. However, two
proteins, p42 and p44, were prominently phosphorylated in response to all
three of the factors. In MO7 cells, the tyrosyl phosphorylation of p42 and
p44 was transient, peaking at 5 to 15 minutes. In contrast to many of the
other proteins which are tyrosyl phosphorylated in response to these
factors, phosphorylation of p42 and p44 was temperature-dependent,
occurring at 37 degrees C, but not at 4 degrees C. We identified the p42
protein as p42 Mitogen- Activated Protein Kinase (p42mapk, ERK-2) and the
p44 as a p42mapk- related protein using monospecific antisera to MAP
kinase. GM-CSF, IL- 3, and SF were each found to induce MAP kinase activity
when assayed in vitro using myelin basic protein (MBP) as a substrate.
Remarkably, we found that GM-CSF-induced tyrosyl phosphorylation of p42 and
p44 even in nonproliferative cells (neutrophils) that respond to this CSF,
and that p42 and p44 were two of the most prominently tyrosyl
phosphorylated proteins following GM-CSF stimulation of these cells. These
results implicate p42mapk and p44 as important signal transducing molecules
in myeloid cells, and it is likely that these kinases play a role as part
of a sequential "kinase cascade" linking growth factor receptors to
mitogenesis and other cellular responses.
Volume 79,
Issue 11,
pp. 2880-2887,
06/01/1992
Copyright © 1992 by The American Society of Hematology
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