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Interleukin-3 regulates the activity of the LYN protein-tyrosine kinase in
myeloid-committed leukemic cell lines
T Torigoe, R O'Connor, D Santoli and JC Reed
Department of Pathology and Laboratory Medicine, University of
Pennsylvania, Philadelphia.
The lymphokine interleukin-3 (IL-3) promotes the growth and survival of
immature hematopoietic cells. Previous studies have shown that IL-3 induces
rapid increases in protein-tyrosine kinase (PTK) activity in IL-
3--dependent cells. Unlike some other hematopoietic growth factor receptors
(eg, c-fms and c-kit), however, the known subunits of the IL- 3 receptor
(IL-3R) lack intrinsic kinase activity. Recently, it was reported that the
IL-2R (whose p75 beta-subunit shares sequence homology with a known murine
IL-3R subunit and a common beta-subunit of the human IL-3R and
granulocyte-macrophage colony-stimulating factor [GM-CSF] receptors) can
physically associate with and regulate the activity of the SRC-family PTK,
p56-LCK. Because most IL-3--dependent cells contain p53/56-LYN, but not
p56-LCK, we explored the effects of IL-3 on the activities of LYN and other
SRC-like PTKs in two human leukemic cell lines, AML-193 and TALL-101, which
are phenotypically myeloid, and whose in vitro growth is dependent on IL-3.
These cells expressed four of the eight known SRC-family proto-oncogenes:
lyn, fyn, yes, and hck. When these factor-dependent leukemic cell lines
were deprived of lymphokine to achieve cellular quiescence and then
restimulated with IL-3, rapid increases (detectable within 1 minute and
maximal by 10 minutes) were observed in the activity of the p53/56-LYN
kinase, as assessed by in vitro kinase assays. In contrast, no alteration
in the activities of other SRC-family PTKs present in these cells was
detected after restimulation with IL-3 under the same conditions. This
effect of IL-3 reflected an increase in the specific activity of the LYN
kinase, because levels of the 53-Kd and 56-Kd LYN proteins were unaltered
by IL-3 stimulation, as assessed by immunoblotting. Furthermore, the
magnitude of these inducible increases in LYN kinase activity was dependent
on the concentration of IL-3, and correlated with IL-3--induced
proliferation. The IL-3--induced upregulation of LYN kinase activity may be
mediated by the 120-Kd common subunit of the human IL-3 and GM-CSF
receptors, because GM-CSF also stimulated marked increases in the activity
of the LYN kinase, whereas granulocyte-CSF (G-CSF) did not, despite
inducing cellular proliferation. These observations provide the first
example of an IL-3-- regulable PTK, and strongly suggest that the
p53/56-LYN kinase participates in early IL-3--initiated signalling events,
at least in some human leukemic cell lines.
Volume 80,
Issue 3,
pp. 617-624,
08/01/1992
Copyright © 1992 by The American Society of Hematology
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