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Granulocyte colony-stimulating factor rapidly activates a distinct STAT-
like protein in normal myeloid cells
DJ Tweardy, TM Wright, SF Ziegler, H Baumann, A Chakraborty, SM White, KF Dyer and KA Rubin
Department of Medicine, University of Pittsburgh School of Medicine, PA,
USA.
Binding of granulocyte colony-stimulating factor (G-CSF) to normal myeloid
cells activates the protein tyrosine kinases Lyn and Syk and results in the
immediate early upregulation of G-CSF receptor (R) mRNA. In our studies of
the signaling pathways activated by G-CSF that are coupled to proliferation
and differentiation of myeloid cells, we examined whether G-CSF activated a
latent transcription factor belonging to the STAT protein family.
Electrophoretic mobility shift assays (EMSAs) of nuclear extracts from
G-CSF-stimulated human myeloid cells showed the rapid activation of a
DNA-binding protein that bound to the high-affinity serum-inducible element
(hSIE) and migrated with mobility similar to serum inducible factor (SIF)-A
(Stat3 homodimer). The G-CSF-stimulated SIF-A complex (G-SIF-A) did not
bind to duplex oligonucleotides used to purify and characterize other Stat
proteins (Stat1-6). In addition, antibodies raised against Stat1-6 failed
to supershift the G-SIF-A complex or interfere with its formation. Based on
its binding to the hSIE and lack of antigenic cross-reactivity with other
known STAT proteins that bind to this element, it is likely that G-SIF-A is
composed of a distinct member of the STAT protein family. EMSAs of
whole-cell extracts prepared from cell lines containing full- length and
truncated mutants of the G-CSFR showed that activation of G- SIF-A did not
correlate with proliferation; rather, optimal activation requires the
distal half of the cytosolic domain of the G-CSFR that is essential for
differentiation. Activation of G-SIF-A, therefore, may be an early
G-CSFR-coupled event that is critical for myeloid maturation.
Volume 86,
Issue 12,
pp. 4409-4416,
12/15/1995
Copyright © 1995 by The American Society of Hematology
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