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Blood, Vol. 95 No. 5 (March 1), 2000:
pp. 1656-1662
Activation of Akt kinase by granulocyte colony-stimulating factor
(G-CSF): evidence for the role of a tyrosine kinase activity distinct
from the janus kinases
Fan Dong and
Andrew C. Larner
From the Department of Immunology, Cleveland Clinic Research
Institute, Cleveland, OH.
Activation of the serine/threonine kinase Akt has been shown to be a
critical component for growth factor and cytokine stimulation of cell
survival. Although some of the immediate upstream activators of Akt
have been defined, the roles of tyrosine kinases in the activation of
Akt are not well delineated. Granulocyte colony-stimulating factor
(G-CSF) regulates the proliferation, differentiation, and survival of
neutrophilic granulocytes. G-CSF exerts its actions by stimulating
several signaling cascades after binding its cell surface receptor.
Both Jak (Janus) and Src families of tyrosine kinases are stimulated by
incubation of cells with G-CSF. In this report, we show that G-CSF
stimulation of cells leads to activation of Akt. The membrane-proximal
55 amino acids of the G-CSF receptor cytoplasmic domain are sufficient
for mediating Akt activation. However, activation of Akt appears to be
downregulated by the receptor's carboxy-terminal region of 98 amino
acids, a region that has been shown to be truncated in some patients
with acute myeloid leukemia associated with severe congenital
neutropenia. Furthermore, we demonstrate that G-CSF-induced activation
of Akt requires the activities of Src family kinases but can be clearly dissociated from G-CSF-stimulated activation of Stats (signal transducers and activators of transcripton) by the Jak kinases. Thus,
cytokine activation of the Jak/Stat and other signaling cascades can be
functionally separated.
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