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Hck expression correlates with granulocyte-macrophage colony- stimulating
factor-induced proliferation in HL-60 cells
D Linnekin, OM Howard, L Park, W Farrar, D Ferris and DL Longo
Laboratory of Leukocyte Biology, National Cancer Institute, Frederick
Cancer Research and Development Center, MD.
The human myeloid cell line HL-60 expresses approximately 300 high-
affinity granulocyte-macrophage colony-stimulating factor receptors (GM-
CSFRs), yet treatment of these cells with GM-CSF does not result in
enhanced cellular proliferation or increases in protein tyrosine
phosphorylation. In contrast, GM-CSF induces rapid increases in protein
tyrosine phosphorylation and proliferative responses in HL-60 cells
pretreated for 3 days in dimethyl sulfoxide (DMSO). Similarly, HL-60 cells
pretreated with retinoic acid or 1,25 dihydroxyvitamin D3 were also capable
of responding to GM-CSF. Interestingly, each of these treatments resulted
in increased expression of the src-like tyrosine kinase hck. Stimulation
with GM-CSF increased hck autophosphorylation in DMSO-treated HL-60 cells,
suggesting that hck is a component of the GM-CSF signal transduction
pathway. To determine if hck has a role in the DMSO-induced recoupling of
the GM-CSFR, we overexpressed hck in HL- 60 cells. The resulting cell line
(HL-60/hck) expresses hck mRNA and protein at levels comparable with
DMSO-treated HL-60 cells. Stimulation of HL-60/hck cells with GM-CSF
results in activation of hck, increases in protein tyrosine
phosphorylation, and increased proliferation. These results show that
cytokine receptors can exist in an uncoupled form and suggest that in HL-60
cells, appropriate levels of the src-like tyrosine kinase hck are critical
for functional coupling of the GM-CSFR to biologic responses.
Volume 84,
Issue 1,
pp. 94-103,
07/01/1994
Copyright © 1994 by The American Society of Hematology
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