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Binding of G-CSF, GM-CSF, tumor necrosis factor-alpha, and gamma-
interferon to cell surface receptors on human myeloid leukemia cells
triggers rapid tyrosine and serine phosphorylation of a 75-Kd protein
JP Evans, AR Mire-Sluis, AV Hoffbrand and RG Wickremasinghe
Department of Haematology, Royal Free Hospital School of Medicine, London,
UK.
Granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage
colony-stimulating factor (GM-CSF), gamma-interferon (gamma-IFN), or tumor
necrosis factor-alpha (TNF-alpha) triggered the rapid, stable
phosphorylation of a 75-Kd protein (p75) when incubated with permeabilized
HL60 human myeloid leukemia cells in the presence of [gamma-32P] ATP. Among
several chemical inducers of HL60 cell differentiation, dimethyl sulfoxide
also triggered p75 labeling, but retinoic acid or
12-O-tetradecanoylphorbol-13-acetate did not elicit this response.
Pretreatment of cells with G-CSF or GM-CSF for more than 30 seconds before
permeabilization rendered the p75 labeling undetectable, suggesting that
ligand-stimulated labeling was rapidly completed within this time in intact
cells. Phosphorylation of p75 occurred on serine and tyrosine residues.
This conclusion was confirmed by direct phosphoamino acid analysis.
Immunoblot analysis of lysates of intact HL60 cells that had been incubated
with G-CSF, GM-CSF, IFN, or TNF confirmed that tyrosine phosphorylation of
a p75 also occurred in response to these cytokines in intact cells.
Pretreatment of intact HL60 cells with one biologic agent or dimethyl
sulfoxide abolished p75 labeling in response to incubation of permeabilized
cells with a second agent, strongly suggesting that the same protein was
phosphorylated in response to these treatments. p75 labeling was strictly
dependent on expression of the appropriate ligand receptor. Data suggest
that activation of a tyrosine kinase system is an early response to the
binding of G-CSF, GM-CSF, TNF, or IFN to their respective cell surface
receptors, or to the addition of dimethyl sulfoxide, and that the resulting
phosphorylation event(s) may play a role in securing common elements in the
biologic responses to these agents.
Volume 75,
Issue 1,
pp. 88-95,
01/01/1990
Copyright © 1990 by The American Society of Hematology
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