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Functional reconstitution of the human interleukin-3 receptor
T Kitamura and A Miyajima
Department of Molecular Biology, DNAX Research Institute of Molecular and
Cellular Biology, Palo Alto, CA 94304.
The high-affinity receptors for human interleukin-3 (IL-3), GM-CSF, and
IL-5 are composed of alpha and beta subunits. The alpha subunits are
primary ligand binding proteins specific for each ligand, whereas the three
human receptors share a common beta subunit (beta c). In contrast to humans
mice have two closely related genes, AIC2A and AIC2B, which are homologous
to human beta c. The AIC2A gene encodes a low-affinity murine IL-3 binding
protein, and the AIC2B protein is the beta subunit shared between murine
GM-CSF receptors (mGMR) and IL-5 receptors (mIL- 5R). To examine the
function of these receptor components, we established various stable
transfectants of murine IL-2-dependent CTLL- 2 cells. CTLL-2 transfectants
expressing both the alpha and beta subunits of the human IL-3 receptor
(hIL-3R) proliferated in response to physiologic concentrations of hIL-3.
Coexpression of hIL-3R alpha with AIC2B but not with AIC2A in CTLL-2 cells
conferred a growth response to hIL-3. Although CTLL-2 transfectants
expressing hIL-3R alpha alone did not proliferate in the presence of hIL-3,
hIL-3- responsive sublines were repeatedly isolated. These sublines
expressed endogenous AIC2B but not AIC2A. These results indicate that human
beta c is essential for hIL-3 signaling and that AIC2B is a murine
equivalent of human beta c. We also showed that hIL-3 and hGM-CSF induced
tyrosine phosphorylation of several proteins in CTLL transfectants, similar
to those observed in human factor-dependent TF-1 cells stimulated with
hIL-3 and hGM-CSF.
Volume 80,
Issue 1,
pp. 84-90,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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