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The insulin receptor substrate-1-related 4PS substrate but not the
interleukin-2R gamma chain is involved in interleukin-13-mediated signal
transduction
LM Wang, P Michieli, WR Lie, F Liu, CC Lee, A Minty, XJ Sun, A Levine, MF White and JH Pierce
Laboratory of Cellular and Molecular Biology, National Institutes of
Health, Bethesda, MD 20892-4255, USA.
Interleukin-13 (IL-13) induced a potent mitogenic response in IL-3-
dependent TF-1 cells and DNA synthesis to a lesser extent in MO7E and
FDC-P1 cells. IL-13 stimulation of these lines, like IL-4 and insulin- like
growth factor-1 (IGF-1), resulted in tyrosine phosphorylation of a 170-kD
substrate. The tyrosine-phosphorylated 170-kD substrate strongly associated
with the 85-kD subunit of phosphoinositol-3 (PI-3) kinase and with Grb-2.
Anti-4PS serum readily detected the 170-kD substrate in lysates from both
TF-1 and FDC-P1 cells stimulated with IL-13 or IL-4. These data provide
evidence that IL-13 induces tyrosine phosphorylation of the 4PS substrate,
providing an essential interface between the IL- 13 receptor and signaling
molecules containing SH2 domains. IL-13 and IL-4 stimulation of murine L
cell fibroblasts, which endogenously express the IL-4 receptor (IL-4R
alpha) and lack expression of the IL-2 receptor gamma subunit (IL-2R
gamma), resulted in tyrosine phosphorylation of insulin receptor
substrate-1 (IRS-1)/4PS. Enhanced tyrosine phosphorylation of IRS-1/4PS was
observed in response to IL-4, but not IL-13 treatment of L cells
transfected with the IL-2R gamma chain. These results indicate that IL-13
does not use the IL-2R gamma subunit in its receptor complex and that
expression of IL-2R gamma enhances, but is not absolutely required for
mediating IL-4-induced tyrosine phosphorylation of IRS-1/4PS.
Volume 86,
Issue 11,
pp. 4218-4227,
12/01/1995
Copyright © 1995 by The American Society of Hematology
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