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Volume 270,
Number 2,
Issue of January 13, 1995 pp. 966-970
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Both Interleukin
4 and Interleukin 13 Induce Tyrosine Phosphorylation of the 140-kDa
Subunit of the Interleukin 4 Receptor
(Received for publication, July 8, 1994; and in revised form, November 8,
1994)
Claudia
Smerz-Bertling ,
Albert
Duschl
We have investigated tyrosine phosphorylation of cellular
proteins induced by interleukin (IL) 4 and compared it with the effects
of three related cytokines, IL-2, IL-7, and IL-13. We show here that
both IL-4 and IL-13 stimulate tyrosine phosphorylation of the 140-kDa
IL-4 receptor subunit, which suggests that this receptor protein is
used by both cytokines. Receptor phosphorylation induced by IL-13 was
both weaker and slower than with IL-4. Stimulation of cells with IL-2
and IL-7 induced identical phosphorylation patterns to each other but
not phosphorylation of the 140-kDa IL-4 receptor subunit. The only
signal appearing upon stimulation with any of the four cytokines was
the weak phosphorylation of an unidentified protein of 160 kDa. SH2
domains of p56 and p59 precipitated the same proteins as anti-phosphotyrosine
antibodies after IL-4 stimulation, which suggests that a src-type kinase may be involved in signal transduction through
the IL-4 receptor.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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