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Interleukin-13 Receptor   But Not Chain: A
Functional Component of Interleukin-4 Receptors
Takashi Murata,
Jun Taguchi, and
Raj K. Puri
From the Laboratory of Molecular Tumor Biology, Division of Cellular
and Gene Therapy, Center for Biologics Evaluation and Research, Food
and Drug Administration, Bethesda, MD.
In hematopoietic cells, interleukin-2 receptor (IL-2R)  chain
(termed c) is shown to be a component of the IL-4R
system, whereas in nonhematopoietic cells, c is absent
and it is not a component of the IL-4R system. Here, we show that the
IL-13R   chain (termed IL-13R) but not the IL-13R
chain (termed IL-13R) can substitute for c and,
thus, IL-13R forms a novel component of the IL-4R system.
This conclusion was drawn on the basis of chemical cross-linking,
immunoprecipitation, the ability of IL-13R but not IL-13R
to augment IL-4 binding affinity, and the requirement of
IL-13R for IL-4-induced STAT6 activation in Chinese hamster
ovary (CHO) cells transfected with various receptor subunits.
Cotransfection of IL-4 receptor p140 (termed IL-4R ) with
c or IL-13R increased IL-4 binding affinity
and allowed for STAT6 activation in response to IL-4. However,
cotransfection of all three chains did not further increase IL-4
binding or alter the extent of STAT6 activation suggesting that all
three chains together do not seem to participate in IL-4 function.
Instead, IL-4R heterodimerizes with c or
IL-13R and mediates STAT6 activation. Cotransfection of
IL-4R with IL-13R neither increased IL-4 binding affinity nor
allowed for STAT6 activation in response to IL-4 indicating that
IL-13R does not convert binding affinity nor transmit signals for
IL-4. Because IL-4 phosphorylates JAK1 and JAK2 tyrosine kinases in
nonhematopoietic cells, we investigated whether JAK1 and JAK2 are
required for IL-4-induced STAT6 activation in various transfectants.
Cotransfection experiments with different chains of IL-4R and
kinase-deficient JAK1 and JAK2 mutants in CHO cells showed that JAK1
and JAK2 are required for optimal activation of STAT6 in the
transfectant but only partially in the
c transfectant. Taken together, our results show that
IL-13R is a novel functional component of the IL-4R system
and that JAK1 and JAK2 mediate IL-4-induced optimal activation of
STAT6 in nonhematopoietic cells.
Blood, Vol. 91 No. 10 (May 15), 1998:
pp. 3884-3891
© 1998 by The American Society of Hematology.
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