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(Received for publication, August 24, 1995; and in revised form, October 31, 1995)
Interleukin-4 (IL-4) and IL-13 are functionally similar
cytokines. The functional IL-4 receptor (IL-4R) consists of the
IL-4R
chain (IL-4R) and the IL-2R chain
(
), which is shared by the IL-2, IL-7, IL-9, and IL-15
receptors. The functional IL-13R is thought to involve the IL-4R
but not . In this study, we have analyzed activation
of members of the Janus tyrosine kinase (Jak) family and signal
transducers and activators of transcription (STAT) 6 induced by IL-4
and IL-13 in Epstein-Barr virus-transformed B cells derived from two
patients of X-linked severe combined immunodeficiency, who have
mutations of the gene in the extracellular and
intracellular domains. In these B cells, IL-4 failed to induce tyrosine
phosphorylation of Jak3 and activation of STAT6, or activation of these
molecules was significantly decreased compared with Epstein-Barr
virus-transformed normal B cells. In contrast, IL-13 activated STAT6 in
these cells as well as normal B cells. However, Jak3 was not activated
by IL-13, even in normal B cells. These results clearly indicated that
is essential for activation of Jak3 and STAT6 in the
signal transduction pathway of IL-4 in human B cells and that IL-13
does not utilize but activates STAT6 through an
alternative pathway, which is not impaired in B cells of X-linked
severe combined immunodeficiency patients.
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