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Blood, Vol. 93 No. 12 (June 15), 1999:
pp. 4318-4327
Interleukin-9 Regulates NF- B Activity Through BCL3 Gene
Induction
Mélisande Richard,
Jamila Louahed,
Jean-Baptiste Demoulin, and
Jean-Christophe Renauld
From the Ludwig Institute for Cancer Research, Brussels Branch,
Brussels, Belgium; and the Experimental Medicine Unit, Christian de
Duve Institute of Cellular Pathology, Université Catholique de
Louvain, Brussels, Belgium.
BCL3 encodes a protein with close homology to I B proteins
and interacts with p50 NF-B homodimers. However, the regulation and
transcriptional activity of BCL3 remain ill-defined. We observed here
that interleukin-9 (IL-9) and IL-4, but not IL-2 or IL-3, transcriptionally upregulated BCL3 expression in T cells and
mast cells. BCL3 induction by IL-9 was detected as soon as 4 hours after stimulation and appeared to be dependent on the Jak/STAT pathway. IL-9 stimulation was associated with an increase in p50 homodimers DNA binding activity, which was mimicked by stable BCL3 expression. This contrasts with tumor necrosis factor
(TNF)-dependent NF-B activation, which occurs earlier, involves
p65/p50 dimers, and is dependent on IB degradation. Moreover, IL-9
stimulation or BCL3 transient transfection similarly inhibited
NF-B-mediated transcription in response to TNF. Taken together, our
observations show a new regulatory pathway for the NF-B
transcription factors through STAT-dependent upregulation of
BCL3 gene expression.
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