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* Department of Immunology and Host Defenses, Ehime University School of Medicine, Shigenobu, Ehime, Japan; and
Department of Immunology, Graduate School of Medicine, University of Tokyo, Tokyo, Japan
IL-12 is a heterodimer composed of p40 and p35 and is a key
cytokine that functions to protect the host from viral and microbial
infections. IL-12 links the innate immune system with the acquired
immune system during infection, and induces differentiation of type 1 T
cells that play an important role in the eradication of microbes. The
induction of the IL-12 p40 gene is regulated by NF-
B in the presence
of IFN-
. IFN- induces IFN regulatory factor-1 (IRF-1), which in
turn induces the transcription of the IL-12 p40 gene. However, the
IRF-1 binding site in the promoter region of the IL-12 p40 gene has not
yet been formally determined. In the present study, we demonstrated
that IRF-1 directly binds to the IL-12 p40 gene promoter and identified
its binding site. The IRF-1 binding site in the promoter region of the
IL-12 p40 gene is shown to be in the -72 to -58 area of the
5'-upstream region. The -63 to -61 position is the critical site
within this region for the binding of IRF-1 to the IL-12 p40 gene
promoter. While IFN- must be present for IL-12 p40 gene induction,
the p35 gene is strongly induced by LPS, even in the absence of
IFN-, and therefore the induction of the p35 gene is IRF-1
independent.
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