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J Biol Chem, Vol. 273, Issue 6, 3285-3290, February 6, 1998
B p65
Transactivation Mediated by Tumor Necrosis Factor
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From the Interleukin-6 (IL-6) is a pleiotropic cytokine,
which is involved in inflammatory and immune responses, acute phase
reactions, and hematopoiesis. In the mouse fibrosarcoma cell line L929,
the nuclear factor (NF)- Laboratory of Molecular Biology, Flanders
Interuniversity Institute for Biotechnology and University of Gent,
B-9000 Gent, Belgium and the ¶ Department of Immunochemistry,
German Cancer Research Center, D-69120 Heidelberg, Germany
B plays a crucial role in IL-6 gene
expression mediated by tumor necrosis factor (TNF). The levels of the
activated factor do not, however, correlate with the variations of IL-6 gene transcription; therefore, other factors and/or regulatory mechanisms presumably modulate the levels of IL-6 mRNA production. Upon analysis of various deletion and point-mutated variants of the
human IL-6 gene promoter coupled to a reporter gene, we screened for
possible cooperating transcription factors. Even the smallest deletion
variant, containing almost exclusively a NF-B-responsive sequence
preceding the IL-6 minimal promoter, as well as a recombinant construction containing multiple B-motifs, could still be stimulated with TNF. We observed that the p38 mitogen-activated protein kinase (MAPK) inhibitor SB203580 was able to repress TNF-stimulated expression of the IL-6 gene, as well as of a B-dependent reporter
gene construct, without affecting the levels of NF-B binding to DNA.
Furthermore, we clearly show that, using a nuclear Gal4
"one-hybrid" system, the MAPK inhibitors SB203580 and PD0980589
have a direct repressive effect on the transactivation potential of the
p65 B subunit. Therefore, we conclude that, in addition to
cytoplasmic activation and DNA binding of NF-B, the p38 and
extracellular signal-regulated kinase MAPK pathways act as necessary
cooperative mechanisms to regulate TNF-induced IL-6 gene expression by
modulating the transactivation machinery.
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