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B-Dependent IL-6 Expression in Human Monocytes1
*
Division of Hematology, Department of Medicine, and
Division of Developmental Genetics, Department of Biology, University of Groningen, Groningen, The Netherlands
In the present study we investigated the possible involvement of
the mitogen-activated protein kinase family members
extracellular-regulated kinase 1/2 (ERK1/2) and c-Jun N-terminal kinase
(JNK) in mediating IL-6 gene expression in human monocytes, in
particular their role in enhancing NF-
B activity. Freshly isolated
monocytes treated with the protein phosphatase inhibitor okadaic acid
secreted high levels of IL-6 protein, which coincided with enhanced
binding activity of NF-B as well as with phosphorylation and
activation of the ERK1/2 and JNK proteins. The ERK pathway-specific
inhibitor PD98059 inhibited IL-6 secretion from monocytes. Transient
overexpression of inactive mutants of either Raf-1 or JNK1 showed that
both pathways were involved in B-dependent IL-6 promoter activity.
By using PD98059, we demonstrated that the Raf1/MEK1/ERK1/2 pathway did
not affect the DNA binding of NF-B but, rather, acted at the level
of transcriptional activity of NF-B. Interestingly, it was shown
that NF-B-mediated gene transcription, both in the context of the
IL-6 promoter as well as on its own, was dependent on both serine
kinase activity and interaction with c-Jun protein. We conclude that
okadaic acid-induced IL-6 gene expression is at least partly mediated
through the ERK1/2 and JNK pathway-dependent activation of NF-B
transcriptional capacity. Our results suggest that the JNK pathway may
regulate NF-B-mediated gene transcription through its
phosphorylation and activation of c-Jun.
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