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J Biol Chem, Vol. 273, Issue 37, 23681-23689, September 11, 1998
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From the The cytokine interleukin-1 (IL-1) is a major
inflammatory hormone which activates a broad range of genes during
inflammation. The signaling mechanisms triggered by IL-1 include
activation of several distinct protein kinase systems. The
stress-activated protein kinase (SAPK), also termed Jun N-terminal
kinase (JNK), is activated particularly strongly by the cytokine. In an
attempt to delineate its role in activation of gene expression by IL-1, we inhibited the IL-1-induced SAPK/JNK activity by stable
overexpression of either a catalytically inactive mutant of SAPK Institute of Molecular Pharmacology, Medical
School Hannover, Carl Neuberg Straße 1, D-30625 Hannover, Germany and
the § Kennedy Institute of Rheumatology, 1 Aspenlea Rd.,
Hammersmith, London W6 8LH, United Kingdom
(SAPK(K-R)) or antisense RNA to SAPK in human epidermal carcinoma
cells. A detailed analysis of signal transduction in those cells showed that activation of neither NF
B nor p38 mitogen-activated protein kinase was affected, suggesting that we achieved specific blockade of
the SAPK/JNK. In untransfected and vector-transfected KB cells, IL-1
induced a strong increase in expression of IL-6 and IL-8 mRNA,
along with the synthesis of high amounts of the proteins. In two KB
cell clones stably overexpressing the mutant SAPK(K-R), and three
clones stably overexpressing antisense RNA to SAPK, expression of
IL-6 and IL-8 in response to IL-1 was strongly reduced at both the
mRNA and protein level. These data indicate that the SAPK/JNK
pathway provides an indispensable signal for IL-1-induced expression of
IL-6 and IL-8.
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