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J Biol Chem, Vol. 274, Issue 22, 15875-15882, May 28, 1999

Transient Nuclear Factor B (NF-B) Activation Stimulated by Interleukin-1 May Be Partly Dependent on Proteasome Activity, but Not Phosphorylation and Ubiquitination of the IB Molecule, in C6 Glioma Cells
REGULATION OF NF-B LINKED TO CHEMOKINE PRODUCTION

Takashi Uehara, Junko Matsuno, Masayuki Kaneko, Tadashi Nishiya, Masahiro Fujimuro^§, Hideyoshi Yokosawa^§, and Yasuyuki Nomura

From the Departments of  Pharmacology and ^§ Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan

We previously reported that several stresses can induce cytokine-induced neutrophil chemoattractant expression in a nuclear factor B (NF-B)-dependent manner. In this study, we focused further on the regulation of NF-B. The activation of NF-B and the subsequent cytokine-induced neutrophil chemoattractant induction in response to interleukin-1 (IL-1) were inhibited by proteasome inhibitors, MG132 and proteasome inhibitor I. Translocation of NF-B into nuclei occurs by the phosphorylation, multi-ubiquitination, and degradation of IB, a regulatory protein of NF-B. Nascent IB began to degrade 5 min after treatment with IL-1 and disappeared completely after 15 min. However, IB returned to basal levels after 45-60 min. Interestingly, resynthesized IB was already phosphorylated at Ser-32. These results suggest that 1) the upstream signals are still activated, although the translocation of NF-B peaks at 15 min; and 2) the regulated protein(s) acts downstream of IB phosphorylation. Western blotting showed that the resynthesized and phosphorylated IB molecules were also upward-shifted by multi-ubiquitination in response to IL-1 treatment. On the other hand, ATP-dependent Leu-Leu-Val-Tyr cleaving activity transiently increased, peaked at 15 min, and then decreased to basal levels at 60 min. Furthermore, the cytosolic fraction that was stimulated by IL-1 for 15 min, but not for 0 and 60 min, could degrade phosphorylated and multi-ubiquitinated IB. These results indicate that the transient translocation of NF-B in response to IL-1 may be partly dependent on transient proteasome activation.

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