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B Activity by the Novel Quinone Derivative E33301
*
Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama;
Department of Clinical Development Section, Eisai Co., Ltd., Tokyo;
Department of Anatomy, Nihon University School of Medicine, Tokyo; and
§
Second Department of Internal Medicine, Asahikawa Medical College, Asahikawa, Japan
The activation of NF-
B consists of at least three steps:
degradation of IB
, translocation of NF-B into the nucleus, and
post-translational modification of NF-B (e.g., phosphorylation of
p65). In the present study, we found that a novel quinone derivative
E3330 selectively inhibited NF-B-mediated gene expression without
affecting any of these steps. E3330, when included in the culture
medium, suppressed NF-B DNA-binding activity in PMA-induced Jurkat
cell nuclear extracts, suggesting that the inhibition by E3330 of
NF-B-mediated gene expression was due to its ability to suppress
NF-B DNA-binding activity. Fractionation of the nuclear extracts by
column chromatography revealed that a nuclear factor enhanced NF-B
DNA-binding activity and that this enhancing activity was interrupted
after treatment with E3330. Moreover, a major polypeptide with a
molecular mass of 40 kDa was found to be in the highly purified
fraction containing the NF-B-enhancing activity and predominantly
bind E3330. Taken together, these results suggest that the NF-B
activity, after dissociation from IB, is enhanced by a nuclear
factor that is active irrespective of PMA treatment, and the nuclear
factor-mediated enhancement is selectively inhibited by E3330. Thus, we
conclude that E3330 may belong to a novel class of anti-NF-B
drugs.
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