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J Biol Chem, Vol. 275, Issue 17, 12676-12683, April 28, 2000

Superinduction of CYP1A1 Gene Expression
REGULATION OF 2,3,7,8-TETRACHLORODIBENZO-p-DIOXIN-INDUCED DEGRADATION OF Ah RECEPTOR BY CYCLOHEXIMIDE*

Qiang MaDagger §, Anthony J. RenzelliDagger , Kimberly T. BaldwinDagger , and James M. Antonini

From the Dagger  Molecular Toxicology Laboratory, Toxicology and Molecular Biology Branch, and  Pathology and Physiology Research Branch, Health Effects Laboratory Division, NIOSH, National Institutes of Health, Centers for Disease Control and Prevention, Morgantown, West Virginia 26505

Cycloheximide superinduces the transcription of CYP1A1 in the presence of an agonist for the Ah receptor (AhR). To investigate the molecular target for "superinduction," we analyzed the agonist-induced degradation of AhR. Whereas 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a potent agonist of AhR, induces a rapid reduction of the AhR protein, cycloheximide blocks the down-regulation of steady state AhR. Analyses of the turnover of AhR reveal that cycloheximide blocks the shortening of the half-life of AhR by TCDD. Blocking of the TCDD-induced AhR degradation requires inhibition of protein synthesis, because (a) cycloheximide inhibits protein synthesis at the concentration at which it causes superinduction and inhibition of AhR degradation; and (b) puromycin, an inhibitor of protein synthesis by mimicking aminoacyl-tRNA, also blocks the TCDD-induced AhR degradation. The blocking of the TCDD-induced AhR degradation correlates with the superinduction of CYP1A1 gene expression in a time- and dose-dependent manner. Furthermore, cycloheximide is shown to increase the accumulation of the TCDD-activated AhR and the functional AhR·Arnt complex in nucleus. Collectively, our results reveal a mechanism of superinduction by cycloheximide by enhancing the stability of agonist-activated AhR. The finding that inhibition of protein synthesis blocks the TCDD-induced AhR turnover implicates a cycloheximide-sensitive, labile factor (designated as AhR degradation promoting factor, or ADPF) in controlling the removal of agonist-activated AhR in nucleus.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: CDC/NIOSH/HELD/TMBB, Mailstop 3014, 1095 Willowdale Rd., Morgantown, WV 26505. Tel.: 304-285-6241; Fax: 304-285-5708.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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