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Journal of Biochemistry 2006 139(3):527-534; doi:10.1093/jb/mvj055
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© 2006 The Japanese Biochemical Society.

Regular Paper

Binding of Steroidogenic Factor-1 to the Regulatory Region Might Not Be Critical for Transcriptional Regulation of the Human CYP1B1 Gene

Yuki Tsuchiya1, Miki Nakajima1, Shingo Takagi1, Miki Katoh1, Wenchao Zheng2, Colin R Jefcoate2 and Tsuyoshi Yokoi1,*

1 Drug Metabolism and Toxicology, Division of Pharmaceutical Sciences, Graduate School of Medical Science, Kanazawa University, Kakuma-machi, Kanazawa 920-1192; and 2 Department of Pharmacology, Medical Science Center, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA

* To whom all correspondence should be addressed. Tel/Fax: +81-76-234-4407, E-mail: TYOKOI{at}kenroku.kanazawa-u.ac.jp

Cytochrome P450 (CYP) 1B1, which catalyzes 17ß-estradiol 4-hydroxylation, is expressed in steroid-related tissues including ovary, testis, and adrenal gland. Generally, the expressions of steroidogenic CYPs are transcriptionally regulated by steroidogenic factor-1 (SF-1) and cAMP response element (CRE) binding protein (CREB). In the present study, we examined the possibility that the human CYP1B1 gene might be regulated by SF-1 and CREB. Gel shift analyses revealed that in vitro translated SF-1 can bind to the putative SF-1 binding sites, SF-1a (at –1722) and SF-1b (at –2474), on the CYP1B1 gene. In vitro translated CREB barely binds to the putative SF-1 binding sites. Luciferase analysis revealed that a reporter plasmid, pGL3 (–2623/+25), containing the SF-1a and SF-1b elements is transactivated by the concomitant co-expression of SF-1 and protein kinase A (PKA). However, the transcriptional activity is induced by PKA alone. Mutations in the SF-1a and SF-1b elements did not affect the luciferase activity. Thus, the binding of SF-1 to the putative SF-1 binding sites of the human CYP1B1 gene might not be essential for transcriptional regulation. Interestingly, deletion and mutation analyses indicated that the PKA signaling pathway is involved in the xenobiotic responsive element (XRE)–mediated transactivation of the human CYP1B1 gene.


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