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Journal of Biochemistry Advance Access originally published online on March 20, 2009
Journal of Biochemistry 2009 146(1):113-122; doi:10.1093/jb/mvp049
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Placenta Expressing the Greatest Quantity of Bisphenol A Receptor ERR{gamma} among the Human Reproductive Tissues: Predominant Expression of Type-1 ERR{gamma} Isoform

Yukimasa Takeda1,*, Xiaohui Liu1, Miho Sumiyoshi2, Ayami Matsushima1, Miki Shimohigashi2 and Yasuyuki Shimohigashi1,{dagger}

1Laboratory of Structure-Function Biochemistry, Department of Chemistry, The Research- Education Centre of Risk Science, Faculty of Sciences, Kyushu University, Fukuoka 812-8581; and 2Division of Biology, Faculty of Science, Fukuoka University, Fukuoka 814-0180, Japan

{dagger}To whom correspondence should be addressed. Tel/Fax: +81-92-642-2584, E-mail: shimo{at}chem.kyushu-univ.jp

Received February 19, 2009; Accepted March 7, 2009


  Abstract

Estrogen-related receptor {gamma} (ERR{gamma}), one of the 48 human nuclear receptors, has a fully active conformation with no ligand. We recently demonstrated that ERR{gamma} binds strongly bisphenol A (BPA), one of the nastiest endocrine disruptors, and thus retaining ERR{gamma}'s high basal constitutive activity. A report that BPA accumulates in the human maternal–fetal placental unit has led us to hypothesize that a large amount of ERR{gamma} might exist in the human placenta. Here we report evidence that placenta indeed expresses ERR{gamma} exceptionally strongly. We first ascertained the presence of nine different ERR{gamma} mRNA variants and the resulting three ERR{gamma} protein isoforms. By real-time PCR, we estimated the relative amount of ERR{gamma} mRNA using total RNA extracts from human reproductive tissues. Placenta was found to express ERR{gamma} extremely highly. Among the three ERR{gamma} protein isoforms, placenta exclusively expresses the type-1 isoform, which possesses additional 23-mer amino-acid residues at the N-terminus of the ordinary ERR{gamma}. This N-terminal elongation was found to elevate by approximately 50% the basal constitutive activity of ERR{gamma}, as evidenced in the luciferase reporter gene assay. The present results suggest that BPA accumulates in the placenta by binding to ERR{gamma}.

Key Words: alternative splicing, bisphenol A receptor, estrogen-related receptor {gamma}, placenta, real-time PCR

Abbreviations: AR, androgen receptor; BPA, bisphenol A; ER, estrogen receptor; ERR, estrogen-related receptor; ERRE, ERR-response element; ERR{gamma}, estrogen-related receptor {gamma}; NRs, nuclear receptors; 4-OHT, 4-hydroxytamoxifen

*Present address: Cell Biology Section, Laboratory of Respiratory Biology, NIH-NIEHS, Research Triangle Park, NC 27709, USA.


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