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J Biol Chem, Vol. 274, Issue 42, 29749-29754, October 15, 1999
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From the Intestinal bile acid-binding protein (I-BABP) is
a cytosolic protein that binds bile acids (BAs) with a high affinity.
In the small intestine, its expression is restricted to the ileum where
it is involved in the enterohepatic circulation of BAs. Using the human
enterocyte-like Caco-2 cell line, we have recently shown that BAs
increased I-BABP gene expression. To determine whether this regulation
occurs in vivo, the effect of BA depletion or
supplementation was studied in mice. A dramatic drop in I-BABP mRNA
levels was observed in mice treated with the BA-binding resin cholestyramine, whereas an increase was found in animals fed with taurocholic acid. BAs are physiological ligands for the nuclear farnesoid X receptor (FXR). Both FXR and I-BABP are co-expressed along
the small intestine and in Caco-2 cells. To determine the role of FXR
in the regulation of I-BABP expression, the promoter of the human
I-BABP gene was cloned. In Caco-2 cells, cotransfection of FXR and
RXR Physiologie de la Nutrition, Ecole Nationale
Supérieure de Biologie Appliquée à la Nutrition et
à l'Alimentation, EP 1777 CNRS-CESG, F- 21000, Dijon, France,
the ¶ Department of Biochemistry, Niigata University School of
Medecine, 1-757 Asahimachi-dori, Niigata 951, Japan, and the
Departments of Molecular Endocrinology and ** Medicinal
Chemistry, Glaxo Wellcome Research and Development,
Research Triangle Park, North Carolina 27709
is required to obtain the full transactivation of the I-BABP
promoter by BAs. Deletion and mutation analyses demonstrate that the
FXR/RXR heterodimer activates transcription through an inverted
repeat bile acid responsive element located in position 
160/148 of
the human I-BABP promoter. In conclusion, we show that FXR is a
physiological BA sensor that is likely to play an essential role in BA
homeostasis through the regulation of genes involved in their
enterohepatic circulation.
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