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J. Biol. Chem., Vol. 277, Issue 28, 25125-25132, July 12, 2002
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,
From INSERM U128, Institut Federatif de Recherche 24, CNRS,
1919 Route de Mende, 34293 Montpellier, Cedex 05, France
The fully active dihydroxylated metabolite of
vitamin D3 induces the expression of
CYP3A4 and, to a lesser extent, CYP2B6 and
CYP2C9 genes in normal differentiated primary human
hepatocytes. Electrophoretic mobility shift assays and cotransfection
in HepG2 cells using wild-type and mutated oligonucleotides revealed
that the vitamin D receptor (VDR) binds and transactivates those
xenobiotic-responsive elements (ER6, DR3, and DR4) previously
identified in CYP3A4, CYP2B6, and
CYP2C9 promoters and shown to be targeted by the pregnane X
receptor (PXR) and/or the constitutive androstane receptor (CAR). Full
VDR response of various CYP3A4 heterologous/homologous
promoter-reporter constructs requires both the proximal ER6 and the
distal DR3 motifs, as observed previously with rifampicin-activated
PXR. Cotransfection of a CYP3A4 homologous
promoter-reporter construct (including distal and proximal PXR-binding
motifs) and of PXR or CAR expression vectors in HepG2 cells revealed
the ability of these receptors to compete with VDR for transcriptional
regulation of CYP3A4. In conclusion, this work suggests
that VDR, PXR, and CAR control the basal and inducible expression of
several CYP genes through competitive interaction with the
same battery of responsive elements.
Supported by Glaxo Wellcome.
§
To whom correspondence should be addressed. Tel.: 33-4-6761-3369;
Fax: 33-4-6752-3681; E-mail: vilarem@falbala.crbm.cnrs-mop.fr.
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