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Vol. 60, Issue 3, 427-431, September 2001
Department of Molecular Endocrinology, GlaxoSmithKline Research and
Development, Research Triangle Park, North Carolina
Cytochromes P450 (P450s) are involved in the oxidative
metabolism of a plethora of structurally unrelated compounds, including therapeutic drugs. Two orphan members of the nuclear receptor superfamily, the pregnane X receptor (PXR; NR1I2) and constitutive androstane receptor (CAR; NR1I3) have been implicated in this phenomenon. In the present study, we examined the transcriptional regulation of the human CYP2B6 gene. In primary cultures
of human hepatocytes, CYP2B6 was highly inducible by a
number of compounds known to be human PXR ligands, including rifampicin
and hyperforin. PXR was shown to be capable of activating the
phenobarbital-responsive enhancer module (PBREM) region of the
CYP2B6 gene, a 51-base-pair enhancer element that
mediates induction of CYP2B6 expression by CAR. The two
nuclear receptor-binding motifs within the PBREM effectively bound PXR
as a heterodimer with the 9-cis retinoic acid receptor
(NR2B1). Taken together, these observations demonstrate that the
CYP2B6 gene is directly regulated by PXR and further establish this receptor as a key regulator of drug-metabolizing P450s.
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