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Vol. 56, Issue 6, 1329-1339, December 1999
Department of Clinical Pharmacology and Storr Liver Unit,
University of Sydney at Westmead Hospital, Westmead, Australia
Cytochrome P-450 3A4 (CYP3A4), the predominant cytochrome P-450
expressed in adult human liver, is subject to transcriptional induction
by a variety of structurally unrelated xenobiotics, including the
antibiotic rifampicin. The molecular mechanisms underlying this
phenomenon are poorly understood. We transfected a human liver-derived
cell line (HepG2) with various CYP3A4-luciferase reporter gene constructs containing a nested set of 5'-deletions of the
CYP3A4 5'-flanking region. Rifampicin-inducible
transcription of the reporter gene was observed only with the longest
construct, which encompassed bases 
13000 to +53 of
CYP3A4 (3-fold induction). The responsive region was
functional regardless of its position or orientation relative to the
proximal promoter of CYP3A4 and was capable of
conferring rifampicin-inducible expression on a heterologous promoter.
Further deletion mutants localized the induction to bases 7836 to
7607. In vitro DNase I footprint analysis of this region revealed
four protected sites (FP1, FP2, FP3, and FP4). Two of these sites, FP3
(bases 7738 to 7715) and FP4 (bases 7698 to 7682), overlapped
binding motifs for the orphan human pregnane X receptor (hPXR).
Cotransfection of responsive constructs with a hPXR expression vector
substantially increased the rifampicin-inducibility to ~50-fold. In
addition, the rifampicin-responsive constructs were strongly activated
by a range of CYP3A inducers. Finally, we demonstrate
cooperativity between elements within the distal enhancer region and
cis-acting elements in the proximal promoter of
CYP3A4. Our results provide evidence for the existence
of a potent enhancer module, 8 kb distal to the transcription start
point, which mediates the transcriptional induction of
CYP3A4 by activators of hPXR.
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