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J. Biol. Chem., Vol. 266, Issue 26, 17031-17039, Sep, 1991
CN Hahn, AJ Hansen and BK May
The mechanism by which the drugs phenobarbital and 2-allyl-2-
isopropylacetamide induce levels of chicken cytochrome P-450 (CYP) mRNAs
has been investigated in primary hepatocyte cultures from 17-day- old chick
embryos. It has been demonstrated that three CYP mRNAs of 3.5, 2.5, and 2.2
kilobases (kb) are strongly induced by phenobarbital in primary
hepatocytes, as found previously in chick embryo liver in ovo (Hansen, A.
J., Elferink, L. A., and May, B. K. (1989) DNA (NY) 8, 179-191), and that,
at least for the 3.5-kb mRNA, this is predominantly a result of enhanced
transcription of the corresponding gene, CYP2H1. Transient transfection
assays were carried out in primary cultures using constructs containing
different lengths of CYP2H1 gene 5'- flanking sequence fused to the
reporter chloramphenicol acetyl- transferase (CAT) gene. These experiments
established that cis-acting elements located in the first 0.5 kb of the
CYP2H1 gene 5'-flanking region direct high basal expression of the CAT
gene, but do not mediate phenobarbital inducibility. When constructs
containing more than 1.1 kb of CYP2H1 gene 5'-flanking sequence were
examined, phenobarbital induction of CAT expression was observed, and a
drug-responsive domain between positions -5.9 and -1.1 kb was identified.
This domain has the properties of an enhancer, since it is able to confer
phenobarbital responsiveness to the enhancerless SV40 promoter when tested
in either orientation or at different distances from the promoter. The
enhancer domain also responds to 2-allyl-2-isopropylacetamide, but whether
the action of the two drugs is mediated by a single nuclear receptor
interacting with common DNA elements in the domain remains to be
established.
Transcriptional regulation of the chicken CYP2H1 gene. Localization of a phenobarbital-responsive enhancer domain
Department of Biochemistry, University of Adelaide, South Australia.
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