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J. Biol. Chem., Vol. 265, Issue 14, 8190-8197, 05, 1990
DF Jelinek, S Andersson, CA Slaughter and DW Russell
The rate-limiting step in bile acid biosynthesis is catalyzed by the
microsomal cytochrome P-450 cholesterol 7 alpha-hydroxylase (7 alpha-
hydroxylase). The expression of this enzyme is subject to feedback
regulation by sterols and is thought to be coordinately regulated with
enzymes in the cholesterol supply pathways, including the low density
lipoprotein receptor and 3-hydroxy-3-methylglutaryl-coenzyme A reductase
and synthase. Here we report the purification of rat 7 alpha- hydroxylase
and the determination of a partial amino acid sequence. Oligonucleotides
derived from peptide sequence were used to clone a full-length cDNA
encoding 7 alpha-hydroxylase. DNA sequence analysis of the cDNA revealed a
7 alpha-hydroxylase protein of 503 amino acids with a predicted molecular
weight of 56,890 which represents a novel family of cytochrome P-450
enzymes. Transfection of a 7 alpha-hydroxylase cDNA into simian COS cells
resulted in the synthesis of a functional enzyme whose activity was
stimulated in vitro by the addition of rat microsomal cytochrome P-450
reductase protein. RNA blot hybridization experiments indicated that the
mRNA for 7 alpha-hydroxylase is found only in the liver. The levels of this
mRNA increased when bile acids were depleted by dietary cholestyramine and
decreased when bile acids were consumed. Dietary cholesterol led to an
increase in 7 alpha- hydroxylase mRNA levels. The enzymatic activity of 7
alpha-hydroxylase paralleled the observed changes in mRNA levels. These
results suggest that bile acids and sterols are able to alter the
transcription of the 7 alpha-hydroxylase gene and that this control
explains the previously observed feedback regulation of bile acid
synthesis.
Cloning and regulation of cholesterol 7 alpha-hydroxylase, the rate- limiting enzyme in bile acid biosynthesis
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
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