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J. Biol. Chem., Vol. 276, Issue 27, 24767-24773, July 6, 2001
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,
From the Division of Molecular Medicine, Department of Medicine,
Columbia University, New York, New York 10032
The human cholesteryl ester transfer protein
(CETP) transfers cholesteryl esters from high density lipoproteins to
triglyceride-rich lipoproteins, indirectly facilitating cholesteryl
esters uptake by the liver. Hepatic CETP gene expression is
increased in response to dietary hypercholesterolemia, an effect that
is mediated by the activity of liver X receptor/retinoid X receptor
(LXR/RXR) on a direct repeat 4 element in the CETP
promoter. In this study we show that the orphan nuclear receptor LRH-1
also transactivates the CETP promoter by binding to a
proximal promoter element distinct from the DR4 site. LRH-1 potentiates
the sterol-dependent regulation of the wild type
CETP promoter by LXR/RXR. Small heterodimer partner, a
repressor of LRH-1, abolishes the potentiation effect of LRH-1 but not
its basal transactivation of the CETP promoter. Since this
mode of regulation of CETP is very similar to that recently reported for the bile salt-mediated repression of Cyp7a
(encoding the rate-limiting enzyme for conversion of cholesterol into
bile acid in the liver), we examined the effects of bile salt feeding on CETP mRNA expression in human CETP
transgenic mice. Hepatic CETP mRNA expression was
repressed by a diet containing 1% cholic acid in male mice but was
induced by the same diet in female mice. Microarray analysis of hepatic
mRNA showed that about 1.5% of genes were repressed, and 2.5%
were induced by the bile acid diet. However, the sexually dimorphic
regulatory pattern of the CETP gene was an unusual
response. Our data provide further evidence for the regulation of
CETP and Cyp7a genes by similar molecular mechanisms, consistent with coordinate transcriptional regulation of
sequential steps of reverse cholesterol transport. However, differential effects of the bile salt diet indicate additional complexity in the response of these two genes.
The on-line version of this article (available at
http://www.jbc.org) contains Supplemental Table 1 and Figs.
1 and 2.
To whom correspondence should be addressed: College of Physicians
& Surgeons, 8-401, Division of Molecular Medicine, Dept. of Medicine,
Columbia University, New York, NY 10032. Tel.: 212-305-5789; Fax:
212-305-5052; E-mail: yl220@columbia.edu.
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