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(Received for publication, February 24, 1997, and in revised form, May 27, 1997)
From the Mammalian Cell and Molecular Biology Laboratory,
Department of Biology and Molecular Biology Institute, San Diego State
University, San Diego, California 92182-0057
Stable plasmid-driven expression of the
liver-specific gene product cholesterol 7
-hydroxylase
(7-hydroxylase) was used to alter the cellular content of
transcriptionally active sterol response element binding protein 1 (SREBP1). As a result of stable expression of 7-hydroxylase,
individual single cell clones expressed varying amounts of mature
SREBP1 protein. These single cell clones provided an opportunity to
identify SREBP1-regulated genes that may influence the assembly and
secretion of apoB-containing lipoproteins. Our results show that in
McArdle rat hepatoma cells, which normally do not express
7-hydroxylase, plasmid-driven expression of 7-hydroxylase results
in the following: 1) a linear relationship between (i) the cellular
content of mature SREBP1 and 7-hydroxylase protein, (ii) the
relative expression of 7-hydroxylase mRNA and the mRNA's encoding the enzymes regulating fatty acid, i.e. acetyl-CoA
carboxylase and sterol synthesis, i.e. HMG-CoA reductase,
(iii) the relative expression of 7-hydroxylase mRNA and
microsomal triglyceride transfer protein mRNA, a gene product that
is essential for the assembly and secretion of apoB-containing
lipoproteins; 2) increased synthesis of all lipoprotein lipids
(cholesterol, cholesterol esters, triglycerides, and phospholipids);
and 3) increased secretion of apoB100 without any change in apoB
mRNA. Cells expressing 7-hydroxylase contained significantly
less cholesterol (both free and esterified). The increased cellular
content of mature SREBP1 and increased secretion of apoB100 were
concomitantly reversed by 25-hydroxycholesterol, suggesting that the
content of mature SREBP1, known to be decreased by
25-hydroxycholesterol, mediates the changes in the lipoprotein assembly
and secretion pathway that are caused by 7-hydroxylase. These data
suggest that several steps in the assembly and secretion of
apoB-containing lipoproteins by McArdle hepatoma cells may be
coordinately linked through the cellular content of mature SREBP1.
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