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J Biol Chem, Vol. 273, Issue 51, 34316-34327, December 18, 1998
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From the Departments of Oxysterols regulate the expression of genes
involved in cholesterol and lipid metabolism and serve as intermediates
in cholesterol catabolism. Among the most potent of regulatory
oxysterols is 25-hydroxycholesterol, whose biosynthetic enzyme has not
yet been isolated. Here, we report the cloning of cholesterol
25-hydroxylase cDNAs from the mouse and human. The encoded enzymes
are polytopic membrane proteins of 298 and 272 amino acids,
respectively, which contain clusters of histidine residues that are
essential for catalytic activity. Unlike most other sterol
hydroxylases, cholesterol 25-hydroxylase is not a cytochrome P450, but
rather it is a member of a small family of enzymes that utilize diiron
cofactors to catalyze the hydroxylation of hydrophobic substrates. The
cholesterol 25-hydroxylase gene lacks introns, and in the human it is
located on chromosome 10q23. The murine gene is expressed at low levels in multiple tissues. Expression of cholesterol 25-hydroxylase in
transfected cells reduces the biosynthesis of cholesterol from acetate
and suppresses the cleavage of sterol regulatory element binding
protein-1 and -2. The data suggest that cholesterol 25-hydroxylase has
the capacity to play an important role in regulating lipid metabolism
by synthesizing a co-repressor that blocks sterol regulatory element
binding protein processing and ultimately leads to inhibition of gene transcription.
Molecular Genetics and
§ Cell Biology, University of Texas Southwestern Medical
Center, Dallas, Texas 75235-9046
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