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J Biol Chem, Vol. 273, Issue 46, 30729-30735, November 13, 1998
From the Oxysterols exert a major influence
over cellular cholesterol homeostasis. We examined the effects of
oxysterols on the expression of steroidogenic acute regulatory
protein (StAR), which increases the delivery of cholesterol to
sterol-metabolizing P450s in the mitochondria.
22(R)-hydroxycholesterol (22(R)-OHC), 25-OHC,
and 27-OHC each increased steroidogenic factor-1 (SF-1)-mediated StAR gene transactivation by ~2-fold in CV-1 cells. In contrast,
cholesterol, progesterone, and the 27-OHC metabolites,
27-OHC-5
Oxysterol Regulation of Steroidogenic Acute Regulatory Protein
Gene Expression
STRUCTURAL SPECIFICITY AND TRANSCRIPTIONAL AND
POSTTRANSCRIPTIONAL ACTIONS
,
,,
Center for Research on Reproduction and
Women's Health, University of Pennsylvania,
Philadelphia, Pennsylvania 19104, the ¶ Department of Cellular
and Molecular Physiology, Pennsylvania State College of Medicine,
Hershey, Pennsylvania 17033, the Department of Medicine, New
York University Medical Center, New York, New York 10016, and
the ** Department of Molecular Biology and Biochemistry,
University of California, Irvine, California 92717
-3-one and 7
,27-OHC, had no effect. Unlike our findings
in CV-1 cells, SF-1-dependent StAR promoter activity was
not augmented by 27-OHC in COS-1 cells, Y-1 cells, BeWo choriocarcinoma
cells, Chinese hamster ovary (CHO) cells, and human granulosa cells.
Studies examining the metabolism of 27-OHC indicated that CV-1 cells
formed a single polar metabolite, 3-OH-5-cholestenoic acid from
radiolabeled 27-OHC. However, this metabolite inhibited StAR promoter
activity in CV-1, COS-1 and CHO cells. Because 7,27-OHC was unable
to increase SF-1-dependent StAR promoter activity, we
examined 27-OHC 7-hydroxylase in COS-1 and CHO cells. COS-1 cells
contained high 7-hydroxylase activity, whereas the enzyme was
undetectable in CHO cells. The hypothesis that oxysterols act in CV-1
cells to increase StAR promoter activity by reducing nuclear levels of
sterol regulatory element binding protein was tested. This notion was
refuted when it was discovered that sterol regulatory element binding
protein-1a is a potent activator of the StAR promoter in CV-1, COS-1,
and human granulosa cells. Human granulosa and theca cells, which
express endogenous SF-1, contained more than 5-fold more StAR protein
following addition of 27-OHC, whereas StAR mRNA levels remained
unchanged. We conclude that 1) there are cell-specific effects of
oxysterols on SF-1-dependent transactivation; 2) the
ability to increase transactivation is limited to certain oxysterols;
3) there are cell-specific pathways of oxysterol metabolism; and 4)
oxysterols elevate StAR protein levels through posttranscriptional actions.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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