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J Biol Chem, Vol. 273, Issue 15, 9270-9278, April 10, 1998
From the Department of Nuclear Receptors, Wyeth-Ayerst Research,
Radnor, Pennsylvania 19087
Estrogen replacement therapy increases plasma
concentrations of high density lipoprotein and its major protein
constituent, apolipoprotein AI (apoAI). Studies with animal model
systems, however, suggest opposite effects. In HepG2 cells stably
expressing estrogen receptor
Estrogen Regulation of the Apolipoprotein AI Gene Promoter
through Transcription Cofactor Sharing
(ER), 17
-estradiol (E2) potently
inhibited apoAI mRNA steady state levels. ApoAI promoter deletion
mapping experiments indicated that ER plus E2 inhibited apoAI
activity through the liver-specific enhancer. Although the ER DNA
binding domain was essential but not sufficient for apoAI enhancer
inhibition, ER binding to the apoAI enhancer could not be detected
by electrophoretic mobility shift assays. Western blotting and
cotransfection assays showed that ER plus E2 did not influence the
abundance or the activity of the hepatocyte-enriched factors HNF-3
and HNF-4, two transcription factors essential for apoAI enhancer
function. Expression of the ER coactivator RIP140 dramatically
repressed apoAI enhancer function in cotransfection experiments,
suggesting that RIP140 may also function as a coactivator on the apoAI
enhancer. Moreover, estrogen regulation of apoAI enhancer activity was
dependent upon the balance between ER and RIP140 levels. At low
ratios of RIP140 to ER, E2 repressed apoAI enhancer activity,
whereas at high ratios this repression was reversed. Regulation of the apoAI gene by estrogen may thus vary in direction and magnitude depending not only on the presence of ER and E2 but also upon the
intracellular balance of ER and coactivators utilized by ER and
the apoAI enhancer.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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