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J Biol Chem, Vol. 273, Issue 30, 18959-18965, July 24, 1998
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From the We have examined the regulation of apolipoprotein
A-I (apoA-I) gene expression in response to glucose and insulin. In Hep G2 cells, endogenous apoA-I mRNA was suppressed by one-half or induced 2-fold following 48 h of exposure to high concentrations of glucose (22.4 mM) or insulin (100 microunits/ml),
respectively, compared with control. Transcriptional activity of the
rat apoA-I promoter ( Endocrine Research Group, Departments of
Medicine and Medical Biochemistry, the Faculty of Medicine, University
of Calgary, Calgary, Alberta T2N 4N1, Canada and the ¶ St. Louis
Veterans Affairs Medical Center and Division of Endocrinology,
Department of Internal Medicine, St. Louis University,
St. Louis, Missouri, 63104
474 to 7) in Hep G2 cells paralleled
endogenous mRNA expression, and this activity was dependent on the
dose of glucose or insulin. Deletional analysis showed that a 50-base
pair fragment spanning 425 to 376 of the promoter mediated the
effects of both insulin and glucose. Within this DNA fragment there is
a motif (411 to 404) that is homologous to a previously identified insulin response core element (IRCE). Mutation of this motif abolished not only the induction of the promoter by insulin but also abrogated its suppression by glucose. Electrophoretic mobility shift assay analysis of nuclear extracts from Hep G2 cells revealed IRCE binding activity that formed a duplex with radiolabeled probe. The IRCE binding
activity correlated with insulin induction of apoA-I expression. In
summary, our data show that glucose decreases and insulin increases apoA-I promoter activity. This effect appears to be mediated by a
single cis-acting element.
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