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Journal of Lipid Research, Vol. 45, 106-112, January 2004
Copyright © 2004 by American Society for Biochemistry and Molecular Biology

Regulation of apoA-I gene expression

Stefania Lamon-Fava¹ and Dale Micherone

Lipid Metabolism Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging at Tufts University, Boston, MA 02111

¹ To whom correspondence should be addressed. e-mail: stefania.lamon-fava{at}tufts.edu

We have previously shown that 17-ß-estradiol (E₂) and genistein increase the expression of apolipoprotein A-I (apoA-I), the major protein component of HDL, in Hep G2 cells. To elucidate the mechanism mediating the increase in apoA-I gene expression by these compounds, plasmid constructs containing serial deletions of the apoA-I promoter region were generated. The smallest region maintaining response to E₂ and genistein spanned the -220 to -148 sequence, and the estrogen antagonist ICI182,780 completely inhibited the E₂ and genistein effect. Nuclear extracts from cells treated with E₂ and genistein showed increased binding to site B oligonucleotide (-169 to -146), and nuclear extracts from genistein-treated cells showed increased binding to an early growth response factor 1 (Egr-1) oligonucleotide compared to control cells. An increase in the concentrations of Egr-1 and hepatocyte nuclear factor-3ß was observed in nuclear extracts of cells treated with both compounds compared to control cells. Treatment with a specific inhibitor of mitogen-activated protein (MAP) kinase, but not with other inhibitors, abolished the stimulation of apoA-I gene expression by E₂ and genistein.

These results indicate that the MAP kinase pathway is involved in the regulation of apoA-I gene expression by genistein and E₂, possibly through downstream regulation of transcription factors binding to the promoter region.

Supplementary key words apolipoprotein • liver • mitogen-activated protein kinase • early growth response factor 1 • hepatocyte nuclear factor-3ß

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