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Articles in PresS, published online ahead of print April 24, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00308.2001
Submitted on July 6, 2001
Accepted on April 15, 2002
1 Nutrition and Food Science, University of Maryland, College Park, MD
2 Nutrition and Food Science, University of Maryland, College Park, MD, none
* To whom correspondence should be addressed. E-mail: DL165{at}umail.umd.edu.
This study was designed to examine the influence of zinc status on the expression of certain transcription factors known to be involved in the regulation of apolipoprotein A-I
expression in the human hepatoblastoma HepG2 cells. A low zinc basal medium (zinc-deficient,ZD), consisting of DMEM and 10% Chelex100-treated fetal bovine serum, was used to deplete cellular zinc over one passage. Cells were also cultured for one passage in media supplemented with 0.4 (ZD0.4), 4.0 (zinc-normal, ZN), 16.0 (zinc-adequate,
ZA), or 32.0 µM of zinc (zinc-supplemented, ZS). As compared to ZN cells, cellular zinc levels were 43% and 31% lower in ZD and ZD0.4 cells but 70% and 146% higher in ZA and ZS cells, respectively. Supplementation of 0.4 µM zinc significantly increased the DNA contents per plate, from 65% in ZD cells to 83% in ZD0.4 cells, as compared to ZN cells. Addition of more than 4 µM of zinc in medium did not further increase the DNA contents. The proportion of cells in G1/S and S phase were about 4-fold higher and 3-fold lower, respectively, in ZD cells as compared to ZN and other groups. Nuclear Egr-1 protein was markedly decreased in the ZD and ZD0.4 cells. Moreover, hepatocyte nuclear factor HNF-3ß was severely degraded in ZD and ZD0.4
cells. In contrast, hepatocyte nuclear factor HNF-4
remained stable in all groups, and was not significantly lower in ZD and ZD0.4 cells. Furthermore, the down-regulation of trans-acting factors Egr-1 and cleavage of HNF-3ß were associated with a reduction of
apoA-I promoter activity in zinc-deficient HepG2 cells. Thus, zinc is critical in the transcriptional regulation of apoA-I gene expression in hepatocytes.
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