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Papers In Press, published online ahead of print November 16, 2004
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Human Nutrition and Metabolism, Hebrew University Medical School, Jerusalem 91120
Corresponding Author: bartanaj{at}cc.huji.ac.il
Microsomal triglyceride transfer protein (MTP) catalyzes the assembly of triglycerides-rich apoB-containing liver (e.g., VLDL) and intestinal (e.g., chylomicrons) lipoproteins. The human MTP gene promoter is reported here to associate in vivo with endogenous hepatocyte nuclear factor-4
Revised on November 3, 2004
Accepted on November 9, 2004
Transcriptional regulation of human microsomal triglyceride transfer protein by hepatocyte nuclear factor-4
(HNF-4) and to be transactivated or transuppressed by overexpressed or by dominant negative HNF-4, respectively. hMTP transactivation by HNF-4 is accounted for by the concerted activity of a distal (-83/-70) and proximal (-50/-38) DR1 elements of the hMTP core promoter that bind HNF-4. Transactivation by HNF-4 is specifically antagonized by COUP. Transcriptional activation of hMTP by HNF-4 is mediated by HNF-4 domains engaged in ligand binding and ligand driven transactivation, and is further complemented by HNF-4/HNF-1 synergism that involves the HNF-4 AF-1 domain. hMTP transactivation by HNF-4 is specifically inhibited by Medica 16 acting as HNF-4 antagonist ligand. hMTP transactivation by HNF-4 may account for activation or inhibition of MTP expression and the production of TG-rich lipoproteins by agonist (e.g., saturated fatty acids) or antagonist (e.g., (n-3) PUFA, hypolipidemic fibrate or Medica compounds) HNF-4 ligands, respectively.
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