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Papers In Press, published online ahead of print July 1, 2003
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Biochemistry, University of Alberta, Edmonton, Alberta T6G 2S2
Corresponding Author: dennis.vance{at}ualberta.ca
Phosphatidylcholine is made in the liver by the CDP-choline pathway and via phosphatidylethanolamine N-methyltransferase (PEMT) that catalyzes the conversion of phosphatidylethanolamine to phosphatidylcholine. Unexpectedly, hepatic apolipoprotein B100 secretion is inhibited from male, but not female, Pemt-/- mice (Noga, A.A., Zhao, Y. and Vance, D.E., 2002, J. Biol. Chem. 277: 42358-42365; Noga, A.A and Vance, D.E., 2003, J. Biol. Chem. 278: 21851-21859). To gain further insight into this process, we compared phosphatidylcholine metabolism in male and female mice fed chow or a high fat/high cholesterol diet. Immunoblot analyses demonstrated that twice as much PEMT2 was present in livers from female compared to male mice. In contrast, assays of CTP:phosphocholine cytidylyltransferase from livers of Pemt+/+ mice demonstrated more active cytidylyltransferase in male than in female mice. Secretion of PEMT derived phosphatidylcholine into lipoproteins was examined in vivo by injection of mice with [methyl-3H]methionine in the presence of Triton WR1339. The PEMT-derived phosphatidylcholine shifts to smaller sized particles in response to a high fat/high cholesterol diet but only in male mice. Secretion of PEMT-derived phosphatidylcholine into bile was enhanced in mice fed a high fat/high cholesterol diet. These results demonstrate that the synthesis and targeting of phosphatidylcholine produced by the PEMT pathway in the livers of mice differs in a gender- and diet-specific manner.
Revised on June 26, 2003
Accepted on June 26, 2003
Insights into the requirement of phosphatidylcholine synthesis for liver function in mice
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