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Papers In Press, published online ahead of print June 15, 2005
Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2S2
Corresponding Author: dennis.vance{at}ualberta.ca
Biological methylation reactions and homocysteine (Hcy) metabolism are intimately linked. In previous work, we have shown that phosphatidylethanolamine N-methyltransferase (PEMT), an enzyme that methylates phosphatidylethanolamine to form phosphatidylcholine, plays a significant role in the regulation of plasma Hcy levels through an effect on methylation demand (Noga/Stead et al., J. Biol. Chem., 2003 278:5952-5955). We have further investigated methylation demand and Hcy metabolism in liver-specific CTP:phosphocholine cytidylyltransferase-
J. Biol. Chem, 10.1074/jbc.M501971200
Submitted on February 22, 2005
Accepted on June 15, 2005
Physiological regulation of phospholipid methylation alters plasma homocysteine in mice
(CT) knockout mice, since flux through the PEMT pathway is increased two-fold to meet hepatic demand for phosphatidylcholine. Our data show that plasma Hcy is elevated by 20-40% in mice lacking hepatic CT. CT-deficient hepatocytes secrete 40% more Hcy into the medium than do control hepatocytes. Liver activity of betaine:homocysteine methyltransferase and methionine adenosyltransferase are elevated in the knockout mice as a mechanism for maintaining normal hepatic S-adenosylmethionine and S-adenosylhomocysteine levels. These data suggest that phospholipid methylation in the liver is a major consumer of AdoMet and a significant source of plasma Hcy.
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