Why has phosphatidylethanolamine N-methyltransferase survived in evolution?
نویسندگان
چکیده
Lipid Group Colloquium Organized and Edited by D. C. Wilton (Department of Biochemistry, University of Southampton) and A. Postle (Department of Child Health, Southampton General Hospital) and Sponsored by Yamanouchi Research Institute, Sigma-Aldrich Company, British Biotechnology Group, Celltech Therapeutics, Micrornass (UK) and Pharrnacia and Upjohn. 665th Meeting held at Southampton, 3 I March-2 April I998
منابع مشابه
Cloning and expression of a novel phosphatidylethanolamine N-methyltransferase. A specific biochemical and cytological marker for a unique membrane fraction in rat liver.
Phosphatidylethanolamine N-methyltransferase catalyzes the synthesis of phosphatidylcholine from phosphatidylethanolamine and is most active in liver. A cDNA for this enzyme from a rat liver cDNA library has been cloned, sequenced, and expressed in COS-1 cells, McArdle-RH7777 rat hepatoma cells, and Sf9 insect cells. The expressed protein was capable of converting phosphatidylethanolamine into ...
متن کاملIn Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity.
Phosphatidylethanolamine methyltransferases are biosynthetic enzymes that catalyze the transfer of one or more methyl group(s) from S-adenosyl-L-methionine onto phosphatidylethanolamine, monomethyl-phosphatidylethanolamine, or dimethyl-phosphatidylethanolamine to give either monomethyl-phosphatidylethanolamine, dimethyl-phosphatidylethanolamine or phosphatidylcholine. These enzymes are ubiquito...
متن کاملPhosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes.
Choline is an essential nutrient for humans, though some of the requirement can be met by endogenous synthesis catalyzed by phosphatidylethanolamine N-methyltransferase (PEMT). Premenopausal women are relatively resistant to choline deficiency compared with postmenopausal women and men. Studies in animals suggest that estrogen treatment can increase PEMT activity. In this study we investigated ...
متن کاملPlasma homocysteine is regulated by phospholipid methylation.
Mild hyperhomocysteinemia is an independent risk factor for cardiovascular disease. Homocysteine, a non-protein amino acid, is formed from S-adenosylhomocysteine and partially secreted into plasma. A potential source for homocysteine is methylation of the lipid phosphatidylethanolamine to phosphatidylcholine by phosphatidylethanolamine N-methyltransferase in the liver. We show that mice that la...
متن کاملDiminished expression of phosphatidylethanolamine N-methyltransferase 2 during hepatocarcinogenesis.
Phosphatidylethanolamine N-methyltransferase (PEMT) is a liver-specific enzyme that converts phosphatidylethanolamine into phosphatidylcholine. At least two forms of PEMT are present in hepatocytes. However, PEMT activity is negligible in two hepatoma cell lines. Previous studies have indicated an inverse relationship between the expression of one form, PEMT2, and the rate of liver growth, sugg...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 26 3 شماره
صفحات -
تاریخ انتشار 1998