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Phosphatidylethanolamine methylation and hepatoma cell growth.

Abstract
Phosphatidylethanolamine is converted to phosphatidylcholine in hepatocytes via the enzyme phosphatidylethanolamine N-methyltransferase (PEMT). An isoform, PEMT2 has been cloned, expressed and localized to a mitochondria-associated membrane in rat liver. Expression of PEMT2 caused a decreased rate of cell division of cultured rat hepatoma cells. Mechanistic studies suggest that the slower growth of transfected hepatoma cells may be due to down regulation of CTP: phosphocholine cytidylyltransferase and the CDP-choline pathway for phosphatidylcholine biosynthesis. A role for PEMT2 in the regulation of hepatocyte cell division is also indicated by PEMT2 down-regulation in regenerating rat liver.
AuthorsD E Vance, M Houweling, M Lee, Z Cui
JournalAnticancer research (Anticancer Res) 1996 May-Jun Vol. 16 Issue 3B Pg. 1413-6 ISSN: 0250-7005 [Print] Greece
PMID8694509 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References
  • Phosphatidylethanolamines
  • Methyltransferases
  • Phosphatidylethanolamine N-Methyltransferase
  • Nucleotidyltransferases
  • Choline-Phosphate Cytidylyltransferase
Topics
  • Animals
  • Cell Division
  • Choline-Phosphate Cytidylyltransferase
  • Liver Neoplasms, Experimental (metabolism, pathology)
  • Methylation
  • Methyltransferases (physiology)
  • Nucleotidyltransferases (metabolism)
  • Phosphatidylethanolamine N-Methyltransferase
  • Phosphatidylethanolamines (metabolism)
  • Rats

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