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Papers In Press, published online ahead of print January 14, 2008
Cardiovascular Research, Eli Lilly & Company, Indianapolis, IN 46285
Corresponding Author: guoqing_cao{at}lilly.com
Phosphatidylcholine (PC) is synthesized through the Kennedy pathway but more than 50% of PC is remodeled through Lands cycle, i.e. the deacylation and reacylation of PC to attain the final and proper fatty acids within PC. The reacylation step is catalyzed by lysophosphatidylcholine (LPC) acyltransferase (LPCAT) and we report here the identification of a novel LPCAT, which we named LPCAT3. LPCAT3 belongs to the membrane bound O-acyltransferase (MBOAT) family and encodes a protein of 487 amino acids with a calculated molecular weight of 56 kD. Membranes from HEK293 cells overexpressing LPCAT3 showed significantly increased LPCAT activity as assessed by thin layer chromatography analysis with substrate preference towards unsaturated fatty acids. LPCAT3 is localized within endoplasmic reticulum (ER) and is primarily expressed in metabolic tissues including liver, adipose and pancreas. In a human hepatoma cell line Huh7 cells, RNA interference (RNAi) mediated knockdown of LPCAT3 resulted in virtually complete loss of membrane LPCAT activity suggesting that LPCAT3 is primarily responsible for hepatic LPCAT activity. Furthermore, peroxisome proliferator-activator receptor (PPAR) agonists dose-dependently regulated LPCAT3 in liver in a PPAR-dependent fashion, implicating a role of LPCAT3 in lipid homeostasis. Our studies identify a long-sought enzyme that plays a critical role in PC remodeling in metabolic tissues and provide an invaluable tool for future investigations on how PC remodeling may potentially impact glucose and lipid homeostasis.
J. Biol. Chem, 10.1074/jbc.M710422200
Submitted on December 21, 2007
Revised on January 11, 2008
Accepted on January 14, 2008
Identification and characterization of a lysophosphatidylcholine acyltransferase that is primarily expressed in metabolic tissues
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