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Papers In Press, published online ahead of print May 15, 2006
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Division of Applied Life Sciences, Kyoto University, Kyoto 606-8502
Corresponding Author: uedak{at}kais.kyoto-u.ac.jp
Cholesterol and phospholipids are essential to the body, but an excess of cholesterol or lipids is toxic and a risk factor for arteriosclerosis. ABCG1, one of the half-type ABC proteins, is thought to be involved in cholesterol homeostasis. To explore the role of ABCG1 in cholesterol homeostasis, we examined its subcellular localization and function. ABCG1 and ABCG1-K120M, a Walker A lysine mutant, were localized to the plasma membrane in HEK293 cells stably expressing ABCG1, and formed a homodimer. A stable transformant expressing ABCG1 exhibited efflux of cholesterol and choline phospholipids even without a lipid acceptor like apoA-I orin the presence of BSA, which and the cholesterol efflux is was enhanced by the presence of HDL, whereas cells expressing ABCG1-K120M did not, suggesting that ATP binding and/or hydrolysis is required for the efflux. Mass and TLC analyses revealed that ABCG1 and ABCA1 secrete several species of sphingomyelin and phosphatidylcholine, and sphingomyelins were preferentially secreted by ABCG1 and loaded onto HDL, than while phosphatidylcholines were preferentially secreted by ABCA1. These results suggest that ABCA1 and ABCG1 mediate the lipid efflux in different mechanisms, in which different species of phospholipids are secreted, and function coordinately in the removal of cholesterol and phospholipids from peripheral cells.
Revised on May 15, 2006
Accepted on May 15, 2006
Efflux of sphingomyelin, cholesterol and phosphatidylcholine by ABCG1
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