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Am J Physiol. 1996 Dec;271(6 Pt 1):E1073-82.

Disappearance of two major phosphatidylcholines from plasma is predominantly via LCAT and hepatic lipase.

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  • 1Department of Medicine, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298, USA.


Metabolism of 1-stearoyl-2-arachidonyl-phosphatidyl-choline (SAPC), a major phosphatidylcholine (PC) species in rat plasma, was compared with 1-palmitoyl-2-linoleoyl-PC (PLPC) metabolism. High-density lipoproteins containing SAPC and PLPC tracers labeled in the sn-2 fatty acid with 3H and 14C isotopes, respectively, were administered. The rats were depleted of endogenous bile acids and infused via the ileum with individual bile acids that ranged widely in hydrophobicity. The half-lives for SAPC and PLPC in plasma were 48 and 57 min, respectively. Most of the 3H activity that disappeared from plasma at 1 h was found in the liver in 1-palmitoyl-2-arachidonyl-PC, SAPC, and 1-oleoyl-2-arachidonyl-PC, indicating phospholipase A1 hydrolysis of plasma SAPC forming 2-arachidonyl-lysophosphatidylcholine, which was reacylated in the liver. Plasma PLPC also underwent phospholipase A1 hydrolysis, as reported previously. The fraction of 3H dose that accumulated in plasma cholesteryl arachidonate was two- to threefold higher than the fraction of 14C dose in cholesteryl linoleate. Multicompartmental models for SAPC and PLPC were developed that included lysophosphatidylcholines and cholesteryl esters. Bile acids did not influence plasma PC metabolism. Lecithin-cholesterol acyltransferase and phospholipase A1 (hepatic lipase) hydrolysis accounted for > or = 90% of the SAPC and PLPC that disappeared from plasma; SAPC and PLPC are comparable as substrates for hepatic lipase, but SAPC is preferred by lecithin-cholesterol acyltransferase.

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