Disappearance of two major phosphatidylcholines from plasma is predominantly via LCAT and hepatic lipase
Disappearance of two major phosphatidylcholines from plasma is predominantly via LCAT and hepatic lipase
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DOI:
10.1152/ajpendo.1996.271.6.e1073
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发表时间:
1996-12-01
影响因子:
5.1
通讯作者:
Schwartz, CC
中科院分区:
文献类型:
--
作者:
Shamburek, RD;Zech, LA;Schwartz, CC
Metabolism of 1-stearoyl-2-arachidonyl-phosphatidylcholine (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 H-3 and C-14 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 H-3 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 A(1) hydrolysis of plasma SAPC forming 2-arachidonyl-lysophosphatidylcholine, which was reacylated in the liver. Plasma PLPC also underwent phospholipase A(1) hydrolysis, as reported previously. The fraction of H-3 dose that accumulated in plasma cholesteryl arachidonate was two- to threefold higher than the fraction of C-14 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 A(1) (hepatic lipase) hydrolysis accounted for greater than or equal to 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.