Characterization of a novel CI-976-sensitive lysophospholipid acyltransferase that is associated with the Golgi complex

被引：19

作者：

Chambers, K ^{[1
]}

Brown, WJ ^{[1
]}

机构：

[1] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 313卷 / 03期

关键词：

Golgi complex; membrane tubules; lysophospholipid acyltransferase; CI-976;

D O I：

10.1016/j.bbrc.2003.12.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent studies have identified a novel lysophospholipid acyltransferase (LPAT) that is associated with the Golgi complex and that is sensitive to the previously characterized acyl-CoA cholesterol acyltransferase inhibitor, 2,2-methyl-N-(2,4,6-trimethoxyphenyl)dodecanamide (CI-976). Here we show that besides acting on exogenous lysophospholipid (LPL) substrates, the CI-976-sensitive LPAT is also capable of reacylating endogenous Golgi LPL substrates, preferentially lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE). Moreover, using exogenous substrates, we find that the CI-976-sensitive LPAT is capable of using a variety of fatty acyl-CoA donors ranging in chain length from 10 to 20 carbons. Additional characterization demonstrates that the CI-976-sensitive LPAT is ubiquitously expressed in rat tissues, is tightly associated with Golgi membranes, and has a pH optimum between pH 7.0 and 8.0. These studies further define a unique LPC/LPE-specific LPAT from Golgi membranes that likely has a novel function in membrane trafficking. (C) 2003 Elsevier Inc. All rights reserved.

引用

页码：681 / 686

页数：6

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