Chambers Kimberly, Brown William J
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Biochem Biophys Res Commun. 2004 Jan 16;313(3):681-6. doi: 10.1016/j.bbrc.2003.12.016.
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.
最近的研究鉴定出一种新型溶血磷脂酰转移酶（LPAT），它与高尔基体复合物相关，并且对先前已表征的酰基辅酶A胆固醇酰基转移酶抑制剂2,2-甲基-N-(2,4,6-三甲氧基苯基)十二烷酰胺（CI-976）敏感。在此我们表明，除了作用于外源性溶血磷脂（LPL）底物外，CI-976敏感的LPAT还能够使内源性高尔基体LPL底物再酰化，优先是溶血磷脂酰胆碱（LPC）和溶血磷脂酰乙醇胺（LPE）。此外，使用外源性底物，我们发现CI-976敏感的LPAT能够使用多种链长在10至20个碳之间的脂肪酰基辅酶A供体。进一步的表征表明，CI-976敏感的LPAT在大鼠组织中普遍表达，与高尔基体膜紧密相关，并且最适pH在7.0至8.0之间。这些研究进一步定义了一种来自高尔基体膜的独特的LPC/LPE特异性LPAT，它可能在膜运输中具有新功能。
