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Characterization of a Novel CI-976-sensitive Lysophospholipid Acyltransferase That Is Associated With the Golgi Complex

Characterization of a Novel CI-976-sensitive Lysophospholipid Acyltransferase That Is Associated With the Golgi Complex

Kimberly Chambers, William J Brown

Biochem Biophys Res Commun. 2004 Jan 16;313(3):681-6.

PMID: 14697244

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP114289473	CI 976		114289-47-3	Price

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