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PMID: 18458083 Published · ppublish English Journal Article

Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2.

The Journal of biological chemistry ·Vol. 283 ·No. 27 ·2008-07-04 ·Pages 19049-57

Cao J, Shan D, Revett T, Li D, Wu L, Liu W, Tobin JF, Gimeno RE

Abstract

Acyl-CoA-dependent lysophospholipid acyltransferases play an important role in attaining the appropriate molecular species of phospholipids. A number of genes encoding these activities were recently identified. It has become clear that multiple genes can encode one enzymatic activity and that a given gene may encode multiple activities. Here we report the identification of a gene encoding a mammalian acyl-CoA-dependent lysophospholipid acyltransferase with prominent activity toward ethanolamine-containing lysophospholipids, which we termed acyl-CoA:lysophosphatidylethanolamine acyltransferase 2, LPEAT2 (previously annotated as AYTL3 or AGPAT7). LPEAT2 is predominantly expressed in brain, coinciding with an enrichment of phosphatidylethanolamine in this tissue. Ectopic expression of LPEAT2 in mammalian HEK293T cells led to a dramatic increase (up to 9-fold) in LPEAT activity when compared with cells transfected with empty vector or an unrelated acyltransferase. LPEAT2 also exhibited significant acyl-CoA-dependent acyltransferase activity toward 1-O-alkenyl-lysophosphatidylethanolamine, lysophosphatidylglycerol, 1-O-alkyl-lysophosphatidylcholine, lysophosphatidylserine, and lysophosphatidylcholine but lacked appreciable acylating activity toward glycerol 3-phosphate, lysophosphatidic acid, lysophosphatidylinositol, and diacylglycerol, demonstrating multiple but selective functions of LPEAT2 as an enzyme involved in phospholipid remodeling. LPEAT2 recognizes a broad range of medium and long chain fatty acyl-CoA, and its activity was not affected by Ca(2+). When overexpressed in mammalian cells, LPEAT2 is localized to the endoplasmic reticulum. siRNA-mediated knockdown of LPEAT2 in HEK293T cells significantly decreased LPEAT and 1-alkenyl-LPEAT activities but did not affect other lysophospholipid acylating activities. These findings identify LPEAT2 as an important enzyme in the biosynthesis of ethanolamine-containing phospholipids, especially in brain.

MeSH Terms
1-Acylglycerol-3-Phosphate O-Acyltransferase/genetics,metabolism 1-Acylglycerophosphocholine O-Acyltransferase Brain/enzymology Cell Line Endoplasmic Reticulum/enzymology,genetics Humans Isoenzymes/genetics,metabolism Lysophospholipids/biosynthesis,genetics Nerve Tissue Proteins/genetics,metabolism Organ Specificity/physiology Substrate Specificity/physiology
Chemicals
Isoenzymes Lysophospholipids Nerve Tissue Proteins 1-Acylglycerophosphocholine O-Acyltransferase LPCAT4 protein, human 1-Acylglycerol-3-Phosphate O-Acyltransferase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Cao Jingsong
Department of Cardiovascular and Metabolic Diseases, Wyeth Research, Cambridge, Massachusetts 02140, USA. [email protected]
Shan Dandan
Revett Tracy
Li Dongmei
Wu Leeying
Liu Wei
Tobin James F
Gimeno Ruth E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2008-07-04
Epub
2008-00-05
Pages
19049-57
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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