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Papers In Press, published online ahead of print May 1, 2009
J. Lipid Res., doi:10.1194/jlr.M800468-JLR200

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Journal of Lipid Research, Vol. 50, 860-869, May 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Characterization of mouse lysophosphatidic acid acyltransferase 3: an enzyme with dual functions in the testis^1,

Koichi Yuki, Hideo Shindou², Daisuke Hishikawa and Takao Shimizu

Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan

¹ Nucleotide sequence data are available in the DDBJ/EMBL/GenBank databases under the accession numbers AB377215 (mouse).

The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of one table and three figures.

This work was supported in part by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (T.S.). T.S. and H.S. were supported by the Center for NanoBio Integration at the University of Tokyo. H.S. was supported by Health and Labour Sciences Research Grants (Research on Allergic Disease and Immunology) supported by the Ministry of Health, Labour, and Welfare of Japan, Mitsubishi Pharma Research Foundation, and Ono Medical Research Foundation.

Published, JLR Papers in Press, December 29, 2008.

² To whom correspondence should be addressed. e-mail: hshindou-tky{at}umin.ac.jp

Glycerophospholipids are structural and functional components of cellular membranes as well as precursors of various lipid mediators. Using acyl-CoAs as donors, glycerophospholipids are formed by the de novo pathway (Kennedy pathway) and modified in the remodeling pathway (Lands' cycle). Various acyltransferases, including two lysophosphatidic acid acyltransferases (LPAATs), have been discovered from a 1-acylglycerol-3-phosphate O-acyltransferase (AGPAT) family. Proteins of this family contain putative acyltransferase motifs, but their biochemical properties and physiological roles are not completely understood. Here, we demonstrated that mouse LPAAT3, previously known as mouse AGPAT3, possesses strong LPAAT activity and modest lysophosphatidylinositol acyltransferase activity with a clear preference for arachidonoyl-CoA as a donor. This enzyme is highly expressed in the testis, where CDP-diacylglycerol synthase 1 preferring 1-stearoyl-2-arachidonoyl-phosphatidic acid as a substrate is also highly expressed. Since 1-stearoyl-2-arachidonoyl species are the main components of phosphatidylinositol, mouse LPAAT3 may function in both the de novo and remodeling pathways and contribute to effective biogenesis of 1-stearoyl-2-arachidonoyl-phosphatidylinositol in the testis. Additionally, the expression of this enzyme in the testis increases significantly in an age-dependent manner, and β-estradiol may be an important regulator of this enzyme's induction. Our findings identify this acyltransferase as an alternative important enzyme to produce phosphatidylinositol in the testis.

Supplementary key words 1-acylglycerol-3-phosphate O-acyltransferase • phosphatidic acid • phosphatidylinositol • β-estradiol

Abbreviations: AGPAT, 1-acylglycerol-3-phosphate O-acyltransferase; CDP-diacylglycerol, cytidine diphosphodiacylglycerol; CHO, Chinese hamster ovary; DDBJ, DNA Data Bank of Japan; ER, endoplasmic reticulum; LPAAT, lysophosphatidic acid acyltransferase; LPIAT, lysophosphatidylinositol acyltransferase; LPLAT, lysophospholipid acyltransferases; NCBI, National Center for Biotechnology Information; PA, phosphatidic acid; PI, phosphatidylinositol

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