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J. Biol. Chem., Vol. 281, Issue 29, 20140-20147, July 21, 2006

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Cloning and Characterization of Mouse Lung-type Acyl-CoA:Lysophosphatidylcholine Acyltransferase 1 (LPCAT1)

EXPRESSION IN ALVEOLAR TYPE II CELLS AND POSSIBLE INVOLVEMENT IN SURFACTANT PRODUCTION^*

Hiroki Nakanishi, Hideo Shindou¹, Daisuke Hishikawa, Takeshi Harayama, Rie Ogasawara^¶, Akira Suwabe^¶, Ryo Taguchi^||, and Takao Shimizu²

From the Departments of Metabolome and Biochemistry and Molecular Biology, Faculty of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, the ^¶Department of Laboratory Medicine, School of Medicine, Iwate Medical University, 19-1 Uchimaru, Morioka, Iwate 020-8505, and ^||CREST of the Japan Science and Technology Agency, Kawaguchi, Saitama, 332-8613, Japan

Phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), is an important constituent of biological membranes. It is also the major component of serum lipoproteins and pulmonary surfactant. In the remodeling pathway of PC biosynthesis, 1-acyl-sn-glycero-3-phosphocholine (LPC) is converted to PC by acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT, EC 2.3.1.23 [EC] ). Whereas LPCAT activity has been detected in several tissues, the structure and detailed biochemical information on the enzyme have not yet been reported. Here, we present the cloning and characterization of a cDNA for mouse lung-type LPCAT (LPCAT1). The cDNA encodes an enzyme of 60 kDa, with three putative transmembrane domains. When expressed in Chinese hamster ovary cells, mouse LPCAT1 exhibited Ca²⁺-independent activity with a pH optimum between 7.4 and 10. LPCAT1 demonstrated a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl- or 1-palmitoyl-LPC as acyl donors and acceptors, respectively. Furthermore, the enzyme was predominantly expressed in the lung, in particular in alveolar type II cells. Thus, the enzyme might synthesize phosphatidylcholine in pulmonary surfactant and play a pivotal role in respiratory physiology.

Received for publication, January 10, 2006 , and in revised form, May 10, 2006.

^* This work was supported in part by Grants-in-aid from the Ministry of Education, Science, Culture, Sports and Technology of Japan (to T. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. A and B.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB244717 [GenBank] (mouse), AB244719 [GenBank] (human), and AB244983 [GenBank] (rat).

¹ Supported by the Center for NanoBio Integration at The University of Tokyo.

² Supported by the Center for NanoBio Integration at The University of Tokyo. To whom correspondence should be addressed. Tel.: 81-3-5802-2925; Fax: 81-3-3813-8732; E-mail: tshimizu{at}m.u-tokyo.ac.jp.

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