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J. Biol. Chem., Vol. 280, Issue 15, 14755-14764, April 15, 2005

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Identification of Two Novel Human Acyl-CoA Wax Alcohol Acyltransferases

MEMBERS OF THE DIACYLGLYCEROL ACYLTRANSFERASE 2 (DGAT2) GENE SUPERFAMILY^*

Aaron R. Turkish, Annette L. Henneberry¶||, Debra Cromley**, Mahajabeen Padamsee¶, Peter Oelkers¶, Hisham Bazzi, Angela M. Christiano, Jeffrey T. Billheimer**, and Stephen L. Sturley¶¶¶

From the Departments of Pediatrics, Dermatology, Genetics, and Development and the ^¶Institute of Human Nutrition, Columbia University Medical Center, New York, New York 10032 and the ^**Center for Experimental Therapeutics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6160

The esterification of alcohols such as sterols, diacylglycerols, and monoacylglycerols with fatty acids represents the formation of both storage and cytoprotective molecules. Conversely, the overproduction of these molecules is associated with several disease pathologies, including atherosclerosis and obesity. The human acyl-CoA:diacylglycerol acyltransferase (DGAT) 2 gene superfamily comprises seven members, four of which have been previously implicated in the synthesis of di- or triacylglycerol. The remaining 3 members comprise an X-linked locus and have not been characterized. We describe here the expression of DGAT2 and the three X-linked genes in Saccharomyces cerevisiae strains virtually devoid of neutral lipids. All four gene products mediate the synthesis of triacylglycerol; however, two of the X-linked genes act as acyl-CoA wax alcohol acyltransferases (AWAT 1 and 2) that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation. The enzymes are expressed in many human tissues but predominate in skin. In situ hybridizations demonstrate a differentiation-specific expression pattern within the human sebaceous gland for the two AWAT genes, consistent with a significant role in the composition of sebum.

Received for publication, January 3, 2005

^* This work was supported by the American Heart Association (National and Heritage), the Ara Parseghian Medical Research Foundation, the Hirschl/Weil-Caulier Trust, and the National Institutes of Health (DK54320). 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 Material.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY947638.

Recipient of NHLBI, National Institutes of Health postdoctoral training fellowship in atherosclerosis (T32HL07343 to H. N. Ginsberg).

^|| Supported by the Heart and Stroke Foundation of Canada.

Recipient of NHLBI, National Institutes of Health postdoctoral training fellowship in atherosclerosis (T32HL07343 to H. N. Ginsberg). Current address: Dept. of Bioscience and Biotechnology, Drexel University, 3141 Chestnut St., Philadelphia, PA 19104.

^¶¶ To whom correspondence should be addressed: Institute of Human Nutrition, Columbia University Medical Center, 650 W168th St., New York, NY 10032. Tel.: 212-305-6304; Fax: 212-305-3079; E-mail: sls37{at}columbia.edu.

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