J. Lipid Res.
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A more recent version of this article appeared on November 1, 2005

Papers In Press, published online ahead of print August 16, 2005
J. Lipid Res., doi:10.1194/jlr.M500168-JLR200
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Submitted on May 2, 2005
Revised on July 29, 2005
Accepted on August 3, 2005

A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters

Chi-Liang Eric Yen, Charles H. Brown IV., Mara Monetti, and Robert V. Farese . Jr

Gladstone Insitute of Cardiovascular Disease, Gladstone Institutes, UCSF, San Francisco, CA 94158

Corresponding Author: eyen{at}gladstone.ucsf.edu

Acyl CoA-dependent O-acyltransferases catalyze reactions in which fatty acyl CoAs are joined to acyl acceptors containing free hydroxyl groups to produce neutral lipids. In this report, we characterize a human multifunctional O-acyltransferase (designated MFAT) that belongs to the DGAT2/MGAT gene family and is highly expressed in the skin. Membranes of insect cells and homogenates of mammalian cells overexpressing MFAT exhibited significantly increased acyl CoA:monoacylglycerol acyltransferase (MGAT), acyl CoA:fatty acyl alcohol acyltransferase (wax synthase), and acyl CoA:retinol acyltransferase (ARAT) activities, which catalyze the synthesis of diacylglycerols, wax monoesters, and retinyl esters, respectively. Furthermore, when provided with the appropriate substrates, intact mammalian cells overexpressing MFAT accumulated more waxes and retinyl esters than did control cells. We conclude that MFAT is a multifunctional acyltransferase that likely plays an important role in lipid metabolism in human skin.


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