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Journal of Lipid Research, Vol. 46, 2388-2397, November 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology


,
* Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94158
Cardiovascular Research Institute, University of California, San Francisco, CA 94143
Department of Medicine, University of California, San Francisco, CA 94143
Published, JLR Papers in Press, August 16, 2005. DOI 10.1194/jlr.M500168-JLR200
1 To whom correspondence should be addressed. e-mail: 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 acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase (MGAT) gene family and is highly expressed in the skin. Membranes of insect cells and homogenates of mammalian cells overexpressing MFAT exhibited significantly increased 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 control cells.
We conclude that MFAT is a multifunctional acyltransferase that likely plays an important role in lipid metabolism in human skin.
Abbreviations: ARAT, acyl-coenzyme A:retinol acyltransferase; DGAT, acyl-coenzyme A:diacylglycerol acyltransferase; MFAT, multifunctional acyltransferase; MGAT, acyl-coenzyme A:monoacylglycerol acyltransferase; NCBI, National Center for Biotechnology Information
Supplementary key words neutral lipids diacylglycerol fatty alcohol esterification
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