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

• Main Authors: Chi-Liang Eric Yen, Charles H. Brown, IV, Mara Monetti, Robert V. Farese, Jr.
• Format: Article
• Language: English
• Published: Elsevier 2005-11-01
• Series: Journal of Lipid Research
• Subjects: neutral lipids; diacylglycerol; fatty alcohol; esterification
• Online Access: http://www.sciencedirect.com/science/article/pii/S0022227520328765

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.