J. Lipid Res. Neurobiology of Lipids (ISSN1683-5506)
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A more recent version of this article appeared on May 1, 2007 Originally published In Press as doi:10.1194/jlr.M600437-JLR200 on February 28, 2007

Papers In Press, published online ahead of print February 26, 2007
J. Lipid Res., doi:10.1194/jlr.M600437-JLR200
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Submitted on October 3, 2006
Revised on January 17, 2007
Accepted on February 26, 2007

Unsaturated fatty acidsphosphorylate and destabilize ABCA1 through a protein kinase Cdelta pathway

Yutong Wang and John F. Oram

Medicine, Box 356426, University of Washington, Seattle, WA 98195-6426

Corresponding Author: joram{at}u.washington.edu

Abnormal high density lipoprotein (HDL) metabolism among patients with diabetes and insulin resistance may contribute to their increased risk of atherosclerosis. ATP-binding cassette transporter ABCA1 mediates the transport of cholesterol and phospholipids from cells to HDL apolipoproteins and thus modulates HDL levels and atherogenesis. Unsaturated fatty acids, which are elevated in diabetes, impair the ABCA1 pathway in cultured cells by destabilizing ABCA1 protein. We previously reported that unsaturated fatty acids destabilize ABCA1 in murine macrophages and ABCA1-transfected baby hamster kidney (BHK) cells by increasing its serine phosphorylation through a phospholipase D (PLD) pathway. Here we examined the cellular pathway downstream of PLD that mediates the ABCA1 destabilizing effects of unsaturated fatty acids. The protein kinase C delta (PKC)-specific inhibitor rottlerin and PKC siRNA completely abolished the ability of unsaturated fatty acids to inhibit lipid transport activity, to reduce protein levels, and to increase serine phosphorylation of ABCA1, implicating a role for PKC in the ABCA1 destabilizing effects of fatty acids. These data indicate that unsaturated fatty acids destabilize ABCA1 by activating a PKC pathway that phosphorylates ABCA1 serines.


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