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Originally published In Press as doi:10.1074/jbc.M010459200 on April 24, 2001

J. Biol. Chem., Vol. 276, Issue 27, 24473-24481, July 6, 2001
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Apolipoprotein A-I Promotes the Formation of Phosphatidylcholine Core Aldehydes That Are Hydrolyzed by Paraoxonase (PON-1) during High Density Lipoprotein Oxidation with a Peroxynitrite Donor*

Zakaria AhmedDagger §, Amir Ravandi, Graham F. MaguireDagger , Andrew Emili||, Dragomir Draganov**, Bert N. La Du**, Arnis Kuksis, and Philip W. ConnellyDagger §||Dagger Dagger §§

From the Dagger  J. Alick Little Lipid Research Laboratory, St. Michael's Hospital, the § Department of Laboratory Medicine and Pathobiology,  Banting and Best Department of Medical Research, the Departments of || Biochemistry and Dagger Dagger  Medicine, University of Toronto, Toronto, Ontario M5B 1A6, Canada, and the ** Department of Pharmacology, University of Michigan, Ann Arbor, Michigan 48109-0572

High density lipoprotein (HDL) is rich in polyunsaturated phospholipids that are sensitive to oxidation. However, the effect of apolipoprotein A-I and paraoxonase-1 (PON-1) on phosphatidylcholine oxidation products has not been identified. We subjected native HDL, trypsinized HDL, and HDL lipid suspensions to oxidation by the peroxynitrite donor, 3-morpholinosydnonimine. HDL had a basal level of phosphatidylcholine mono- and di-hydroperoxides that increased to a greater extent in HDL, compared with either trypsinized HDL or HDL lipid alone. Phosphatidylcholine core aldehydes, which were present in small amounts, increased 10-fold during oxidation of native HDL, compared with trypsinized HDL (p = 0.004), and 4-fold compared with HDL lipid suspensions (p = 0.0021). In addition, the content of lysophosphatidylcholine increased 300% during oxidation of native HDL, but only 80 and 25%, respectively, during oxidation of trypsinized HDL and HDL lipid suspensions. Phosphatidylcholine isoprostanes accumulated in comparable amounts during the oxidation of all three preparations. Incubation of apolipoprotein A-I with 1-palmitoyl-2-linoleoyl glycerophosphocholine proteoliposomes in the presence of 3-morpholinosydnonimine or apoAI with phosphatidylcholine hydroperoxides resulted in a significant increase in phosphatidylcholine core aldehydes with no formation of lysophosphatidylcholine. We propose that apolipoprotein A-I catalyzes a one-electron oxidation of alkoxyl radicals. Purified PON-1 hydrolyzed phosphatidylcholine core aldehydes to lysophosphatidylcholine. We conclude that, upon HDL oxidation with peroxynitrite, apolipoprotein AI increases the formation of phosphatidylcholine core aldehydes that are subsequently hydrolyzed by PON1.

* This work was supported by Heart and Stroke Foundation of Ontario Grant T4027 (to P. W. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§§ To whom correspondence should be addressed: J. Alick Little Lipid Research Laboratory, St. Michael's Hospital, University of Toronto, 38 Shuter St., Rm. 1004 WA, Toronto, Ontario M5B 1A6, Canada. E-mail: p.connelly@utoronto.ca.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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