J. Lipid Res.
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Journal of Lipid Research, Vol. 42, 1082-1088, July 2001
Copyright © 2001 by Lipid Research, Inc.

Original Article

Oxidation of LDL by rabbit and human 15-lipoxygenase: prevalence of nonenzymatic reactions

Dagmar Heydecka, Joanne M. Upstona, Helena Viitab, Seppo Ylä-Herttualab, and Roland Stockera
a Biochemistry Group, The Heart Research Institute, 145 Missenden Road, Camperdown, Sydney, 2050 N.S.W., Australia
b A. I. Virtanen Institute and Department of Medicine, University of Kuopio, Kuopio, Finland

Correspondence to: Roland Stocker, To whom correspondence should be addressed., r.stocker{at}hri.org.au (E-mail)

15-Lipoxygenase (15-LO)-induced oxidation of lipids in human LDL may be pro-atherogenic. However, the extent to which 15-LO promotes enzymatic oxidation of esterified (i.e., major) lipids in LDL may depend on various factors. Here, we show that overall, LDL lipid oxidation was favored with high activity of human 15-LO, that phospholipids were the preferred esterified substrate, and that low temperature maintained a higher proportion of enzymatic product. However, under all conditions, 15-LO induced {alpha}-tocopherol consumption and the accumulation of nonenzymatic products that predominated with increasing time of incubation and inactivation of the enzyme. Lysates prepared from cells overexpressing human 15-LO oxidized linoleic acid readily and in an almost exclusive enzymatic manner. In sharp contrast, such lysates failed to oxidize LDL lipids unless linoleic acid was added, in which case nonenzymatic oxidation of LDL lipids occurred.

We conclude that although purified 15-LO can oxidize isolated LDL lipids in vitro, such oxygenation always includes nonenzymatic reactions that likely play a major role in the more extensive oxidation of LDL by cell-derived 15-LO. — Heydeck, D., J. M. Upston, H. Viita, S. Ylä-Herttuala, and R. Stocker. Oxidation of LDL by rabbit and human 15-lipoxygenase: prevalence of nonenzymatic reactions. J. Lipid Res. 2001. 42: 1082;–1088.

Supplementary key words: mammalian 15-lipoxygenase, lipid oxidation, vitamin E, lipoprotein


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