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Journal of Lipid Research, Vol 36, 1996-2004, Copyright © 1995 by Lipid Research, Inc.
M Ezaki, JL Witztum and D Steinberg
Oxidative modification of LDL plays an important role in early
atherogenesis but the mechanisms, nonenzymatic and/or enzymatic, by which
LDL is oxidized in vivo remain to be established. Several lines of evidence
suggest that cellular 15-lipoxygenase (arachidonate 15- oxidoreductase,
EC.1.13.11.13) (15-LO) may contribute to oxidative modification of LDL,
including recent studies demonstrating that murine fibroblasts
overexpressing 15-LO have an enhanced capacity to oxidize LDL in the
medium. The present studies were undertaken to better understand the
mechanisms by which cells expressing 15-LO bring about oxidative
modification of LDL. LDL incubated 1-2 h with the 15-LO- enriched cells
showed a much higher lipoperoxide (LOOH) content than did LDL incubated
with control cells. By far the largest absolute increase occurred in
cholesteryl ester hydroperoxide (CE-OOH), a much lesser increase in free
fatty acid hydroperoxides (FFA-OOH), and only a very small increase in
phospholipid hydroperoxides (PL-OOH). Addition of EDTA to the medium
abolished these increases in LDL lipid hydroperoxides. Enrichment of LDL
with probucol or vitamin E also prevented CE-OOH accumulation. Incubation
of LDL with linoleic acid hydroperoxide in the absence of cells also caused
a significant increase in CE-OOH and this was markedly inhibited by EDTA.
These findings provide further evidence for the potential of 15-LO to
participate in LDL oxidation by way of a mechanism involving introduction
of LOOH into the LDL particle followed by metal-catalyzed propagation.
ARTICLES
Lipoperoxides in LDL incubated with fibroblasts that overexpress 15- lipoxygenase
Department of Medicine, University of California, San Diego, La Jolla 92093-0682, USA.
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