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Journal of Lipid Research, Vol 32, 63-70, Copyright © 1991 by Lipid Research, Inc.
MK Cathcart, AK McNally and GM Chisolm
We have been studying the mechanisms involved in the oxidative modification
of low density lipoprotein (LDL) that lead to its transformation to a
cytotoxic complex. Here we examine the direct effect-of soybean
lipoxygenase (SLO), a 15-lipoxygenase, on normal human LDL. SLO oxidized
LDL and rendered it cytotoxic; agents known to interfere with lipoxygenase
activity inhibited this reaction. Enhancement of both the SLO-mediated LDL
oxidation and the conversion of LDL to a cytotoxin was observed when either
superoxide dismutase or copper (II) (3,5,-diisopropylsalicylic acid)2, both
of which dismute superoxide anion, were included during the incubation of
SLO with LDL. In contrast, catalase inhibited this reaction in the presence
or absence of agents that dismute superoxide anion. Thus, purified
lipoxygenase can mediate LDL modification and superoxide anion inhibits
this reaction, Furthermore, H2O2 is essential for SLO-mediated LDL
oxidation and conversion of LDL to a cytotoxin.
ARTICLES
Lipoxygenase-mediated transformation of human low density lipoprotein to an oxidized and cytotoxic complex
Department of Immunology, Cleveland Clinic Foundation, OH 44195.
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