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J Biol Chem, Vol. 274, Issue 29, 20271-20280, July 16, 1999
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From the Levuglandin (LG) E2, a
cytotoxic seco prostanoic acid co-generated with prostaglandins by
nonenzymatic rearrangements of the cyclooxygenase-derived endoperoxide,
prostaglandin H2, avidly binds to proteins. That
LGE2-protein adducts can also be generated nonenzymatically
is demonstrated by their production during free radical-induced
oxidation of low density lipoprotein (LDL). Like oxidized LDL,
LGE2-LDL, but not native LDL, undergoes receptor-mediated uptake and impaired processing by macrophage cells. Since
radical-induced lipid oxidation produces isomers of
prostaglandins, isoprostanes (isoPs), via endoperoxide
intermediates, we postulated previously that a similar family of
LG isomers, isoLGs, is cogenerated with isoPs. Now
iso[4]LGE2-protein epitopes produced by radical-induced oxidation of arachidonic acid in the presence of protein were detected
with an enzyme-linked immunosorbent assay.
Iso[4]LGE2-protein epitopes are also generated during
free radical-induced oxidation of LDL. All of the LGE2
isomers generated upon oxidation of LDL are efficiently sequestered by
covalent adduction with LDL-based amino groups. The potent
electrophilic reactivity of iso-LGs can be anticipated to have
biological consequences beyond their obvious potential as markers for
specific arachidonate-derived protein modifications that may be of
value for the quantitative assessment of oxidative injury.
Department of Chemistry, Case Western
Reserve University, Cleveland, Ohio 44106-7078, the ¶ Departments
of Pharmacology and Medicine, Vanderbilt University, Nashville,
Tennessee 37232-6602, and the Department of Cell Biology, The
Lerner Research Institute, The Cleveland Clinic Foundation,
Cleveland, Ohio 44195
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