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  • Title: Distinguishing levuglandins produced through the cyclooxygenase and isoprostane pathways.
    Author: Salomon RG.
    Journal: Chem Phys Lipids; 2005 Mar; 134(1):1-20. PubMed ID: 15752459.
    Abstract:
    The cyclooxygenase (COX) pathway generates enantiomerically pure levuglandin (LG) E(2) by a rearrangement of the prostaglandin (PG) endoperoxide PGH(2). The isoprostane pathway generates racemic LGE(2) together with stereoisomers, designated collectively as isoLGE(2), through free radical-induced lipid oxidation. Within seconds, both LGs and isoLGs are rapidly sequestered by protein adduction. In theory, the diastereomeric purity of LGE(2)-protein adduct-derived lysyl lactams can reveal the relative contributions of the COX and isoprostane pathways to LGE(2) stereoisomer production in vivo. Notably, however, the detection of LGE(2)-protein adducts does not provide a basis for inferring their formation through the isoprostane pathway in vivo unless the COX pathway can be rigorously excluded. In contrast, LGE(2)structural isomers, designated collectively as iso[n]LGE(2)s, are produced exclusively through the isoprostane pathway. Immunoassays that selectively recognize iso[n]LGE(2)-protein adducts are the only tools available to unambiguously detect and quantify the production of isolevuglandins in vivo through free radical-induced oxidation of arachidonates.
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