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  • Title: Preferential hydrolysis of oxidized phosphatidylcholine in cholesterol-containing phosphatidylcholine liposome by phospholipase A2.
    Author: Kambayashi Y, Yamamoto Y, Nakano M.
    Journal: Biochem Biophys Res Commun; 1998 Apr 28; 245(3):705-8. PubMed ID: 9588178.
    Abstract:
    Hydrolysis of 1-palmitoyl-2-linoleoyl-phosphatidylcholine (PLPC) hydroperoxide (PLPC-OOH) in PLPC liposomal membrane by Crotalus adamanteus venom phospholipase A2 (PLA2) was studied by measuring the decay of PLPC and PLPC-OOH and the formation of linoleate and linoleate hydroperoxide. We demonstrate that PLA2 has a preference to hydrolyze PLPC-OOH over PLPC when more than 25 mole % of cholesterol is incorporated into the PLPC liposomal membrane. Similar results were obtained for PLPC hydroxide (PLPC-OH). These results suggest that cholesterol displaces the hydrophilic hydroperoxyl and hydroxyl moieties of PLPC-O(O)H to the surface interface of the liposomal membrane where they are more accessible to PLA2 hydrolysis.
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