linoleic-acid-hydroperoxide and 1-palmitoyl-2-linoleoylphosphatidylcholine

linoleic-acid-hydroperoxide has been researched along with 1-palmitoyl-2-linoleoylphosphatidylcholine* in 1 studies

Other Studies

1 other study(ies) available for linoleic-acid-hydroperoxide and 1-palmitoyl-2-linoleoylphosphatidylcholine

Article	Year
Preferential hydrolysis of oxidized phosphatidylcholine in cholesterol-containing phosphatidylcholine liposome by phospholipase A2. Biochemical and biophysical research communications, 1998, Apr-28, Volume: 245, Issue:3 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. Topics: Cholesterol; Crotalid Venoms; Hydrolysis; Linoleic Acid; Linoleic Acids; Lipid Peroxides; Liposomes; Oxidation-Reduction; Phosphatidylcholines; Phospholipases A; Phospholipases A2	1998

Article

Year

Preferential hydrolysis of oxidized phosphatidylcholine in cholesterol-containing phosphatidylcholine liposome by phospholipase A2.

Biochemical and biophysical research communications, 1998, Apr-28, Volume: 245, Issue:3

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.

Topics: Cholesterol; Crotalid Venoms; Hydrolysis; Linoleic Acid; Linoleic Acids; Lipid Peroxides; Liposomes; Oxidation-Reduction; Phosphatidylcholines; Phospholipases A; Phospholipases A2

1998