title: On the ability of high density lipoproteins to remove phospholipid peroxidation products from erythrocyte membranes.
abstract: To study the transfer of oxidized phospholipids from cell membranes to high-density lipoproteins (HDL), human Cu2+-oxidized erythrocyte membranes were incubated with HDL3 subfraction for 17 h at 37 degrees C followed by isolation of the supernatant, precipitation from it of HDL3, and determination of lipid peroxide products (LPP) in them. The incubation increased the content of lipid hydroperoxides in HDL3 significantly (by 32 and 40% calculated per ml of sample or mg of protein) and of malondialdehyde (by 27 and 34%, respectively) compared to control (incubation of HDL3 alone). The content of conjugated dienes did not change significantly. Fluorescence analyses of isolated HDL3 particles showed that the content of fluorescent products (lambdaex = 365 nm, lambdaem = 430 nm) in them was 2.5 times higher than in control, and the number of binding sites for the 1-anilinonaphthalene-8-sulfonic acid probe decreased by 22%. This also confirms accumulation of LPP in the lipoprotein subfraction. It seems likely that an increase in LPP (at least hydroperoxides) in HDL3 after their incubation with oxidized membranes occurs via transport of phospholipids containing LPP from erythrocyte membranes to lipoproteins. The data on the ability of HDL3 to accept LPP from erythrocyte membranes in vitro suggest that HDL3 may have a protective action on cell membranes undergoing oxidation in vivo as well.
authors.affiliation: Institute of Experimental Medicine, Russian Academy of Medical Sciences, St. Petersburg, 197376, Russia. bio@bio.iem.ras.spb.ru
authors.forename: A N
authors.initials: AN
authors.lastname: Klimov
authors.forename: K A
authors.initials: KA
authors.lastname: Kozhevnikova
authors.forename: A A
authors.initials: AA
authors.lastname: Kuzmin
authors.forename: A S
authors.initials: AS
authors.lastname: Kuznetsov
authors.forename: E V
authors.initials: EV
authors.lastname: Belova
mesh_terms: D000817:Anilino Naphthalenesulfonates / Q000494:pharmacology; D001665:Binding Sites; D002412:Cations; D002462:Cell Membrane / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000494:pharmacology; D006801:Humans; D008054:Lipid Peroxides / Q000378:metabolism; D008075:Lipoproteins, HDL / Q000378:metabolism*; D008956:Models, Chemical; D010743:Phospholipids / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013997:Time Factors
chemical_list: D000817:Anilino Naphthalenesulfonates; D002412:Cations; D005456:Fluorescent Dyes; D008054:Lipid Peroxides; D008075:Lipoproteins, HDL; D010743:Phospholipids; C027132:1-anilino-8-naphthalenesulfonate; D003300:Copper