Singlet oxygen in copper-catalyzed lipid peroxidation in erythrocyte membranes.
Lipid hydroperoxide was generated in human erythrocyte membranes by irradiation with near ultraviolet (UV) light in the presence of a photosensitizer, hematoporphyrin, but no production of 2-thiobarbituric acid-reactive materials (malonaldehyde and its precursors) was detected. Incubation of the irradiated membranes with CuSO4 led to increased levels of hydroperoxide and formation of malonaldehyde. Hydroperoxides were essential for initiating the Cu(II)-catalyzed peroxidation as no significant activity was observed with nonirradiated membranes and Cu(II) unless an organic peroxide, either t-butyl hydroperoxide or cumene hydroperoxide, was added. Catalytic activity was also found with Fe(II), but not with other metal ions tested. The peroxidation catalyzed with Cu(II) was partially inhibited by several singlet oxygen quenchers but was not affected by superoxide dismutase, catalase or OH radical scavengers. The possible involvement of singlet oxygen in the Cu(II)-catalyzed peroxidation reaction was further supported by a 3-fold enhancement of malonaldehyde production in D2O.
D003300:Copper / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005609:Free Radicals; D006801:Humans; D007501:Iron / Q000494:pharmacology; D008054:Lipid Peroxides / Q000378:metabolism*; D008315:Malondialdehyde / Q000378:metabolism; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D026082:Singlet Oxygen; D014466:Ultraviolet Rays
D005609:Free Radicals; D008054:Lipid Peroxides; D026082:Singlet Oxygen; D008315:Malondialdehyde; D003300:Copper; D007501:Iron; D010100:Oxygen