Inhibition by the protein ceruloplasmin of lipid peroxidation stimulated by an Fe3+-ADP-adriamycin complex.
Self-reduction of an Fe3+-ADP-adriamycin complex under anaerobic conditions and reduction of ferricytochrome c by the complex under aerobic conditions were strongly inhibited by ceruloplasmin, but not by superoxide dismutase or albumin at the same protein concentration. Ceruloplasmin, a protein with ferroxidase activity, is able to catalyse oxidation of Fe2+ to the ferric state. The inhibitory activity of ceruloplasmin towards reactions stimulated by the complex suggests that Fe2+ is formed during the self-reduction process. As expected, the Fe3+-ADP-adriamycin complex stimulated lipid peroxidation in which the Fe2+ moiety was implicated. This stimulation was again effectively prevented by ceruloplasmin but not by superoxide dismutase.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D000818:Animals; D002570:Ceruloplasmin / Q000378:metabolism*; D004317:Doxorubicin / Q000494:pharmacology*; D005290:Ferric Compounds / Q000494:pharmacology*; D007501:Iron / Q000494:pharmacology*; D007700:Kinetics; D008054:Lipid Peroxides / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism*; D010084:Oxidation-Reduction; D010743:Phospholipids / Q000378:metabolism; D051381:Rats; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013482:Superoxide Dismutase / Q000378:metabolism
D005290:Ferric Compounds; D008054:Lipid Peroxides; D008563:Membrane Lipids; D010743:Phospholipids; C040440:doxorubicin-ferric-ADP complex; D012710:Serum Albumin, Bovine; D000244:Adenosine Diphosphate; D004317:Doxorubicin; D007501:Iron; D013482:Superoxide Dismutase; D002570:Ceruloplasmin