Inhibition by the protein ceruloplasmin of lipid peroxidation stimulated by an Fe3+—ADP—adriamycin complex

FEBS Letters

Nakano, Hiroko¹  Ogita, Kouji¹  Nakano, Minoru¹  Gutteridge, John M.C.² 

[1] College of Medical Care and Technology, Gunma University, Maebashi, Gunma, Japan;National Institute for Biological Standards and Control, Holly Hill, Hampstead, London NW3 6RB, England

关键词: Ceruloplasmin;    Superoxide dismutase;    Adriamycin;    Ferroxidase activity;    Lipid peroxidation;    Oxygen radical;   

DOI  :  10.1016/0014-5793(84)80086-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown