ADRIAMYCIN-INDUCED LIPID-PEROXIDATION OF ERYTHROCYTE-MEMBRANES IN THEPRESENCE OF FERRITIN AND THE INHIBITORY EFFECT OF CERULOPLASMIN

Citation
T. Miura et al., ADRIAMYCIN-INDUCED LIPID-PEROXIDATION OF ERYTHROCYTE-MEMBRANES IN THEPRESENCE OF FERRITIN AND THE INHIBITORY EFFECT OF CERULOPLASMIN, Biological & pharmaceutical bulletin, 16(7), 1993, pp. 664-667
Citations number
37
Categorie Soggetti
Pharmacology & Pharmacy
ISSN journal
09186158
Volume
16
Issue
7
Year of publication
1993
Pages
664 - 667
Database
ISI
SICI code
0918-6158(1993)16:7<664:ALOEIT>2.0.ZU;2-7
Abstract
When erythrocyte membranes were incubated with adriamycin (ADM) in the presence of ferritin, lipid peroxidation occurred with release of iro n from the ferritin. In the presence of apoferritin, ADM did not cause lipid peroxidation. Deferoxamine inhibited the ADM-induced lipid pero xidation in the presence of ferritin. These results indicate that lipi d peroxidation depends upon the release of iron from ferritin. Even wh en the iron content in ferritin was very low, ADM could induce lipid p eroxidation. Superoxide dismutase, catalase and hydroxyl radical scave ngers did not substantially affect lipid peroxidation, indicating that the peroxidation reaction was independent of superoxide, H2O2 and hyd roxyl radicals. Ceruloplasmin, a ferroxidase, markedly inhibited lipid peroxidation but did not affect the release of iron from ferritin. AD M-Fe3+-binding erythrocyte membranes were readily formed during the in cubation of erythrocyte membranes with ADM in the presence of ferritin , and deferoxamine removed iron from the ADM-Fe3+-binding membranes, i ndicating that the iron moiety of the ADM-Fe3+ complex is exposed at t he membrane surface. These results may suggest that the peroxidation r eaction occurs in a site-specific manner.