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
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.