Evidence of peroxidative damage to the erythrocyte membrane in iron deficiency.

The mechanism responsible for reduced red blood cell (RBC) survival in iron- deficient infants or animals is unknown. To investigate the possible role of membrane peroxidation in iron-deficiency anemia, we studied RBC membrane lipids and proteins of rats fed iron-deficient (2 ppm Fe) and control (50 ppm Fe) diets between 21 and 41 days of age. Thin-layer chromatog- raphy of lipids showed that iron-deficient rats' RBC contained a novel phospholipid (1.9% of the total phospholipid) which moved between phosphatidylserine and phosphatidylethanolamine. Detailed studies showed that this PL is a Schiff's base adduct of phosphatidylserine, phosphatidyl- ethanolamine, and malonyldialdehyde, an end product of lipid peroxidation. Polyacrylamide gel electrophoresis of RBC proteins of iron-deficient rats also showed presence of high molecular protein complexes similar to that formed in in vitro malonyldialdehyde-treated RBC. To examine the role of such membrane cross-linking on in vivo RBC survival, we have studied survival of in vitro malonyldialdehyde-treated RBC in rabbits. 5tCr-T #{189} of 5 ,.aM malonyldialdehyde-treated RBC, which contained about the same amount of phospholipid/malonyldialdehyde adduct, was reduced to 6 days as compared to 11 days of sham-treated RBC. The in vitro study suggests that peroxidative damage results in significant reduction in RBC T #{189} and may be analogous to decreased RBC survival in iron-deficient infants and animals. Am J Clin Nutr l983;37:26-30.