Human erythrocytes are protected against chromate-induced peroxidation.

In previous studies performed in this laboratory it was realized that in a broad concentration range (0.5-8 mM) dichromate does not induced red blood cell (RBC) peroxidation. To investigate the reasons behind RBC protection against chromate-induced peroxidation, the effects of 8 mM dichromate on white ghost and RBC peroxidation, RBC antioxidant system and hemoglobin status, as well as RBC osmotic fragility and morphology, were studied in more detail. It was observed that the peroxidation level induced by dichromate on RBCs is practically negligible when compared with the peroxidation induced in white ghosts. Furthermore, the osmotic fragility of RBCs exposed to dichromate is not altered, but the cells undergo echinocytic transformation, probably due to chromate-induced structural RBC membrane modifications. The activities of catalase, gluthatione peroxidase, and superoxide dismutase of RBCs exposed to dichromate were similar to those observed in controls, but the gluthatione reductase and GSH levels were significantly reduced (P<0. 05). Concomitantly, GSSG and methemoglobin levels increased and NADH-methemoglobin reductase activity decreased. These results indicate that chromate does not induce RBC peroxidation, but does promote echinocytic shape transformation, oxidation of hemoglobin and GSH, and inhibition of gluthatione reductase and methemoglobin reductase. The enzymatic antioxidant defense system and hemoglobin oxidation are probably involved in the mechanism of RBC proctection against chromate-induced peroxidation, as is discussed.
(Copyright 1999 Academic Press.)