D-Galactose induced early aging in human erythrocytes: Role of band 3 protein

Aging, a time-dependent multifaceted process, affects both cell structure and function and involves oxidative stress as well as glycation. The present investigation focuses on the role of the band 3 protein (B3p), an anion exchanger essential to red cells homeostasis, in a D-galactose (D-Gal)-induced aging model. Anion exchange capability, measured by the rate constant of SO42- uptake through B3p, levels of lipid peroxidation, oxidation of membrane sulfhydryl groups, B3p expression, methemoglobin, glycated hemoglobin (Hb), and the reduced glutathione/oxidized glutathione ratio were determined after exposure of human erythrocytes to 25, 35, 50, and 100 mmol/L D-Gal for 24 h. Our results show that: (i) in vitro application of D-Gal is useful to model early aging in human erythrocytes; (ii) assessment of B3p ion transport function is a sensitive tool to monitor aging development; (iii) D-Gal leads to Hb glycation and produces substantial changes on the endogenous antioxidant system; (iv) the impact of aging on B3p function proceeds through steps, first involving Hb glycation and then oxidative events at the membrane level. These findings offer a useful tool to understand the mechanisms of aging in human erythrocytes and propose B3p as a possible target for new therapeutic strategies to counteract age-related disturbances.

Automated summary

The study found that utilizing D-Gal can mimic early aging in human erythrocytes, assessing B3p ion transport function is a sensitive tool to monitor aging development, and D-Gal leads to Hb glycation and substantial changes in the endogenous antioxidant system. Aging impacts B3p function through stages involving Hb glycation first and then oxidative events at the membrane level.