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<scp>d</scp>‐Galactose induced early aging in human erythrocytes: Role of band 3 protein

Alessia Remigante, Sara Spinelli, Vincenzo Trichilo, Saverio Loddo, Antonio Sarikas, Michael Pusch, Silvia Dossena, Angela Marino, Rossana Morabito

2021Journal of Cellular Physiology37 citationsDOIOpen Access PDF

Abstract

Abstract 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.

Topics & Concepts

Band 3GlycationChemistryOxidative stressGlutathioneHemoglobinMethemoglobinBiochemistryOxidative phosphorylationLipid peroxidationGalactoseAntioxidantIn vitroRed blood cellMembrane proteinMembraneEnzymeReceptorErythrocyte Function and PathophysiologyPancreatic function and diabetesBiomedical Research and Pathophysiology