The efficiency of transport through Band 3 protein, mediating HCO3–/Cl– exchange across erythrocytes membrane, is reduced by oxidative stress. The aim of the present study was to verify whether Band 3 protein transport efficiency is compromised by treatment with Cadmium (Cd2+), an extremely toxic heavy metal known to interfere with antioxidant enzymes, energy metabolism, gene expression and cell membranes. To this end, the rate constant for SO4= uptake through Band 3 protein (accounting for velocity of anion exchange) was measured along with membrane –SH groups, Malonyldialdehyde (MDA) and Band 3 protein expression levels in Cd2+-treated human erythrocytes (300 μM, 1 mM). Our results show that Cd2+ reduced the rate constant for SO4= uptake, with a significant increase in MDA levels at both concentrations and with a reduction in –SH groups observed after 1 mM Cd2+ treatment, whereas Band 3 protein expression levels were unchanged in both conditions. In conclusion: i) Cd2+ reduces Band 3 protein transport efficiency via different mechanisms depending on metal concentration and with unchanged expression levels; ii) the assessment of Band 3 protein anion exchange capability is a good tool to assay the impact of heavy metals on cell homeostasis and, possibly, useful for diagnosis and monitoring of development of Cd2+ toxicity-related pathologies.
Morabito R, R.A. (2018). Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes. JOURNAL OF BIOLOGICAL RESEARCH, 91(7203), 1-7.
Data di pubblicazione: | 2018 |
Titolo: | Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes |
Autori: | |
Citazione: | Morabito R, R.A. (2018). Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes. JOURNAL OF BIOLOGICAL RESEARCH, 91(7203), 1-7. |
Rivista: | |
Digital Object Identifier (DOI): | http://dx.doi.org/10.4081/jbr.2018.7203 |
Abstract: | The efficiency of transport through Band 3 protein, mediating HCO3–/Cl– exchange across erythrocytes membrane, is reduced by oxidative stress. The aim of the present study was to verify whether Band 3 protein transport efficiency is compromised by treatment with Cadmium (Cd2+), an extremely toxic heavy metal known to interfere with antioxidant enzymes, energy metabolism, gene expression and cell membranes. To this end, the rate constant for SO4= uptake through Band 3 protein (accounting for velocity of anion exchange) was measured along with membrane –SH groups, Malonyldialdehyde (MDA) and Band 3 protein expression levels in Cd2+-treated human erythrocytes (300 μM, 1 mM). Our results show that Cd2+ reduced the rate constant for SO4= uptake, with a significant increase in MDA levels at both concentrations and with a reduction in –SH groups observed after 1 mM Cd2+ treatment, whereas Band 3 protein expression levels were unchanged in both conditions. In conclusion: i) Cd2+ reduces Band 3 protein transport efficiency via different mechanisms depending on metal concentration and with unchanged expression levels; ii) the assessment of Band 3 protein anion exchange capability is a good tool to assay the impact of heavy metals on cell homeostasis and, possibly, useful for diagnosis and monitoring of development of Cd2+ toxicity-related pathologies. |
Settore Scientifico Disciplinare: | Settore MED/49 - Scienze Tecniche Dietetiche Applicate Settore BIO/09 - Fisiologia |
Appare nelle tipologie: | 1.01 Articolo in rivista |
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