The efficiency of transport through Band 3 protein, mediatingHCO3–/Cl– exchange across erythrocytes membrane, is reduced byoxidative stress. The aim of the present study was to verify whetherBand 3 protein transport efficiency is compromised by treatmentwith Cadmium (Cd2+), an extremely toxic heavy metal known tointerfere with antioxidant enzymes, energy metabolism, geneexpression and cell membranes. To this end, the rate constant forSO4= uptake through Band 3 protein (accounting for velocity ofanion exchange) was measured along with membrane –SH groups,Malonyldialdehyde (MDA) and Band 3 protein expression levelsin Cd2+-treated human erythrocytes (300 μM, 1 mM). Our resultsshow that Cd2+ reduced the rate constant for SO4= uptake, with asignificant increase in MDA levels at both concentrations and witha reduction in –SH groups observed after 1 mM Cd2+ treatment,whereas Band 3 protein expression levels were unchanged in bothconditions. In conclusion: i) Cd2+ reduces Band 3 protein transportefficiency via different mechanisms depending on metalconcentration and with unchanged expression levels; ii) theassessment of Band 3 protein anion exchange capability is a goodtool to assay the impact of heavy metals on cell homeostasis and,possibly, useful for diagnosis and monitoring of development ofCd2+ toxicity-related pathologies.
|Numero di pagine||7|
|Rivista||JOURNAL OF BIOLOGICAL RESEARCH|
|Stato di pubblicazione||Published - 2018|
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