Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes

The efficiency of 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 efficiency is compromised by treatment with Cadmium (Cd2+), an extremely toxic heavy metal known to interfere...

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Main Authors: Rossana Morabito, Alessia Remigante, Benedetta Arcuri, Angela Marino, Marco Giammanco, Giuseppina La Spada
Format: Article
Language:English
Published: PAGEPress Publications 2018-05-01
Series:Journal of Biological Research
Subjects:
Online Access:https://www.pagepressjournals.org/index.php/jbr/article/view/7203
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spelling doaj-985bab111f7f4d73b1192314afc77a902020-11-25T04:02:11ZengPAGEPress PublicationsJournal of Biological Research1826-88382284-02302018-05-0191110.4081/jbr.2018.72035716Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytesRossana Morabito0Alessia Remigante1Benedetta Arcuri2Angela Marino3Marco Giammanco4Giuseppina La Spada5Angela Marino6Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaDepartment of Biomedicine and Clinical Neurosciences, University of Palermo, PalermoDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaDepartment of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, MessinaThe efficiency of 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 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 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 devalopment of Cd2+ toxicity-related pathologies.https://www.pagepressjournals.org/index.php/jbr/article/view/7203CadmiumOxidative stressSO4= uptakeBand 3 proteinErythrocyte.
collection DOAJ
language English
format Article
sources DOAJ
author Rossana Morabito
Alessia Remigante
Benedetta Arcuri
Angela Marino
Marco Giammanco
Giuseppina La Spada
Angela Marino
spellingShingle Rossana Morabito
Alessia Remigante
Benedetta Arcuri
Angela Marino
Marco Giammanco
Giuseppina La Spada
Angela Marino
Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
Journal of Biological Research
Cadmium
Oxidative stress
SO4= uptake
Band 3 protein
Erythrocyte.
author_facet Rossana Morabito
Alessia Remigante
Benedetta Arcuri
Angela Marino
Marco Giammanco
Giuseppina La Spada
Angela Marino
author_sort Rossana Morabito
title Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
title_short Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
title_full Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
title_fullStr Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
title_full_unstemmed Effect of cadmium on anion exchange capability through Band 3 protein in human erythrocytes
title_sort effect of cadmium on anion exchange capability through band 3 protein in human erythrocytes
publisher PAGEPress Publications
series Journal of Biological Research
issn 1826-8838
2284-0230
publishDate 2018-05-01
description The efficiency of 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 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 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 devalopment of Cd2+ toxicity-related pathologies.
topic Cadmium
Oxidative stress
SO4= uptake
Band 3 protein
Erythrocyte.
url https://www.pagepressjournals.org/index.php/jbr/article/view/7203
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