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Melatonin Protects Band 3 Protein in Human Erythrocytes against H2O2-Induced Oxidative Stress

1
Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, Viale F. Stagno D’Alcontres 31, 98166 Messina, Italy
2
Institute of Pharmacology and Toxicology, Paracelsus Medical University, 5020 Salzburg, Austria
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(15), 2741; https://doi.org/10.3390/molecules24152741
Received: 27 June 2019 / Revised: 18 July 2019 / Accepted: 27 July 2019 / Published: 28 July 2019
The beneficial effect of Melatonin (Mel), recognized as an anti-inflammatory and antioxidant compound, has been already proven to prevent oxidative stress-induced damage associated to lipid peroxidation. As previous studies modeled the impact of oxidative stress on Band 3 protein, an anion exchanger that is essential to erythrocytes homeostasis, by applying H2O2 at not hemolytic concentrations and not producing lipid peroxidation, the aim of the present work was to evaluate the possible antioxidant effect of pharmacological doses of Mel on Band 3 protein anion exchange capability. The experiments have been performed on human erythrocytes exposed to 300 μM H2O2-induced oxidative stress. To this end, oxidative damage has been verified by monitoring the rate constant for SO4= uptake through Band 3 protein. Expression levels of this protein Mel doses lower than 100 µM have also been excluded due to lipid peroxidation, Band 3 protein expression levels, and cell shape alterations, confirming a pro-oxidant action of Mel at certain doses. On the other hand, 100 µM Mel, not provoking lipid peroxidation, restored the rate constant for SO4= uptake, Band 3 protein expression levels, and H2O2-induced cell shape alterations. Such an effect was confirmed by abolishing the endogenous erythrocytes antioxidant system. Therefore, the present findings show the antioxidant power of Mel at pharmacological concentrations in an in vitro model of oxidative stress not associated to lipid peroxidation, thereby confirming Band 3 protein anion exchange capability measurement as a suitable model to prove the beneficial effect of Mel and support the use of this compound in oxidative stress-related diseases affecting Band 3 protein. View Full-Text
Keywords: Melatonin; Band 3 protein; SO4= uptake; oxidative damage; H2O2 Melatonin; Band 3 protein; SO4= uptake; oxidative damage; H2O2
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MDPI and ACS Style

Morabito, R.; Remigante, A.; Marino, A. Melatonin Protects Band 3 Protein in Human Erythrocytes against H2O2-Induced Oxidative Stress. Molecules 2019, 24, 2741. https://doi.org/10.3390/molecules24152741

AMA Style

Morabito R, Remigante A, Marino A. Melatonin Protects Band 3 Protein in Human Erythrocytes against H2O2-Induced Oxidative Stress. Molecules. 2019; 24(15):2741. https://doi.org/10.3390/molecules24152741

Chicago/Turabian Style

Morabito, Rossana; Remigante, Alessia; Marino, Angela. 2019. "Melatonin Protects Band 3 Protein in Human Erythrocytes against H2O2-Induced Oxidative Stress" Molecules 24, no. 15: 2741. https://doi.org/10.3390/molecules24152741

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