Band 3 Protein Function and Oxidative Stress in Erythrocytes from Systemic Sclerosis Patients with Interstitial Lung Disease

Morabito, Rossana

doi:10.11648/j.ejcbs.20170304.12

Cited by 10 publications

(16 citation statements)

References 19 publications

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“…In particular, the purpose was to evaluate anion exchange capability through B3p and to verify the potential mechanism through which d- Gal may affect this function. As reported elsewhere, B3p is essential to erythrocytes homeostasis, whose assessment is a valid tool to detect damage in case of oxidative stress-related diseases, such as Systemic Sclerodermia [ 56 ], Canine Leishmaniasis [ 45 ] and hyperglycemic conditions [ 33 ], or in other oxidative conditions modeled in vitro [ 27 , 34 ].…”

Section: Discussionmentioning

confidence: 99%

d-Galactose Decreases Anion Exchange Capability through Band 3 Protein in Human Erythrocytes

et al. 2020

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d-Galactose (d-Gal), when abnormally accumulated in the plasma, results in oxidative stress production, and may alter the homeostasis of erythrocytes, which are particularly exposed to oxidants driven by the blood stream. In the present investigation, the effect of d-Gal (0.1 and 10 mM, for 3 and 24 h incubation), known to induce oxidative stress, has been assayed on human erythrocytes by determining the rate constant of SO42− uptake through the anion exchanger Band 3 protein (B3p), essential to erythrocytes homeostasis. Moreover, lipid peroxidation, membrane sulfhydryl groups oxidation, glycated hemoglobin (% A1c), methemoglobin levels (% MetHb), and expression levels of B3p have been verified. Our results show that d-Gal reduces anion exchange capability of B3p, involving neither lipid peroxidation, nor oxidation of sulfhydryl membrane groups, nor MetHb formation, nor altered expression levels of B3p. d-Gal-induced %A1c, known to crosslink with B3p, could be responsible for rate of anion exchange alteration. The present findings confirm that erythrocytes are a suitable model to study the impact of high sugar concentrations on cell homeostasis; show the first in vitro effect of d-Gal on B3p, contributing to the understanding of mechanisms underlying an in vitro model of aging; demonstrate that the first impact of d-Gal on B3p is mediated by early Hb glycation, rather than by oxidative stress, which may be involved on a later stage, possibly adding more knowledge about the consequences of d-Gal accumulation.

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Section: Discussionmentioning

confidence: 99%

d-Galactose Decreases Anion Exchange Capability through Band 3 Protein in Human Erythrocytes

et al. 2020

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“…Hence, due to their sensitivity to oxidation, erythrocytes are a unique cell model [20] to investigate the impact of oxidative stress and to possibly assess the efficacy of antioxidant therapies. In this regard, Band 3 protein function alterations have been correlated to both in vitro oxidative conditions and oxidative stress-related diseases, i.e., systemic sclerodermia, diabetes and canine leishmaniasis [8,9,28].…”

Section: Discussionmentioning

confidence: 99%

“…Our previous investigations demonstrated a reduction in Band 3 protein anion exchange capability and protein expression levels after a short-term period of exposure (30 min) to 300 µM H 2 O 2 associated neither to lipid peroxidation, nor to membrane –SH groups oxidation (mostly belonging to Band 3 protein) or MetHb formation [4]. More recently, SO 4 = uptake measurement has been shown as a valid tool to detect oxidative damage in the case of oxidative stress-related diseases, such as systemic sclerodermia, diabetes, and canine leishmaniasis [7,8,9,10]. In addition, the role of antioxidants in preventing oxidative damage at Band 3 levels has also been investigated [11].…”

Section: Introductionmentioning

confidence: 99%

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

Morabito

Marino

2019

Molecules

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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.

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“…SO 4 = uptake determination has been recognized as a good tool for monitoring erythrocyte homeostasis [26]. In recent years, B3p anion exchange monitoring has been widely used to assay the effect of different experimental conditions, performed by applying oxidants and toxins in vitro [8,27], or in diseases associated with membrane protein degradation [28][29][30][31]. Consequently, this review, for the first time, collects the most recent knowledge about B3p function, taking into account that red blood cells represent a suitable cell model to evaluate cell response to oxidative conditions, due to their sensitivity to oxidation and simple metabolism, with specific regard to its anion exchange capability.…”

Section: Role In Erythrocyte Rigiditymentioning

confidence: 99%

Natural Antioxidants Beneficial Effects on Anion Exchange through Band 3 Protein in Human Erythrocytes

Morabito¹,

Marino²

2019

Antioxidants

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Band 3 protein (B3p) exchanging Cl− and HCO3− through erythrocyte membranes is responsible for acid balance, ion distribution and gas exchange, thus accounting for homeostasis of both erythrocytes and entire organisms. Moreover, since B3p cross links with the cytoskeleton and the proteins underlying the erythrocyte membrane, its function also impacts cell shape and deformability, essential to adaptation of erythrocyte size to capillaries for pulmonary circulation. As growing attention has been directed toward this protein in recent years, the present review was conceived to report the most recent knowledge regarding B3p, with specific regard to its anion exchange capability under in vitro oxidative conditions. Most importantly, the role of natural antioxidants, i.e., curcumin, melatonin and Mg2+, in preventing detrimental oxidant effects on B3p is considered.

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Band 3 Protein Function and Oxidative Stress in Erythrocytes from Systemic Sclerosis Patients with Interstitial Lung Disease

Cited by 10 publications

References 19 publications

d-Galactose Decreases Anion Exchange Capability through Band 3 Protein in Human Erythrocytes

d-Galactose Decreases Anion Exchange Capability through Band 3 Protein in Human Erythrocytes

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

Natural Antioxidants Beneficial Effects on Anion Exchange through Band 3 Protein in Human Erythrocytes

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