Impact of acute inflammation on Band 3 protein anion exchange capability in human erythrocytes

2020 ◽  
pp. 1-7 ◽  
Author(s):  
Rossana Morabito ◽  
Alessia Remigante ◽  
Marika Cordaro ◽  
Vincenzo Trichilo ◽  
Saverio Loddo ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Acute Inflammation ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein

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

Antioxidants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 689
Author(s):  
Alessia Remigante ◽  
Rossana Morabito ◽  
Sara Spinelli ◽  
Vincenzo Trichilo ◽  
Saverio Loddo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Anion Exchange ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein ◽  
Expression Levels ◽  
Vitro Effect ◽  
The Impact

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.

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

2018 ◽  
Vol 91 (1) ◽  
Author(s):  
Rossana Morabito ◽  
Alessia Remigante ◽  
Benedetta Arcuri ◽  
Angela Marino ◽  
Marco Giammanco ◽  
...  
Keyword(s):  
Protein Expression ◽  
Anion Exchange ◽  
Rate Constant ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein ◽  
Toxic Heavy Metal ◽  
Expression Levels ◽  
Sh Groups ◽  
The Impact

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.

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

Molecules ◽  
2019 ◽  
Vol 24 (15) ◽  
pp. 2741 ◽  
Author(s):  
Rossana Morabito ◽  
Alessia Remigante ◽  
Angela Marino
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Protein Expression ◽  
Beneficial Effect ◽  
Anion Exchange ◽  
Rate Constant ◽  
Cell Shape ◽  
Band 3 ◽  
Band 3 Protein ◽  
Expression Levels

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.

scholarly journals Proteolysis of ankyrin and of band 3 protein in chemically induced cell fusion. Ca2+ is not mandatory for fusion

1984 ◽  
Vol 218 (2) ◽  
pp. 295-305 ◽  
Author(s):  
R D A Lang ◽  
C Wickenden ◽  
J Wynne ◽  
J A Lucy
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Band 3 ◽  
Human Erythrocytes ◽  
General Mechanism ◽  
Band 3 Protein ◽  
Fusion Reactions ◽  
Chlorpromazine Hydrochloride

Human erythrocytes were fused by incubation with 0.5-2 mM-chlorpromazine hydrochloride at pH 6.8-7.6. Fusogenic preparations of chlorpromazine were cloudy suspensions of microdroplets, and below pH 6.8 chlorpromazine gave clear solutions that were inactive. Unlike control cells, the lateral mobility of the intramembranous particles of the PF-fracture face of chlorpromazine-treated cells was relatively unrestricted, since the particles were partly clustered at 37 degrees C and they exhibited extensive cold-induced clustering. Ca2+ stimulated fusion, but fusion was only very weakly inhibited by EGTA (10 mM) and by N-ethylmaleimide (50 mM); pretreatment of the cells with Tos-Lys-CH2Cl (7-amino-1-chloro-3-L-tosylamidoheptan-2-one) (7.5 mM) markedly inhibited fusion. Changes in the membrane proteins of erythrocytes fused by chlorpromazine, before and after treatment with chymotrypsin to remove band 3 protein, were investigated. The several observations made indicate that the Ca2+-insensitive component of fusion is associated with degradation of ankyrin (band 2.1 protein) to band 2.3-2.6 proteins and to smaller polypeptides by a serine proteinase that is inhibited by Tos-Lys-CH2Cl, and that the component of fusion inhibited by EGTA and N-ethylmaleimide is associated with degradation of band 3 protein to band 4.5 protein by a Ca2+-activated cysteine proteinase. Proteolysis of ankyrin appeared to be sufficient to permit the chlorpromazine-induced fusion of human erythrocytes, but fusion occurred more rapidly when band 3 protein was also degraded in the presence of Ca2+. Since other cells have structures comparable with the spectrin-actin skeleton of the erythrocyte membrane, the observations reported may be relevant to the initiation of naturally occurring fusion reactions in biomembranes. It is also suggested that, should polypeptides with fusogenic properties be produced from integral and skeletal membrane proteins by endogenous proteolysis, their formation would provide a general mechanism for the fusion of lipid bilayers in biomembrane fusion reactions.

scholarly journals Catecholamine-induced transport systems in trout erythrocyte. Na+/H+ countertransport or NaCl cotransport?

1986 ◽  
Vol 87 (4) ◽  
pp. 551-566 ◽  
Author(s):  
F Borgese ◽  
F Garcia-Romeu ◽  
R Motais
Keyword(s):  
Anion Exchange ◽  
Band 3 ◽  
Cell Swelling ◽  
Transport Systems ◽  
Band 3 Protein ◽  
Free Medium ◽  
Exchange System ◽  
Nucleated Red Blood Cells ◽  
Nacl Cotransport ◽  
Na Uptake

It has previously been shown (Baroin, A., F. Garcia-Romeu, T. Lamarre, and R. Motais. 1984a, b. Journal of Physiology. 350:137, 356:21; Mahé, Y., F. Garcia-Romeu, and R. Motais. 1985. European Journal of Pharmacology. 116:199) that the addition of catecholamines to an isotonic suspension of nucleated red blood cells of the rainbow trout first stimulates a cAMP-dependent, amiloride-sensitive Na+/H+ exchange. This stimulation seems to be transient. It is followed by a more permanent activation of a coupled entry of Na+ and Cl-, which is inhibited by amiloride but also by inhibitors of band 3 protein (DIDS, furosemide, niflumic acid). The coupled entry of Na+ and Cl- could therefore result from the parallel and simultaneous exchange of Na+out for H+in (via the cAMP-dependent Na+/H+ antiporter) and Cl- out for HCO3- in (via the anion exchange system located in band 3 protein). However, in view of the following arguments, it had been proposed that NaCl uptake does not proceed by the double-exchanger system but via an NaCl cotransport: (a) Na+ entry requires Cl- as anion (in NO3- medium, the Na uptake is strongly inhibited, whereas NO3- is an extremely effective substitute for Cl- in the anion exchange system); (b) Na uptake is not significantly affected by the presence of HCO3- in the suspension medium despite the fact that in red cells, Cl-/HCO3- exchange occurs more readily than the exchanges of Cl- for basic equivalents in a theoretically CO2-free medium (the so-called Cl-/OH- exchanges). The purpose of the present paper was a reassessment of the two models by using monensin, an ionophore allowing Na+/H+ exchange. From this study, it appears that NaCl entry results from the simultaneous functioning of the Na+/H+ antiporter and the anion exchange system. The apparent Cl dependence is explained by the fact that, in these erythrocytes, NO3- clearly inhibits the turnover rate of the Na+/H+ antiporter. As Na+/H+ exchange is the driving component in the salt uptake process, this inhibition explains the Cl requirement for Na entry. The lack of stimulation of cell swelling by bicarbonate is explained by the fact that the rate of anion exchange in a CO2-free medium (Cl-/OH- exchange) is roughly equivalent to that of Na+/H+ exchange and thus in practice is not limiting to the net influx of NaCl through the two exchangers.(ABSTRACT TRUNCATED AT 400 WORDS)

Anion exchange through band 3 protein in canine leishmaniasis at different stages of disease

2017 ◽  
Vol 469 (5-6) ◽  
pp. 713-724 ◽  
Author(s):  
Rossana Morabito ◽  
Alessia Remigante ◽  
Mauro Cavallaro ◽  
Alessandro Taormina ◽  
Giuseppina La Spada ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Band 3 ◽  
Canine Leishmaniasis ◽  
Band 3 Protein

Anion exchange protein (band 3) in human erythrocytes characterized by different abnormalities

1993 ◽  
Vol 220 (2) ◽  
pp. 211-217 ◽  
Author(s):  
A. Giuliani ◽  
S. Marini ◽  
L. Ferroni ◽  
S.G. Condo' ◽  
M.T. Ramacci ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Protein Band ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Anion Exchange Protein ◽  
Exchange Protein

scholarly journals The Lyn-Catalyzed Tyr Phosphorylation of the Transmembrane Band-3 Protein of Human Erythrocytes

1996 ◽  
Vol 240 (2) ◽  
pp. 394-399 ◽  
Author(s):  
Anna Maria Brunati ◽  
Luciana Bordin ◽  
Giulio Clari ◽  
Vittorio Moret
Keyword(s):  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein

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

Antioxidants ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 25 ◽  
Author(s):  
Alessia Remigante ◽  
Rossana Morabito ◽  
Angela Marino
Keyword(s):  
Anion Exchange ◽  
Natural Antioxidants ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
Ion Distribution ◽  
Beneficial Effects ◽  
Cross Links

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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