Anion transport in normal erythrocytes, sickle red cells, and ghosts in relation to hemoglobins and magnesium

Teti, Diana; Venza, Isabella; Crupi, Marilena; Busá, Maria; Loddo, Saverio; Romano, L.

doi:10.1016/s0003-9861(02)00310-7

Cited by 7 publications

(4 citation statements)

References 20 publications

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“…At specified intervals, 5 ml samples of suspension were removed and added to a test tube containing 5 µM of 4,4'-diisothiocyanato-stilbene-2,2'-disulfonate (DIDS) stopping medium and kept under ice. The presence of 5 µM DIDS, a chemical agent that binds irreversibly and specifically to the exterior part of the integral band 3 protein [25,39,40], inhibited SO 4 -transport both in normal and G6PDH-deficient cells. After the last sample withdrawal, the erythrocytes were washed three times in a sulphate-free medium at 0°C to remove the sulphate trapped outside.…”

Section: Erythrocyte Preparationmentioning

confidence: 99%

“…Depletion of cytoplasmic Mg 2+ or treatments with oxidant agents reduce the set point and induce KCC-and Gardos K + channel-dependent volume decrease [10-12, 15, 22-24]. Besides, it has been recently reported that free, ionized cytoplasmic Mg 2+ determines the activity of transport processes that control the ionic composition and cellular volume of many cell types, including RBCs, [25][26][27][28][29][30]. In fact, in some diseases in which K-Cl co-transport is pathologically elevated, the dietary Mg 2+ supplementation increases its content in erythrocytes and leads to inhibition of KCC [10,[31][32][33].…”

Section: Introductionmentioning

confidence: 99%

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Chemical and Pathological Oxidative Influences on Band 3 Protein Anion-exchanger

Teti¹,

Maria²,

Busá³

et al. 2005

Cell Physiol Biochem

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Background/aims: The erythrocyte is a cell exposed to a high level of oxygen pressure and to oxidative chemical agents. This stress involves SH-groups oxidation, cell shrinkage by activation of K-Cl cotransport (KCC) and elevation of the band 3 tyrosine phosphorylation level. The aim of our study was to test whether oxidative stress could influence band 3-mediated anion transport in human red blood cells. Methods: To evaluate this hypothesis, normal and pathological (glucose 6 phosphate dehydrogenase (G6PDH) defficient) erythrocytes were treated with known sulphydryl-blocking or thiol-oxidizing agents, such as N-ethylmaleimide (NEM), azodicarboxylic acid bis[dimethylamide] (diamide), orthovanadate, Mg 2+ and tested for sulphate (SO 4 -) uptake, K + efflux, G6PDH activity and glutathione (GSH) concentration. Results: In normal red blood cells, the rate constants of SO 4 -uptake decreased by about 28 % when cells were incubated with NEM, diamide and orthovanadate. In G6PDH-deficient red blood cells, in which oxidative stress occurs naturally, the rate constant of sulphate uptake was decreased by about 40% that of normal red cells. Addition of oxidizing and phosphatase inhibitor agents to pathological erythrocytes further decreased anion transport. In contrast, G6PDH activity was increased under oxidative stress in normal as well as in pathological cells and was lower in the presence of exogenous Mg 2+

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Section: Erythrocyte Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Chemical and Pathological Oxidative Influences on Band 3 Protein Anion-exchanger

Teti¹,

Maria²,

Busá³

et al. 2005

Cell Physiol Biochem

View full text Add to dashboard Cite

show abstract

“…Successively, at regular intervals, 5‐ml samples of each suspension were removed and added to a test tube containing 6 µl of 4,4′‐diisothiocyanostilbene‐2,2′‐disulfonic acid (DIDS) stopping medium and kept in ice. The presence of 4,4′‐diisothiocyanostilbene‐2,2′‐disulfonic acid, a compound that binds irreversibly and specifically to the exterior part of the integral membrane band 3 protein, inhibits SO 4 = transport in RBCs . After the last sample withdrawal, the erythrocytes were washed and centrifuged three times in a sulfate‐free medium at 0 °C to remove extracellular sulfate.…”

Section: Methodsmentioning

confidence: 99%

“…The presence of 4,4 0 -diisothiocyanostilbene-2, 2 0 -disulfonic acid, a compound that binds irreversibly and specifically to the exterior part of the integral membrane band 3 protein, inhibits SO 4 = transport in RBCs. 17,[25][26][27] After the last sample withdrawal, the erythrocytes were washed and centrifuged three times in a sulfate-free medium at 0 C to remove extracellular sulfate.…”

Section: Erythrocytes Preparationmentioning

confidence: 99%

Sulfate influx on band 3 protein of equine erythrocyte membrane (Equus caballus) using different experimental temperatures and buffer solutions

Casella

Piccione

Ielati

et al. 2012

Cell Biochemistry & Function

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The aim of this study was to assess the anion transport in equine erythrocytes through the measurement of the sulfate uptake operating from band 3 using different experimental temperatures and buffer solutions. Blood samples of six clinically healthy horses were collected via jugular vein puncture, and an emochrome-citometric examination was performed. The blood was divided into four aliquots and by centrifugation and aspiration the plasma and buffy coat were carefully discarded. The red blood cells were washed with an isosmotic medium and centrifuged. The obtained cell suspensions were incubated with two different experimental buffer solutions (buffer A: 115 mM Na2SO4, 10 mM NaCl, 20 mM ethylenediaminetetraacetic acid, 30 mM glucose; and buffer B: 115 mM Na2SO4, 10 mM NaCl, 20 mM ethylenediaminetetraacetic acid, 30 mM MgCl2) in a water bath for 1 h at 25 °C and 37 °C. Normal erythrocytes, suspended at 3% hematocrit, were used to measure the SO4= influx by absorption spectrophotometry at 425 nm wavelength. Unpaired Student's t-test showed a statistically significant decrease (P < 0.01) of rate constants in equine erythrocytes at 25 °C versus 37 °C using both experimental buffer solutions. Comparing the buffer A with buffer B unpaired Student's t-test showed statistically lower values (P < 0.0001) for A solution versus B solution both at 25 °C and at 37 °C. The greater inhibition of SO4 (=) influx measured in equine erythrocytes indicates the increased formation of the sulfydryl bonds in band 3 and the modulation of the sulfydryl groups, culminating in the conformational changes in band 3.

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K+-Cl- Cotransport in Vertebrate Red Cells

Gibson

Ellory

2003

Red Cell Membrane Transport in Health and Disease

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Anion transport in normal erythrocytes, sickle red cells, and ghosts in relation to hemoglobins and magnesium

Cited by 7 publications

References 20 publications

Chemical and Pathological Oxidative Influences on Band 3 Protein Anion-exchanger

Chemical and Pathological Oxidative Influences on Band 3 Protein Anion-exchanger

Sulfate influx on band 3 protein of equine erythrocyte membrane (Equus caballus) using different experimental temperatures and buffer solutions

K+-Cl- Cotransport in Vertebrate Red Cells

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