Defective anion transport activity of the abnormal band 3 in hereditary ovalocytic red blood cells

Nature ◽  
1992 ◽  
Vol 355 (6363) ◽  
pp. 836-838 ◽  
Author(s):  
Ann E. Schofield ◽  
David M. Reardon ◽  
Michael J. A. Tanner
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Band 3 ◽  
Anion Transport ◽  
Transport Activity ◽  
Abnormal Band ◽  
Anion Transport Activity

scholarly journals Altered band 3 structure and function in glycophorin A- and B-deficient (MkMk) red blood cells

Blood ◽  
1994 ◽  
Vol 84 (3) ◽  
pp. 916-922 ◽  
Author(s):  
LJ Bruce ◽  
JD Groves ◽  
Y Okubo ◽  
B Thilaganathan ◽  
MJ Tanner
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Band 3 ◽  
Anion Transport ◽  
Glycophorin A ◽  
Sulfate Transport ◽  
Transport Activity ◽  
Anion Transporter ◽  
Glycan Chain ◽  
Anion Transport Activity

The anion transport activity of the human erythrocyte anion transporter (band 3; AE1) has been examined in both normal and glycophorin A (GPA)- deficient (MkMk) human red blood cells (RBCs). The sulfate transport activity of MkMk cells (from two ethnically diverse sources) was approximately 60% that of normal erythrocytes under the transport assay conditions used. However, MkMk and normal RBCs contained similar amounts of band 3. The reduction in sulfate transport activity was shown to be caused by an increase in the apparent Km for sulfate in MkMk RBCs, suggesting the band 3 in the MkMk RBCs has a lowered binding affinity for sulfate anions. The size of the N-glycan chain on band 3 of the MkMk cells was larger than that on band 3 from normal RBCs. In contrast, the size of the N-glycan chain on the glucose transporter (GLUT1) from MkMk cells was smaller than that on GLUT1 from normal cells. The possible role of GPA in the biosynthesis and anion transport activity of band 3 in normal RBCs is discussed.

scholarly journals Altered band 3 structure and function in glycophorin A- and B-deficient (MkMk) red blood cells

Blood ◽  
1994 ◽  
Vol 84 (3) ◽  
pp. 916-922 ◽  
Author(s):  
LJ Bruce ◽  
JD Groves ◽  
Y Okubo ◽  
B Thilaganathan ◽  
MJ Tanner
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Band 3 ◽  
Anion Transport ◽  
Glycophorin A ◽  
Sulfate Transport ◽  
Transport Activity ◽  
Anion Transporter ◽  
Glycan Chain ◽  
Anion Transport Activity

Abstract The anion transport activity of the human erythrocyte anion transporter (band 3; AE1) has been examined in both normal and glycophorin A (GPA)- deficient (MkMk) human red blood cells (RBCs). The sulfate transport activity of MkMk cells (from two ethnically diverse sources) was approximately 60% that of normal erythrocytes under the transport assay conditions used. However, MkMk and normal RBCs contained similar amounts of band 3. The reduction in sulfate transport activity was shown to be caused by an increase in the apparent Km for sulfate in MkMk RBCs, suggesting the band 3 in the MkMk RBCs has a lowered binding affinity for sulfate anions. The size of the N-glycan chain on band 3 of the MkMk cells was larger than that on band 3 from normal RBCs. In contrast, the size of the N-glycan chain on the glucose transporter (GLUT1) from MkMk cells was smaller than that on GLUT1 from normal cells. The possible role of GPA in the biosynthesis and anion transport activity of band 3 in normal RBCs is discussed.

K562 cell anion exchange differs markedly from that of mature red blood cells

1983 ◽  
Vol 244 (1) ◽  
pp. C68-C74 ◽  
Author(s):  
F. Y. Law ◽  
R. Steinfeld ◽  
P. A. Knauf
Keyword(s):  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Chloride Transport ◽  
K562 Cells ◽  
Band 3 ◽  
Anion Transport ◽  
Leukemic Cells ◽  
Anion Transport System

Human K562 leukemic cells exhibit several erythroid properties, including synthesis and expression of the major red blood cell sialoglycoprotein, glycophorin. This has led us to ask if these cells express a functional anion transport system analogous to that which is associated with the other major erythrocyte glycoprotein, band 3. The chloride-36 exchange flux in K562 cells is less than 0.6% of that which would be expected in mature erythrocytes under similar conditions. Unlike red blood cells, K562 cells do not exhibit a high chloride-sulfate selectivity, and various agents that inhibit red blood cell chloride exchange are all much less effective in K562 cells. On the basis of these flux measurements, K562 cells probably contain less than 600 fully functional red blood cell-like band 3 molecules per cell, in contrast to about a million molecules in the mature red blood cell. The possible-existence of greatly altered band 3 molecules with a reduced turnover rate and/or a reduced affinity for chloride and for various inhibitors is unlikely but cannot be completely excluded. Anion transport was also measured in K562 cells that had been induced to increase hemoglobin synthesis by various chemical agents. Even under these conditions, chloride fluxes indicated no substantial increase in the number of functional anion transport sites or their chloride transport rate.

scholarly journals Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868→Leu in the membrane domain of band 3

1993 ◽  
Vol 293 (2) ◽  
pp. 317-320 ◽  
Author(s):  
L J Bruce ◽  
M M Kay ◽  
C Lawrence ◽  
M J Tanner
Keyword(s):  
Cell Shape ◽  
Band 3 ◽  
Anion Transport ◽  
Red Cell ◽  
Transport Activity ◽  
Binding Properties ◽  
Red Cell Shape ◽  
Disulphonic Acid ◽  
Anion Transport Activity ◽  
Cell Variant

1. We have studied band 3 HT, a human red-cell band 3 variant with increased M(r), which is associated with abnormal red-cell shape (acanthocytosis) and increased anion-transport activity. 2. We have shown that the increased M(r) does not result from the presence of the band 3 Memphis mutation, and that the variant band 3 is covalently labelled by 4,4′-di-isothiocyanato-1,2-diphenylethane-2,2′-disulphonic acid (H2DIDS) less readily than normal. 3. cDNA cloning studies show that band 3 HT results from the mutation Pro-868-->Leu, and the possible significance of the mutation in the altered anion-transport activity and cytoskeleton binding properties of band 3 HT is discussed.

Further Studies on Zn2+-Mediated Domain–Domain Communication in Human Erythrocyte Band 3

1998 ◽  
Vol 18 (5) ◽  
pp. 265-277
Author(s):  
Hong Xu ◽  
Xujia Zhang ◽  
Fu Yu Yang
Keyword(s):  
Conformational Change ◽  
Human Erythrocyte ◽  
Cytoplasmic Domain ◽  
Band 3 ◽  
Anion Transport ◽  
Intrinsic Fluorescence ◽  
Transport Activity ◽  
Membrane Domain ◽  
Nmr Study ◽  
Anion Transport Activity

Human erythrocyte band 3 is purified and reconstituted into vesicles, forming right-side-out proteoliposomes. Zn2+ entrapped inside the proteoliposomes inhibits the anion transport activity of band 3, and removal of the cytoplasmic domain of band 3 is able to diminish Zn2+ inhibition. Thus, the inhibition of activity of band 3 results from the Zn2+ induced conformational change of the cytoplasmic domain, which in turn is transmitted to the membrane domain. The results of intrinsic fluorescence and its quenching by HB and the 35Cl NMR study indicate that the cytoplasmic domain is essential for the conformational change induced by Zn2+.SH-blocking reagents, CH3I and GSSG, are used to modify the cytoplasmic domain, where they specifically bind to Cys201 and Cys317. It is observed that the Zn2+ induced inhibition of anion transport activity is blocked. This demonstrates that Cys201 and Cys317 are required in Zn2+-mediated domain–domain communication.

Resveratrol treatment induces redox stress in red blood cells: a possible role of caspase 3 in metabolism and anion transport

2010 ◽  
Vol 391 (9) ◽  
Author(s):  
Antonio Galtieri ◽  
Ester Tellone ◽  
Silvana Ficarra ◽  
Annamaria Russo ◽  
Ersilia Bellocco ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Caspase 3 ◽  
Conformational Transition ◽  
Reducing Power ◽  
Band 3 ◽  
Anion Transport ◽  
Heme Iron ◽  
Strong Impact ◽  
Oxygen Binding

AbstractResveratrol, an important phytoalexine found in many plants, has been shown to be significantly effective in the treatment of several pathological conditions such as cancer, coronary heart disease and osteoarthritis. This study focuses on the effects of this drug on human red blood cells. In particular, we have examined the influence of resveratrol on Band 3, the anion exchanger protein, and hemoglobin as a function of the oxygenation-deoxygenation cycle. Moreover, special attention has been given to the metabolic changes imposed by caspase 3 activation. Resveratrol has proved to lower superoxide production, thereby decreasing heme-iron oxidation and saving the reducing power required for met-hemoglobin reduction. Oxygen binding experiments showed that resveratrol interacts with hemoglobin, shifting the T→R conformational transition towards the higher-affinity R state. This might contribute to altering the metabolic balance of the cell through an intensification of the pentose phosphate pathway. Moreover, at high oxygenation levels of the erythrocytic hemoglobin, resveratrol induces a significant activation of caspase 3, the action of which on Band 3 has a strong impact on cellular metabolism and anion transport.

Characterization of anion transport system in trout red blood cell

1984 ◽  
Vol 246 (3) ◽  
pp. C330-C338 ◽  
Author(s):  
L. Romano ◽  
H. Passow
Keyword(s):  
Blood Cell ◽  
Red Blood Cells ◽  
Red Blood Cell ◽  
Blood Cells ◽  
Sodium Dodecyl ◽  
Band 3 ◽  
Anion Transport ◽  
Disulfonic Acid ◽  
Band 3 Protein ◽  
Proton Uptake

Anion transport in the trout red blood cell is mediated by a membrane protein that selectively binds dihydro-4,4'-dithiocyanostilbene-2,2'-disulfonic acid (3H2DIDS) and that forms on sodium dodecyl sulfate (SDS)-polyacrylamide gel electropherograms a band with the same diffuse structure at the same location as the band 3 protein of the mammalian red blood cells. There exists a linear relationship between binding of H2DIDS to this protein and the inhibition of anion equilibrium exchange. At maximal inhibition about 8 X 10(6) molecules/cell are bound to the protein. The kinetics of anion transport in the trout red blood cell differ from those of mammalian red blood cells. In addition to a H2DIDS-sensitive component of sulfate transport there exists a considerable H2DIDS-insensitive component with a relative magnitude that decreases with increasing temperature. At 23 degrees C, it amounts to about 25%. The temperature dependence of the H2DIDS-sensitive component is about 15 kcal/mol instead of 32 as in human red blood cells. Cl- transport increases with increasing pH. Above pH 7.4, the rate of transport becomes too fast to be measurable with either inhibitor stop or filtration technique. SO2-4 transport is nearly pH independent over the pH range 6.5 to 7.8 and the net entry of SO2-4 in exchange against intracellular Cl-, as followed in the absence of CO2, is accompanied by little if any proton uptake. Net proton uptake becomes measurable only at temperatures above 40 degrees C. Possibly at lower and more physiological temperatures, the band 3 protein in the red blood cell of the trout accomplishes part of the SO2-4 movements without cotransporting protons.

Exhaustive-exercise-induced oxidative stress alteration of erythrocyte oxygen release capacity

2018 ◽  
Vol 96 (9) ◽  
pp. 953-962 ◽  
Author(s):  
Yanlian Xiong ◽  
Yanlei Xiong ◽  
Yueming Wang ◽  
Yajin Zhao ◽  
Yaojin Li ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Band 3 ◽  
Anion Transport ◽  
Kinetic Properties ◽  
Oxygen Release ◽  
Transport Activity ◽  
Running Exercise ◽  
Release Capacity ◽  
Anion Transport Activity ◽  
2,3 Dpg

The aim of the present study was to explore the effect of exhaustive running exercise in the oxygen release capacity of rat erythrocytes. Rats were divided into sedentary control, moderate running exercise, and exhaustive running exercise groups. The thermodynamic and kinetic properties of the erythrocyte oxygen release process of the different groups were tested. We also determined the degree of band-3 oxidation and phosphorylation, anion transport activity, and carbonic anhydrase isoform II activity. Biochemical studies suggested that exhaustive running significantly increased oxidative injury parameters in thiobarbituric acid reactive substances and methaemoglobin levels. Furthermore, exhaustive running significantly decreased anion transport activity and carbonic anhydrase isoform II activity. Thermodynamic analysis indicated that erythrocytes oxygen release ability also significantly increased due to elevated 2,3-DPG level after exhaustive running. Kinetic analysis indicated that exhaustive running resulted in significantly decreased T50 value. We presented evidence that exhaustive running remarkably impacted thermodynamic and kinetic properties of RBC oxygen release. In addition, changes in 2,3-DPG levels and band-3 oxidation and phosphorylation could be the driving force for exhaustive-running-induced alterations in erythrocyte oxygen release thermodynamic and kinetic properties.

Sign in / Sign up

Export Citation Format

Share Document