Organic phosphates modulate anion self-exchange across the human erythrocyte membrane

Bursaux, E; Hilly, Mauricette; Bluze, André; Poyart, Claire

doi:10.1016/0005-2736(84)90427-9

Cited by 28 publications

(14 citation statements)

References 32 publications

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“…The transmembrane self-exchange flux of sulfate was studied in normal and spherocytic cells as previously described (22). Efflux measurements were performed at 37 Њ C, at four different values of pH (6.4, 6.7, 6.9, and 7.1) in Hepes-buffered medium containing 50 mM K 2 35 SO 4 .…”

Section: Methodsmentioning

confidence: 99%

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Jenkins¹,

Abou‐Alfa²,

Dhermy³

et al. 1996

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Jenkins¹,

Abou‐Alfa²,

Dhermy³

et al. 1996

J. Clin. Invest.

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“…These conformations are sensitive to protonation-deprotonation reactions and differ substantially-the Stokes' radius of cdb3 increases from 55 to 66 A between pH 6.5 and 10 (8). Finally, several recent observations suggest structural communication between distant regions of band 3, such as between the N terminus and the intramembrane anion channel or the cytoplasmic cysteine cluster located on the C-terminal segment of cdb3 (10)(11)(12)(13). The multiple static and dynamic conformations ofband 3 are likely to have functional importance.…”

mentioning

confidence: 99%

Segmental dynamics of the cytoplasmic domain oferythrocyte band 3 determined by time-resolved fluorescence anisotropy:sensitivity to pH and ligand binding.

Thevenin

Periasamy

Shohet

1994

Proc. Natl. Acad. Sci. U.S.A.

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Interactions between the erythrocyte membrane and its skeleton are mediated primarily by binding of cytoskeletal components to a conformationally sensitive structure, the cytoplasmic domain of band 3 (cdb3). To e-mine the nanosecond segmental motions of cdb3, band 3 was labeled selectively by fluorescein maleimide at Cys-201 near the proposed hinge in cdb3 about which pH-dependent conformational changes occur. Time-resolved anisotropy of labeled cdb3 in Isolated form and in stripped erythrocyte membranes was measured by parallel-acquisition frequency-domain microfluorimetry. Samples had a single-component fluorescein lifetime of -4 ns. Multifrequency phase and modulation data (5-200 MHz) fitted well to a segmental motion model containing two correlation times (1c and 7) and two limiting anisotropies (r1. and r2.). Measurements in protease-cleaved and denatured samples indicated that Tjc (100-150 ps) corresponded to rapid rotation of bound fluorescein and rac (2-5 ns) corresponded to segmental motion of cdb3. Both motions were hindered as quantified by nonzero rl and ra.. The strong pH dependence of segmental motion correlated with that of cdb3 conformation measured by intrinsic tryptophan fluorescence. Significant changes in cdb3 segmental motion occurred upon interactions with the small ligands 2,3-bisphosphoglycerate and calcium and several glycolytic enzymes known to bind to the N terminus of band 3. These time-resolved fluorescence measurements of the nanosecond segmental dynamics of a labeled membrane protein provide evidence for the sensitivity of cdb3 conformation to ligand binding and suggest long-range structural communication through cdb3.The best known function ofband 3, the major integral protein of erythrocyte membranes, is the electroneutral exchange of anions across the plasma membrane (1). However, band 3 has several additional functions, many of which are mediated by interaction of its cytoplasmic domain with various soluble factors and enzymes (2). For example, the association between the cytoplasmic domain of band 3 (cdb3) and ankyrin provides the primary attachment site for the spectrin-based membrane skeleton (3, 4). Other components that interact with cdb3 include band 4.1, band 4.2, hemoglobin, and several glycolytic enzymes (2-4). To accommodate the binding of multiple substrates, cdb3 has an extended asymmetric structure (2). Whereas the binding sites for hemoglobin and glycolytic enzymes are restricted to the extreme N terminus of cdb3 (2), ankyrin and band 4.1 appear to interact also with distal regions of cdb3 (5-7). Several experiments suggest the existence of a flexible "hinge" near the middle of cdb3 (2, 8); the hinge may permit flexion of cdb3 to facilitate ligand binding to noncontiguous band 3 sequences.There is increasing evidence that band 3 has a dynamic structure. Band 3 appears to exist in situ as an equilibrium mixture of dimers and tetramers held together by noncovalent interactions (1, 9). In addition, cdb3 is thought to be poised in a facile equilibrium among th...

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“…The effect of A23187 treatment also appears to be selective for hexose transport, since under identical incubation conditions neither sulfate efflux nor GSH content was affected in the present studies. Bursaux et al [11] similarly found no effect of several different methods of ATP depletion on erythrocyte sulfate efflux at an extracellular pH of 7.2 or greater.…”

Section: Discussionmentioning

confidence: 96%

Effects of ATP depletion on the mechanism of hexose transport in intact human erythrocytes

May

1988

FEBS Letters

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Depletion of ATP is known to inhibit glucose transport in human erythrocytes, but the kinetic mechanism of this effect is controversial. Selective ATP depletion of human erythrocytes by 10/~g/ml A23187 in the presence of extracellular calcium inhibited 3-O-methylglucose influx noncompetitively and efflux competitively. ATP depletion also decreased the ability of either equilibrated 3-O-methylglucose or extracellular maltose to inhibit cytochalasin B binding in intact cells, whereas neither total high-affinity cytochalasin B binding nor its Ka was affected. Under the one-site model of hexose transport these data indicate that ATP depletion decreases both the affinity of the inward-facing glucose carrier for substrate and its ability to reorient outwardly in intact cells.Sugar transport; ATP depletion; Cytochalasin B; One-site carrier model; (Human erythrocyte)

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Organic phosphates modulate anion self-exchange across the human erythrocyte membrane

Cited by 28 publications

References 32 publications

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis.

Segmental dynamics of the cytoplasmic domain oferythrocyte band 3 determined by time-resolved fluorescence anisotropy:sensitivity to pH and ligand binding.

Effects of ATP depletion on the mechanism of hexose transport in intact human erythrocytes

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