Kinetic tests of models for sugar transport in human erythrocytes and a comparison of fresh and cold-stored cells

Weiser, Mark B.; Razin, Michal; Stein, Wilfred D.

doi:10.1016/0005-2736(83)90423-6

Cited by 45 publications

(24 citation statements)

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“…Brain, retina erythrocytes, and lens cells appear to prefer ␤-D-glucose or show no preference (17,26,52,59,65,67,68). ␤-D-Glucose is more potent than ␣-D-glucose in inhibiting vagally mediated secretion of gastric acid (77). These observations emphasize the tissue-specific physiology of anomer transport and utilization and further suggest that cells expressing GLUT1 or GLUT3 may prefer the ␤-anomer, whereas cells expressing GLUT2 or GLUT4 may prefer the ␣-anomer.…”

mentioning

confidence: 74%

“…Human red cell membrane GLUT1 content approaches 10% total protein by mass (36), resulting in extremely rapid sugar transport rates at all temperatures studied (8). Measurements of transport are, therefore, complicated by the necessity for rapid sampling procedures (8,49) but may be simplified by use of the equilibrium exchange condition (77). In equilibrium exchange, intracellular sugar concentration ϭ extracellular sugar concentration, no net transport occurs, and unidirectional sugar fluxes are measured by addition of radiotracer sugar either to the external or to the internal medium.…”

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confidence: 99%

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ATP-dependent sugar transport complexity in human erythrocytes

Leitch¹,

Carruthers²

2007

American Journal of Physiology-Cell Physiology

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. Exchange 3-O-methylglucose (3MG) import and export are monophasic in the absence of cytoplasmic ATP but are biphasic when ATP is present. Biphasic exchange is observed as the rapid filling of a large compartment (66% cell volume) followed by the slow filling of the remaining cytoplasmic space. Biphasic exchange at 20 mM 3MG eliminates the possibility that the rapid exchange phase represents ATP-dependent 3MG binding to the glucose transport protein (GLUT1; cellular [GLUT1] of Յ20 M). Immunofluorescence-activated cell sorting analysis shows that biphasic exchange does not result from heterogeneity in cell size or GLUT1 content. Nucleoside transporter-mediated uridine exchange proceeds as rapidly as 3MG exchange but is monoexponential regardless of cytoplasmic [ATP]. This eliminates cellular heterogeneity or an ATP-dependent, nonspecific intracellular diffusion barrier as causes of biphasic exchange. Red cell ghost 3MG and uridine equilibrium volumes (130 fl) are unaffected by ATP. GLUT1 intrinsic activity is unchanged during rapid and slow phases of 3MG exchange. Two models for biphasic sugar transport are presented in which 3MG must overcome a sugar-specific, physical (diffusional), or chemical (isomerization) barrier to equilibrate with cell water. Partial transport inhibition with the use of cytochalasin B or maltose depresses both rapid and slow phases of transport, thereby eliminating the physical barrier hypothesis. We propose that biphasic 3MG transport results from ATP-dependent, differential transport of 3MG anomers in which V max/apparent Km for ␤-3MG exchange transport is 19-fold greater than Vmax/apparent Km for ␣-3MG transport.carrier-mediated transport; transport kinetics; transport regulation A FAMILY OF INTEGRAL MEMBRANE proteins called glucose transporters (GLUTs) (40) mediates equilibrative sugar transport in mammalian cells. The glucose transport protein GLUT1 catalyzes sugar transport in cells of the reticuloendothelial system (7, 61) and presents an interesting experimental puzzle. The steady-state kinetics of GLUT1-mediated sugar transport in rabbit (70), rat (38, 62), and avian (7, 8) erythrocytes and in basal (insulin-starved) rat adipocytes (76) are consistent with classical models for carrier-mediated solute transport (5, 47). GLUT1-mediated sugar transport in human red cells, however, displays a kinetic complexity that has proven difficult to reconcile with models for carrier-mediated transport (4,21,32,49,56,79).Transport complexity is especially obvious in zero-trans exit and infinite-cis entry conditions (13). In the zero-trans exit condition, cells are loaded with various starting sugar concentrations and the initial rate of exit is measured (49, 56), or the complete time course of exit is analyzed by using an integrated Michaelis-Menten equation (4,16,42,56). Initial rate measurements (49, 56) routinely provide estimates of apparent K m [K m(app) ] for sugar exit that are two to three times lower than those obtained by analysis of the complete time course of sugar exit (4,16,42,...

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confidence: 74%

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confidence: 99%

ATP-dependent sugar transport complexity in human erythrocytes

Leitch¹,

Carruthers²

2007

American Journal of Physiology-Cell Physiology

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“…glucose and nucleoside transport (Jarvis, Hammond, Paterson & Clanachan, 1982;Weiser, Razin & Stein, 1983;Plagemann & Wohlhueter, 1984). In those cases, it has been suggested that accumulation of an intracellular inhibitor may be responsible for the effect (Stein, 1986).…”

Section: Temperature Dependence and Influence Of Monovalent Cationsmentioning

confidence: 99%

Effects of low ionic strength media on passive human red cell monovalent cation transport.

Bernhardt¹,

Hall²,

Ellory³

1991

The Journal of Physiology

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SUMMARY1. The effect of low ionic strength media on the residual, i.e. (ouabain + bumetanide+ Ca2+)-insensitive, K+ influx was characterized in human red blood cells.2. This K+ flux was enhanced significantly in isotonic solutions of low ionic strength using sucrose to maintain constant osmolarity. This effect was found for fresh red blood cells as well as for stored (bank) red blood cells. However, the absolute magnitude of K+ influx in solutions of low ionic strength was halved for stored red blood cells.3. Anion replacement of Cl-by CH3SO4-did not affect residual K+ fluxes, showing that Cl-dependent transport pathways (e.g. the KCl co-transporter) are not involved in the low ionic strength effect.4. The enhanced K+ influx in low ionic strength media was reversible when the cells were resuspended in a solution of physiological ionic strength.5. K+ influx measured in light and dense fractions of erythrocytes (separated by centrifugation and corresponding to samples enriched with either 'young' or 'mature' red cells) showed that the low ionic strength effect does not change markedly with cell age.6. Low ionic strength media elevated residual, i.e. (ouabain + bumetanide + Ca2+)-insensitive, influx of both K+ and Na+ by about the same amount. In both cases the flux was linear with concentration in the range investigated (025-10 mM). No significant increase in the uptake of the cations Ca2+ and lysine in low ionic strength solutions could be found.7. In CH3S04--containing solutions of physiological ionic strength the residual K+ influx was almost independent of cell volume, whereas this flux in CH3S04--containing solutions of low ionic strength declined as cell volume was increased.8. K+ flux measurements in solutions of different external pH, where NaCl was replaced by sodium gluconate or sodium glucuronate, showed that the reduced ionic strength is of more importance for the enhanced residual K+ influx than the changed transmembrane potential or the changed intracellular pH. However, a small pH dependence could be found, the K+ flux passing through a minimum around pHi 7.3.9.

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“…The earlier work [5] indicated a three-fold difference in rate between the anomers, but no difference was found recently [6]. Radioactive tracer-exchange studies at 20°C have yielded valuable insights into the mechanism of transport [7]. Other studies using centrifugal washing of cells, after incubation with the labelled glucose at 0°C (to slow down the exchange rates), have also contributed mechanistic insights [8].…”

Section: Introductionmentioning

confidence: 98%

Glucose transport in human erythrocytes measured using ¹³C NMR spin transfer

1987

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We present the results of a new NMR-based procedure for measuring the fast transmembrane exchange of D-[l:aC]glucose in human erythrocytes. The method relies on different rates of exchange between the ct-and fl-anomers of glucose inside and outside the cells; the rate outside the cells is greatly increased by the addition of mutarotase to the suspension. Theory is developed to describe nuclear-spin transfer in the present system and is used to analyse the data to yield estimates of transmembrane-exchange rate constants and their statistical uncertainties. For a total glucose concentration of 25.5 mmol/l at 40 ° C the first order efflux rate constants for the ct-and fl-anomers were 1.20 + 0.40 s -~ and 0.71 + 0.30 s-~, respectively.Glucose transport; ~3C-NMR; Spin transfer; (Human erythrocyte)

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Kinetic tests of models for sugar transport in human erythrocytes and a comparison of fresh and cold-stored cells

Cited by 45 publications

References 16 publications

ATP-dependent sugar transport complexity in human erythrocytes

ATP-dependent sugar transport complexity in human erythrocytes

Effects of low ionic strength media on passive human red cell monovalent cation transport.

Glucose transport in human erythrocytes measured using ¹³C NMR spin transfer

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Kinetic tests of models for sugar transport in human erythrocytes and a comparison of fresh and cold-stored cells

Cited by 45 publications

References 16 publications

ATP-dependent sugar transport complexity in human erythrocytes

ATP-dependent sugar transport complexity in human erythrocytes

Effects of low ionic strength media on passive human red cell monovalent cation transport.

Glucose transport in human erythrocytes measured using 13C NMR spin transfer

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Glucose transport in human erythrocytes measured using ¹³C NMR spin transfer