Interaction of some disaccharides with the carrier system for aldoses in erythrocytes

Lacko, L.; Burger, M.

doi:10.1042/bj0830622

Cited by 49 publications

(19 citation statements)

References 6 publications

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“…Similar findings have been described in human erythrocytes, i.e. that maltose is a competitive inhibitor of glucose transport, binding at or close to the sugar influx site (Lacko & Burger, 1962 ;Carruthers & Helgerson, 1991).…”

Section: Speciessupporting

confidence: 86%

“…Assuming that the competitive inhibition is caused by the binding of one of the glucose residues of maltose to the extracellular glucose-binding site of the glucose transporter, we wondered whether there was a correlation between the structure of the disaccharide and the inhibition of glucose transport, as previously suggested by Lacko & Burger (1962). Maltose inhibits glucose transport in different yeasts of the genus Saccharomyces ; however, other disaccharides of glucose, cellobiose, isomaltose and α,α-trehalose, did not cause significant inhibition (data not shown).…”

Section: Speciesmentioning

confidence: 92%

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Strategies to determine the extent of control exerted by glucose transport on glycolytic flux in the yeast Saccharomyces bayanus

et al. 1999

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The extent to which the transport of glucose across the plasma membrane of the yeast Saccharomyces bayanus controls the glycolytic flux was determined. The magnitude of control was quantified by measuring the effect of small changes in the activity of the glucose transport system on the rate of glucose consumption. Two effectors were used to modulate the activity of glucose transport : (i) maltose, a competitive inhibitor of the glucose transport system in S. bayanus (as well as in Saccharomyces cerevisiae) and (ii) extracellular glucose, the substrate of the glucose transport system. Two approaches were followed to derive from the experimental data the flux control coefficient of glucose transport on the glycolytic flux : (i) direct comparison of the steadystate glycolytic flux with the zero trans-influx of glucose and (ii) comparison of the change in glycolytic flux with the concomitant change in calculated glucose transport activity on variation of the extracellular glucose concentration. Both these approaches demonstrated that in cells of S. bayanus grown on glucose and harvested at the point of glucose exhaustion, a high proportion of the control of the glycolytic flux resides in the transport of glucose across the plasma membrane.

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Section: Speciessupporting

confidence: 86%

Section: Speciesmentioning

confidence: 92%

Strategies to determine the extent of control exerted by glucose transport on glycolytic flux in the yeast Saccharomyces bayanus

et al. 1999

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“…It was found that light scattering and ANS-fluorescence responses run parallel, both exhibiting higher values after 120 min incubation in the glucose-preloaded membranes (see table 1). Sucrose preloading, on the other hand, revealed higher values in the non-preloaded membranes after 120 min incubation (sucrose has no effect on transport) [8].…”

Section: Resultsmentioning

confidence: 84%

Structural change of human red cell membranes in the glucose‐preloaded state

Zimmer¹,

Lacko²

1971

FEBS Letters

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“…Maltose does not enter erythrocytes [7,14] and its displacement of internally bound cytochalasin B provides strong support for the one-site model of transport. The decreased ability of extracellular maltose to inhibit cytochalasin B binding (table 1) further suggests that the carrier in A23187-treated cells has a decreased capacity to reorient outwardly and bind substrate.…”

Section: Discussionmentioning

confidence: 99%

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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Interaction of some disaccharides with the carrier system for aldoses in erythrocytes

Cited by 49 publications

References 6 publications

Strategies to determine the extent of control exerted by glucose transport on glycolytic flux in the yeast Saccharomyces bayanus

Strategies to determine the extent of control exerted by glucose transport on glycolytic flux in the yeast Saccharomyces bayanus

Structural change of human red cell membranes in the glucose‐preloaded state

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

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