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• W2028183561 abstract "A Cell paper by Montel-Hagen et al. (2008)xMontel-Hagen, A., Kinet, S., Manel, N., Mongellaz, C., Prohaska, R., Battini, J.L., Delaunay, J., Sitbon, M., and Taylor, N. Cell. 2008; 132: 1039–1048Abstract | Full Text | Full Text PDF | PubMed | Scopus (109)See all ReferencesMontel-Hagen et al. (2008) published last year addresses the comparative physiology of ascorbate recycling in erythrocytes (Montel-Hagen et al., 2008xMontel-Hagen, A., Kinet, S., Manel, N., Mongellaz, C., Prohaska, R., Battini, J.L., Delaunay, J., Sitbon, M., and Taylor, N. Cell. 2008; 132: 1039–1048Abstract | Full Text | Full Text PDF | PubMed | Scopus (109)See all ReferencesMontel-Hagen et al., 2008). The authors claim in this paper that GLUT1-mediated glucose transport decreases whereas GLUT1-mediated dehydroascorbate (DHA) transport increases during erythropoiesis despite markedly enhanced GLUT1 expression.To support these claims, the authors measured the uptake of the phosphorylatable analog of glucose, 2-deoxy-D-glucose (2DG), at different stages of erythropoiesis in CD34+ human hematopoietic progenitor cells stimulated to differentiate by erythropoietin. They observed that the ratio of GLUT1 mRNA to GAPDH mRNA increased over 12 days of differentiation by 1000-fold; large increases in GLUT1 expression were also observed by immunoblot analysis. A 4-fold decrease in the rate of labeled 2DG accumulation was observed between day 0 and day 8, whereas with DHA uptake (also transported via GLUT1), there is approximately a 3-fold increase in uptake between day 0 and day 8.These apparent differences are ascribed to a large increase in stomatin expression during the red blood cell maturation process, which could lead to sequestration of GLUT1 within lipid rafts causing inhibition of glucose transport. In support of this hypothesis, the authors showed that 2DG uptake in erythrocytes from two patients with stomatin deficiency was increased by 50%, whereas DHA uptake was decreased by 40%.Unfortunately, interpretation of these data may be obscured by the method used to monitor 2DG uptake. The authors monitored 2DG uptake in CD34+ cells at room temperature for 30 s at a concentration of 0.5 μM. Uptake of 2DG and DHA in control erythrocytes and in erythrocytes from patients was measured over incubation times of 10 min (Figure 5C in the Cell paper). At these concentrations and temperatures, sugar equilibration in human erythrocytes occurs within 1–2 s (Carruthers, 1990xCarruthers, A. Physiol. Rev. 1990; 70: 1135–1176PubMedSee all References, Lowe and Walmsley, 1986xLowe, A.G. and Walmsley, A.R. Biochim. Biophys. Acta. 1986; 857: 146–154Crossref | PubMed | Scopus (92)See all References). It is therefore difficult to see how a difference in transport in human erythrocytes can be ascertained by this methodology. Rather, these measurements report the cellular 2DG space, which comprises cell water (equilibrated in 1–2 s) and a metabolic sink (ongoing over 10 min).The authors indicated that they observed competitive inhibition of 2DG uptake with 5 mM glucose. This will indeed reduce uptake of label via the GLUT1 glucose transporter but also will reduce uptake of label into the hexose phosphate pool. They also state that uptake of the nonmetabolizable sugar 3-O methylglucose is inhibited by 5 mM glucose over a 60 s time period. However, this information is not germane to the comparative data regarding 2DG uptake. We think that all of the differences in radiolabeled 2DG uptake must be due to incorporation of the sugar into the hexose phosphate pool. To the extent that there are differences, these can only reflect changes in the activities of the glycolytic enzymes, hexokinase, and perhaps also glucose-6-phosphate dehydrogenase, rather than GLUT1 activity. Consistent with this notion is the 90- to 150-fold downregulation of hexokinase that occurs during erythroblast maturation in humans (Shinohara et al., 1985xShinohara, K., Yamada, K., Inoue, M., Yoshizaki, Y., Ishida, Y., Kaneko, T., and Matsumoto, N. Am. J. Hematol. 1985; 20: 145–151Crossref | PubMedSee all ReferencesShinohara et al., 1985) and rabbits (Magnani et al., 1984xMagnani, M., Stocchi, V., Dacha, M., and Fornaini, G. Biochim. Biophys. Acta. 1984; 802: 346–351Crossref | PubMed | Scopus (9)See all ReferencesMagnani et al., 1984), which may result from ATP- and ubiquitin-dependent proteolysis of hexokinase (Magnani et al., 1986xMagnani, M., Stocchi, V., Chiarantini, L., Serafini, G., Dacha, M., and Fornaini, G. J. Biol. Chem. 1986; 261: 8327–8333PubMedSee all ReferencesMagnani et al., 1986).It is also probable that the rate of DHA transport is underestimated. The reported lack of inhibition of DHA uptake by glucose in red blood cells is inconsistent with previous findings in human erythrocytes (Mann and Newton, 1975xMann, G.V. and Newton, P. Ann. N Y Acad. Sci. 1975; 258: 243–252Crossref | PubMedSee all ReferencesMann and Newton, 1975), oocytes heterologously expressing GLUT1, GLUT3, or GLUT4 (Rumsey et al., 1997xRumsey, S.C., Kwon, O., Xu, G.W., Burant, C.F., Simpson, I., and Levine, M. J. Biol. Chem. 1997; 272: 18982–18989Crossref | PubMed | Scopus (262)See all References, Rumsey et al., 2000xRumsey, S.C., Daruwala, R., Al-Hasani, H., Zarnowski, M.J., Simpson, I.A., and Levine, M. J. Biol. Chem. 2000; 275: 28246–28253PubMedSee all References), and rat adipocytes expressing GLUT1 and GLUT4 (Rumsey et al., 2000xRumsey, S.C., Daruwala, R., Al-Hasani, H., Zarnowski, M.J., Simpson, I.A., and Levine, M. J. Biol. Chem. 2000; 275: 28246–28253PubMedSee all ReferencesRumsey et al., 2000). This suggests that DHA uptake was measured at time points where intracellular recycling to ascorbate, rather than partially inhibited DHA transport, is rate limiting for intracellular accumulation of radiolabel.We do not question the reproducibility of Montel-Hagen's data, only the interpretation. Although the capacity for and rate of sugar transport in human erythrocytes is large, the use of tracer concentrations of 2DG means that 2DG phosphorylation by intracellular hexokinase will constitute a large component of net radiolabel uptake even at the earliest time points recorded at low temperatures. Thus, linearity of 0.5 μM 2DG uptake by human red blood cells at early time points cannot be ascribed solely to transport. Rather, it is ambiguously affected by intracellular metabolism. At later time points (>5–10 s), even at or above 4°C, when cytosolic free sugar has fully equilibrated with the extracellular sugar pool, net uptake is solely dependent on the rate of 2DG metabolism. The only way to unambiguously define a deficit in glucose transport under the conditions used by Montel-Hagen et al. is to measure glucose flux with a nonmetabolizable analog, such as 3-O-methyl-D-glucose. This has not been done and thus at present there is no good evidence supporting the contention of differential GLUT1 transport function during erythropoiesis." @default.
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• W2028183561 title "Altered GLUT1 Substrate Selectivity in Human Erythropoiesis?" @default.
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• W2028183561 doi "https://doi.org/10.1016/j.cell.2009.04.007" @default.
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