The temperature dependence of the exchange transport of glucose in human erythrocytes

Lacko, L.; Wittke, B.; Geck, Peter

doi:10.1002/jcp.1040820209

Cited by 64 publications

(22 citation statements)

References 9 publications

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“…We are thus faced with difficulties in trying to compare the present results obtained with galactose with all those reported in the literature which deal with glucose. The mere difference in experimental methodologies could be the reason for the discrepancy between the present values of E. for the maximal velocity and some of those reported previously for glucose (Bolis et al 1970;Lacko et al 1973) and for galactose (Lacko & Burger, 1963), which are significantly lower. Nevertheless, the dependence of Vmax on temperature obtained in the present work yields E. values comparable to those reported by several other investigators.…”

Section: Influx Macurement8contrasting

confidence: 90%

“…Similar non-linearities in the Arrhenius plots, previously reported by other investigators (Sen & Widdas, 1962;Bolis et al 1970;Lacko et al 1973) functional implication of changes in the physical state of the lipid matrix requires either an hydrophobic interaction between the membrane lipids and the proteinaceous hexose transporter, or a protein-protein interaction due to changes in the relative concentration of the transporter resulting from its redistribution between liquid and solid phases (Thilo, TrAuble & Overath, 1977). It should be noted here that whereas Vee -Vit at 0 0C, above this temperature the ratio Vee/ Vit is between 2 and 3.…”

Section: Influx Macurement8supporting

confidence: 77%

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Effects of temperature on the transport of galactose in human erythrocytes.

Ginsburg¹,

Yeroushalmy²

1978

The Journal of Physiology

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SUMMARYThe transport of galactose in human erythrocytes has been resolved recently into a mechanism which involves two asymmetric carriers operating in antiparallel fashion. The effects of temperature on this mediated transport system in the range of 0-25 00 show the following features. The Michaelis constants for zero-trans influx and efflux and for equilibrium-exchange efflux, do not vary with temperature. Arrhenius plots of the maximal velocities show breaks between 3 and 15 00 with activation energies two-to threefold larger below the break than above it. The relative contribution of the two types of carriers to the total transport rate is not affected by temperature.The kinetic properties of the prevalent type of carriers are analysed in terms of the simple carrier model as formulated by Lieb & Stein (1974). This analysis shows that the relative concentration of the unloaded carrier at the inner interface of the membrane increases upon cooling. The free energy of translocation of the unloaded carrier and the change in entropy involved in this step are significantly larger in the low temperature range (0-5 "C) than in the higher range (15-25 TC). The results are discussed briefly in terms of possible lipid-protein interaction and the physicochemical nature of the erythrocyte membrane.

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Section: Influx Macurement8contrasting

confidence: 90%

Section: Influx Macurement8supporting

confidence: 77%

Effects of temperature on the transport of galactose in human erythrocytes.

Ginsburg¹,

Yeroushalmy²

1978

The Journal of Physiology

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“…A change in activation energy at about 20 ~ has also been reported for D-glucose exchange transport in human erythrocytes (Lacko, Wittke & Geck, 1973), although a similar study failed to detect a transition temperature for this system (Hankin & Stein, 1972). The transition temperature for 2-deoxy-D-glucose transport in N1S1-67 cells is significantly higher than that reported for the D-glucose transport system of erythrocytes.…”

Section: Resultsmentioning

confidence: 71%

Temperature-dependent changes in activation energies of the transport systems for nucleosides, choline and deoxyglucose of cultured Novikoff rat hepatoma cells and effects of cytochalasin B and lipid solvents

Plagemann

Erbe

1975

J. Membrain Biol.

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The initial rates of transport of uridine, thymidien, purines, choline and 2-deoxy-D-glucose by cultured Novikoff rat hepatoma cells were determined as a function of temperature between 5 and 41 degrees C. Arrhenius plots of all transport systems exhibited sharp breaks in slope; between 17 and 23 degrees for uridine, thymidine and hypoxanthine-guanine transport and between 29 and 32 degrees for choline and 2-deoxy-D-glucose transport. The activation energies for the transport systems changed from 15-26 kcal/mole below the transition temperatures to 4-9 kcal/mole above the transition temperatures. Propagation of the cells in the presence of cis-6-octadecenoic acid which results in marked changes in the lipid composition of cell membrane, had little effect on the temperature characteristics of the various transport systems. Similarly, propagation of the cells for 24 hr in media containing Tween 40 or nystatin had no effect on the capacity of the cells to transport the various substrates or on the temperature dependence of the transport systems. The presence of ethanol, phenethyl alcohol or Persantin at concentrations that inhibited thymidine and 2-deoxy-D-glucose transport between 40 and 70% also did not alter the transition temperatures or activation energies for the transport of these substrates. Cytochalasin B, on the other hand, shifted the transition temperature for 2-deoxy-D-glucose transport to higher temperatures in a concentration-dependent manner, whereas it had no effect on the temperature dependence of thymidien transport.

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“…In an accelerated exchange uptake experiment, cells are first loaded with various concentrations of unlabeled sugar, and the rate of unidirectional, radiolabeled sugar uptake is measured at a fixed extracellular sugar concentration. At 20°C and lower, where transport can be measured accurately, unidirectional sugar uptake is accelerated severalfold by loading cells with unlabeled sugar, and exit is accelerated by extracellular sugar (73).…”

Section: Glut1 Displays Accelerated Exchangementioning

confidence: 99%

Will the original glucose transporter isoform please stand up!

Carruthers

DeZutter

Ganguly

et al. 2009

American Journal of Physiology-Endocrinology and Metabolism

184

190

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Monosaccharides enter cells by slow translipid bilayer diffusion by rapid, protein-mediated, cation-dependent cotransport and by rapid, protein-mediated equilibrative transport. This review addresses protein-mediated, equilibrative glucose transport catalyzed by GLUT1, the first equilibrative glucose transporter to be identified, purified, and cloned. GLUT1 is a polytopic, membranespanning protein that is one of 13 members of the human equilibrative glucose transport protein family. We review GLUT1 catalytic and ligand-binding properties and interpret these behaviors in the context of several putative mechanisms for protein-mediated transport. We conclude that no single model satisfactorily explains GLUT1 behavior. We then review GLUT1 topology, subunit architecture, and oligomeric structure and examine a new model for sugar transport that combines structural and kinetic analyses to satisfactorily reproduce GLUT1 behavior in human erythrocytes. We next review GLUT1 cell biology and the transcriptional and posttranscriptional regulation of GLUT1 expression in the context of development and in response to glucose perturbations and hypoxia in blood-tissue barriers. Emphasis is placed on transgenic GLUT1 overexpression and null mutant model systems, the latter serving as surrogates for the human GLUT1 deficiency syndrome. Finally, we review the role of GLUT1 in the absence or deficiency of a related isoform, GLUT3, toward establishing the physiological significance of coordination between these two isoforms. glucose transport; facilitated diffusion; major facilitator superfamily protein; bloodbrain barrier; placenta; diabetes; glucose transporter 1 deficiency syndrome; development MOST CELLS TRANSPORT SUGARS rapidly down the prevailing concentration gradient into or out of the cell. This equilibrative transport process is mediated by a family of sugar transporters called GLUTs. GLUT1 was the first glucose transporter isoform to be identified, purified (66, 132), and cloned (93) and is one of 13 proteins that comprise the human equilibrative glucose transporter family (63). GLUT1 is a membrane-spanning glycoprotein containing 12 transmembrane domains with a single N-glycosylation site, and its gene is located on chromosome 1 (1p35-31.3) (93). GLUT1 is expressed at the highest levels in the plasma membranes of proliferating cells forming the early developing embryo, in cells forming the blood-tissue barriers, in human erythrocytes and astrocytes, and in cardiac muscle (86). Having a catalytic turnover of ϳ1,200/s (115), glucose transporter 1 (GLUT1) provides an efficient pathway for cellular import and export of glucose. In addition, GLUT1 transports galactose and ascorbic acid (81,107). This review examines the catalytic properties, structure, molecular regulation, and physiology of GLUT1. GLUT1 CATALYTIC PROPERTIES Facilitated DiffusionThe cytoplasm of most cells equilibrates rapidly with nonmetabolizable extracellular sugars. This process is mediated by sugar transport proteins that catalyze unidirectional sugar up...

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The temperature dependence of the exchange transport of glucose in human erythrocytes

Cited by 64 publications

References 9 publications

Effects of temperature on the transport of galactose in human erythrocytes.

Effects of temperature on the transport of galactose in human erythrocytes.

Temperature-dependent changes in activation energies of the transport systems for nucleosides, choline and deoxyglucose of cultured Novikoff rat hepatoma cells and effects of cytochalasin B and lipid solvents

Will the original glucose transporter isoform please stand up!

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