Facilitated Hexose Transporters: New Perspectives on Form and Function

Manolescu, Andrei; Witkowska, Kate; Kinnaird, Adam; Cessford, Tara A.; Cheeseman, Chris I.

doi:10.1152/physiol.00011.2007

Cited by 205 publications

(208 citation statements)

References 56 publications

(62 reference statements)

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“…81 for review). In the original studies, GLUT3 was consistently found to exhibit a lower K m than its other Class 1 counterparts, GLUT1, -2, and -4, with K m values for 2-deoxyglucose uptake of 1.4 mM compared with GLUT1, 6.9 mM, GLUT2, 11.2 mM, and GLUT4, 4.6 mM; K m values for 3-O-methylglucose equilibrium exchange of 10.6 compared with K m for GLUT1, -2, and -4 of 21, 42, and 4.5 mM, respectively (6,46,47,63,81,96). GLUT3 was also shown to transport mannose, galactose, and xylose but is unable to transport fructose.…”

Section: Kineticsmentioning

confidence: 94%

See 1 more Smart Citation

The facilitative glucose transporter GLUT3: 20 years of distinction

Simpson

Dwyer

Malide

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

395

322

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Glucose metabolism is vital to most mammalian cells, and the passage of glucose across cell membranes is facilitated by a family of integral membrane transporter proteins, the GLUTs. There are currently 14 members of the SLC2 family of GLUTs, several of which have been the focus of this series of reviews. The subject of the present review is GLUT3, which, as implied by its name, was the third glucose transporter to be cloned (Kayano T, Fukumoto H, Eddy RL, Fan YS, Byers MG, Shows TB, Bell GI. J Biol Chem 263: [15245][15246][15247][15248] 1988) and was originally designated as the neuronal GLUT. The overriding question that drove the early work on GLUT3 was why would neurons need a separate glucose transporter isoform? What is it about GLUT3 that specifically suits the needs of the highly metabolic and oxidative neuron with its high glucose demand? More recently, GLUT3 has been studied in other cell types with quite specific requirements for glucose, including sperm, preimplantation embryos, circulating white blood cells, and an array of carcinoma cell lines. The last are sufficiently varied and numerous to warrant a review of their own and will not be discussed here. However, for each of these cases, the same questions apply. Thus, the objective of this review is to discuss the properties and tissue and cellular localization of GLUT3 as well as the features of expression, function, and regulation that distinguish it from the rest of its family and make it uniquely suited as the mediator of glucose delivery to these specific cells.neurons; sperm; preimplantation embryo; white blood cells GLUCOSE METABOLISM IS VITAL to most mammalian cells, and the passage of glucose across cell membranes is facilitated by a family of integral membrane transporter proteins, the GLUTs. There are currently 14 members of the SLC2 family of GLUTs, several of which have been the focus of this series of reviews. The subject of the present review is GLUT3 which, as implied by its name, was the third glucose transporter to be cloned (62) and was originally designated as the neuronal glucose transporter. Together with GLUT1, -2, and -4, it comprises the Class 1 group of transporters (For review see Refs. 15,81,121). With the cloning of GLUT3, it became apparent that the brain did not rely exclusively on GLUT1 and that GLUT3 was highly and specifically expressed by neurons. Thus, GLUT3 became the third facilitative glucose transporter isoform with unique characteristics suited for cell-specific expression and function. GLUT2 is ideally suited for expression in liver and pancreas due to its high K m for glucose; GLUT4 and its translocation from intracellular vesicles to the cell surface facilitates insulin-stimulated glucose uptake in insulin-sensitive cells: muscle and fat. The overriding question that drove the early work in GLUT3 in the brain was: why would neurons need a separate glucose transporter isoform; what is it about GLUT3 that specifically suits the needs of the highly metabolic and oxidative neuron with its high glucose demand?...

show abstract

Section: Kineticsmentioning

confidence: 94%

“…Together with GLUT1, -2, and -4, it comprises the Class 1 group of transporters (For review see Refs. 15,81,121). With the cloning of GLUT3, it became apparent that the brain did not rely exclusively on GLUT1 and that GLUT3 was highly and specifically expressed by neurons.…”

mentioning

confidence: 99%

The facilitative glucose transporter GLUT3: 20 years of distinction

Simpson

Dwyer

Malide

et al. 2008

American Journal of Physiology-Endocrinology and Metabolism

395

322

View full text Add to dashboard Cite

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“…The glycogen content in a cell depends on the intracellular levels of glucose, which in turn may also be dependent on the glucose transport across the plasma membrane via GLUTs. In fat and muscle cells, GLUT4, a unique insulin-sensitive glucose transporter, is translocated in the presence of insulin from the cell interior to the plasma membrane, enabling glucose entry (67). Astrocytes appear to express GLUT1 and GLUT3 at a high level but very little GLUT2 and GLUT4 (27).…”

Section: Insulin and Igf-1 Increase Glycogen Content In Astrocytes Inmentioning

confidence: 99%

Insulin and Insulin-like Growth Factor 1 (IGF-1) Modulate Cytoplasmic Glucose and Glycogen Levels but Not Glucose Transport across the Membrane in Astrocytes

Muhič

Vardjan

Chowdhury

et al. 2015

Journal of Biological Chemistry

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Background: Astrocytes contain glycogen, an energy buffer in the brain. Results: Stimulation with insulin and IGF-1 decreases cytosolic glucose concentration in astrocytes without affecting glucose entry across the astrocyte plasma membrane. Conclusion: Insulin and IGF-1 boost the process of glycogen formation. Significance: This is the first high temporal resolution measurement of the decrease of glucose levels in astrocytes resulting from insulin and IGF-1 stimulation.

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“…The glucose transporter (GluT) protein family consists of 14 members grouped into three major classes based on sequence homology and substrate selectivity (8). GluT proteins mediate the transport of glucose and other monosaccharides into and out of mammalian cells according to a concentration gradient (9).…”

Section: Introductionmentioning

confidence: 99%

“…oncogenes and growth factors are responsible for GluT overexpression in malignant cells (8). increase in glucose transport and metabolism may reflect an adaptative requirement by these rapidly growing cells for more sources of energy (11).…”

Section: Introductionmentioning

confidence: 99%

Glucose transporter expression and the potential role of fructose in renal cell carcinoma: A correlation with pathological parameters

Aparicio¹

2010

Mol Med Rep

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Abstract. all mammalian cells contain one or more members of the facilitative glucose transporter (GluT) gene family. Glucose transporter membrane proteins (GluT) regulate the movement of glucose between the extracellular and intracellular compartments, maintaining a constant supply of glucose available for metabolism. Tumor cells are highly energy-dependent, therefore GluT overexpression is often observed. in fact, overexpression of GluT1 has been correlated with hypoxia markers in several tumor types, including renal cell carcinoma (rcc). We retrospectively analyzed 80 paraffin-embedded RCC samples. The pattern of GLUT1-5 expression in rcc specimens was evaluated using tissuearray technology and correlated with histological tumor characteristics. Pathological parameters included tumor location, renal pelvis, vein and lymph vessel invasion, capsule breakage, histological subtype, Furhman grade, hilar invasion and tumor stage at diagnosis. The expression of five facilitative glucose transporters, GluT1 (erythrocyte type), GluT2 (liver type), GluT3 (brain type), GluT4 (muscle/fat type) and GluT5 (small intestinal type), was semi-quantitatively analyzed. in non-parametric, Mann-Whitney u and KruskalWallis tests, a significant positive correlation was consistently found between moderately differentiated rcc tissues and the expression of GluT5 (p=0.024). Patients who had pelvic invasion and capsule breakage at diagnosis also showed increased GluT5 expression levels (p=0.039 and p=0.019, respectively). Moreover, GLUT5 showed statistical significance in those samples identified as being of clear cell histological type (p=0.001). a high expression of GluT5 in human rcc was observed. GluT5 appears to be correlated with grade ii differentiation, locoregional invasion and aggressiveness, and may play a role in rcc development.

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Facilitated Hexose Transporters: New Perspectives on Form and Function

Cited by 205 publications

References 56 publications

The facilitative glucose transporter GLUT3: 20 years of distinction

The facilitative glucose transporter GLUT3: 20 years of distinction

Insulin and Insulin-like Growth Factor 1 (IGF-1) Modulate Cytoplasmic Glucose and Glycogen Levels but Not Glucose Transport across the Membrane in Astrocytes

Glucose transporter expression and the potential role of fructose in renal cell carcinoma: A correlation with pathological parameters

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