Characterization of the rabbit intestinal fructose transporter (GLUT5)

Miyamoto, Ken‐ichi; Tatsumi, Sawako; Morimoto, Akira; Minami, Hisanori; Yamamoto, Hironori; Sone, Kanako; Taketani, Yutaka; Nakabou, Yukihiro; Oka, Tatsuzo; Takeda, Eiji

doi:10.1042/bj3030877

Cited by 67 publications

(67 citation statements)

References 35 publications

(60 reference statements)

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“…Therefore, since GLUT5 is considered to be a fructose transporter in vivo, with only a low affinity for glucose [25], and GLUT1 protein levels in the renal tubule are generally considered to be reduced [26,27] or unchanged in diabetes [9], it is reasonable to hypothesise that GLUT2 might be responsible for glucose-induced tubular cell hypertrophy in diabetes. Indeed, two indirect findings also suggest a potential pathophysiological link between GLUT2 function and the kidney: one is the finding of renal hypertrophy and glomerulopathy in patients with GLUT2 mutations in the Fanconi-Bickel syndrome [28]; the other is the recent observation that flavonoids, which are known to ameliorate the changes of diabetic nephropathy in experimental models [29], inhibit GLUT2 production [30].…”

Section: Discussionmentioning

confidence: 99%

GLUT2 protein at the rat proximal tubule brush border membrane correlates with protein kinase C (PKC)-βl and plasma glucose concentration

et al. 2007

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Aims/hypothesis GLUT2 is the main renal glucose transporter upregulated by hyperglycaemia, when it becomes detectable at the brush border membrane (BBM). Since glucoseinduced protein kinase C (PKC) activation in the kidney is linked to diabetic nephropathy, we investigated the effect of glycaemic status on the protein levels of PKC isoforms α, βI, βII, δ and ɛ in the proximal tubule, as well as the relationship between them and changes in GLUT2 production at the BBM. Methods Plasma glucose concentrations were modulated in rats by treatment with nicotinamide 15 min prior to induction of diabetes with streptozotocin. Levels of GLUT2 protein and PKC isoforms in BBM were measured by western blotting. Additionally, the role of calcium signalling and PKC activation on facilitative glucose transport was examined by measuring glucose uptake in BBM vesicles prepared from proximal tubules that had been incubated either with thapsigargin, which increases cytosolic calcium, or with the PKC activator phorbol 12-myristate,13-acetate (PMA).Results Thapsigargin and PMA enhanced GLUT-mediated glucose uptake, but had no effect on sodium-dependent glucose transport. Diabetes significantly increased the protein levels of GLUT2 and PKC-βI at the BBM. Levels of GLUT2 and PKC-βI correlated positively with plasma glucose concentration. Diabetes had no effect on BBM levels of α, βII, δ or ɛ isoforms of PKC. Conclusions/interpretation Enhanced GLUT2-mediated glucose transport across the proximal tubule BBM during diabetic hyperglycaemia is closely associated with increased PKC-βI. Thus, altered levels of GLUT2 and PKC-βI proteins in the BBM may be important factors in the pathogenic processes underlying diabetic renal injury.

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Section: Discussionmentioning

confidence: 99%

GLUT2 protein at the rat proximal tubule brush border membrane correlates with protein kinase C (PKC)-βl and plasma glucose concentration

et al. 2007

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“…It is thought that GLUT5 participates in the uptake of glucose from the lumen of the small intestine and in the reabsorption of glucose in the kidney. Its physiological function, however, may differ among species [70] and remains unclear in the bovine liver.…”

Section: Immunological Studiesmentioning

confidence: 99%

“…Unlike human organs, the liver and kidney of lactating cows express a high GLUT5 mRNA level [100], the physiological role of this transporter still being a matter of conjoncture [70]. It is thought that GLUT5 participates in the uptake of glucose from the lumen of the small intestine and in the reabsorption of glucose in the kidney.…”

Section: Immunological Studiesmentioning

confidence: 99%

“…The intestinal fructose transporter (GLUT5) was characterized at the protein level in rabbits [70]. The GLUT2 protein was detected in the sheep liver [38], and was studied at the mRNA levels in bovine [101] and chicken liver [97].…”

Section: Regulation Of Glucose Fate By Insulinmentioning

confidence: 99%

“…1). To our knowledge, when considering farm animals, GLUT2 cDNA was only cloned from chickens [97] and GLUT5 cDNA only from rabbits [70].…”

Section: Immunological Studiesmentioning

confidence: 99%

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Facilitative glucose transporters in livestock species

Hocquette

Abé

2000

Reprod. Nutr. Dev.

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-The study of facilitative glucose transporters (GLUT) requires carefully done immunological experiments and sensitive molecular biology approaches to identify the various mechanisms which control GLUT expression at the RNA and protein levels. The cloning of species-specific GLUT cDNAs showed that GLUT4 and GLUT1 diverge less among species than other GLUT isoforms. The key role of GLUT in glucose homeostasis has been demonstrated in livestock species. In vitro studies have suggested specific roles of GLUT1 and GLUT3 in avian cells. In vivo studies have demonstrated a regulation of GLUTs (especially of GLUT4) by nutritional and hormonal factors in pigs and cattle, in lactating cows and goats and throughout the foetal life in the placenta and tissues of lambs and calves. All these results suggest that any changes in GLUT expression and activity (such as GLUT4 in muscles) could modify nutrient partitioning and tissue metabolism, and hence, the qualities of animal products (milk, meat).glucose transporter / pig / ruminant / poultry Résumé -Les transporteurs du glucose à diffusion facilitée chez les animaux de ferme. L'étude des transporteurs du glucose à diffusion facilitée (GLUT) nécessite des techniques en immunologie ou en biologie moléculaire précises et sensibles pour étudier la régulation de leur expression au niveau ARNm ou protéique. Le clonage d'ADNc des différents GLUT a montré que GLUT4 et GLUT1 divergent moins entre espèces que les autres isoformes de GLUT. Le rôle important des GLUT dans le contrôle de l'homéostasie du glucose a été démontré chez les animaux de ferme. Des études in vitro ont suggéré un rôle spécifique de GLUT1 et de GLUT3 dans les cellules aviaires. Des études in vivo ont mis en évidence une régulation des GLUT (notamment GLUT4) par des facteurs nutritionnels ou hormonaux chez le porc et le bovin, chez la vache ou la chèvre en lactation, et tout au long de la vie foetale dans le placenta et les tissus de l'agneau ou du veau. L'ensemble de ces résultats suggère que tout changement dans l'expression et l'activité des GLUT (tel que de GLUT4 dans les muscles) peut modifier la répartition des nutriments et le métabolisme tissulaire, et affecter ainsi la qualité des produits animaux (lait, viande).transporteur du glucose / porc / ruminant / volaille Reprod. Nutr. Dev. 40 (2000) 517-533 517

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Metabolic pathways for glucose in astrocytes

Wiesinger

Hamprecht

Dringen

1997

Glia

164

110

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Cultured astroglial cells are able to utilize the monosaccharides glucose, mannose, or fructose as well as the sugar alcohol sorbitol as energy fuel. Astroglial uptake of the aldoses is carrier‐mediated, whereas a non‐saturable transport mechanism is operating for fructose and sorbitol. The first metabolic step for all sugars, including fructose being generated by enzymatic oxidation of sorbitol, is phosphorylation by hexokinase. Besides glucose only mannose may serve as substrate for build‐up of astroglial glycogen. Whereas glycogen synthase appears to be present in astrocytes as well as neurons, the exclusive localization of glycogen phosphorylase in astrocytes and ependymal cells of central nervous tissue correlates well with the occurrence of glycogen in these cells. The identification of lactic acid rather than glucose as degradation product of astroglial glycogen appears to render the presence of glucose‐6‐phosphatase in cultured astrocytes an enigma. The colocalization of pyruvate carboxylase, phosphenolpyruvate carboxykinase and fructose‐1,6‐bisphosphatase points to astrocytes as being the gluconeogenic cell type of the CNS. GLIA 21:22–34, 1997. © 1997 Wiley‐Liss, Inc.

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Characterization of the rabbit intestinal fructose transporter (GLUT5)

Cited by 67 publications

References 35 publications

GLUT2 protein at the rat proximal tubule brush border membrane correlates with protein kinase C (PKC)-βl and plasma glucose concentration

GLUT2 protein at the rat proximal tubule brush border membrane correlates with protein kinase C (PKC)-βl and plasma glucose concentration

Facilitative glucose transporters in livestock species

Metabolic pathways for glucose in astrocytes

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