Zur Kinetik der Glucose‐Aufnahme in Erythrocyten

Lacko, L.; Wittke, B.; Kromphardt, Hedwig

doi:10.1111/j.1432-1033.1972.tb01714.x

Cited by 87 publications

(18 citation statements)

References 10 publications

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“…The level of GLUT1 may reflect the rate of glucose transport into cells, since this transporter exhibits kinetic asymmetry, with a lower K m value for net influx than for either equilibrium exchange or net efflux [34,53]. High levels of GLUT1 and hexokinase I allow oncocytes to produce large amounts of glucose-6-phosphate, the substrate for various metabolic pathways.…”

Section: Discussionmentioning

confidence: 99%

Over-expression of glucose transporter isoform GLUT1 and hexokinase I in rat renal oncocytic tubules and oncocytomas

Ahn

Rempel

Zerban

et al. 1994

Vichows Archiv A Pathol Anat

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Renal oncocytomas, which have previously been shown to originate from the collecting duct system, were induced in male Sprague-Dawley rats by oral administration of N-nitrosomorpholine (NNM) for 7 weeks. The expression of glucose transporter isoforms GLUT1 and GLUT2, and of several enzymes involved in glucose metabolism [hexokinase (HK), pyruvate kinase (PK), lactate dehydrogenase (LDH), malate dehydrogenase (MDH)] were studied by cytochemical approaches in serial cryostat sections of the kidney 12, 23 and 34 weeks after withdrawal of NNM. Oncocytic tubules connected with collecting ducts were first observed 23 weeks, and oncocytomas 34 weeks after withdrawal. The cytochemical pattern of oncocytic tubules and oncocytomas was similar, but differed markedly from that of normal collecting ducts in nearly all variables studied; expression of GLUT1 and hexokinase I proteins were strongly increased; activities of HK, PK and MDH were elevated, while LDH activity was reduced. These results suggest that oncocytic transformation is associated with fundamental changes in energy metabolism which differ from those in cell lineages leading to other types of renal cell tumours, such as clear/acidophilic and basophilic cell tumours. The characteristic over-expression of GLUT1 may be used as a diagnostic criterion for the discrimination between oncocytes and acidophilic (granular) cells in clear/acidophilic renal cell tumours which show a reduced expression of this glucose transporter protein.

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Section: Discussionmentioning

confidence: 99%

Over-expression of glucose transporter isoform GLUT1 and hexokinase I in rat renal oncocytic tubules and oncocytomas

Ahn

Rempel

Zerban

et al. 1994

Vichows Archiv A Pathol Anat

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“…Moreover, although a wealth of kinetic information is available for glucose transport and the specificity of the erythrocyte-type transporter (GLUTI), relatively little is known about other transporter isoforms [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3) glucose transporters in Xenopus oocytes: substrate specificities and effects of transport inhibitors

Colville

Seatter

Jess

et al. 1993

Biochemical Journal

156

123

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We have expressed the human isoforms of the liver-type (GLUT2) and brain-type (GLUT3) facilitative glucose transporters in oocytes from Xenopus laevis via injection of in vitro transcribed mRNA. As reported previously [Gould, Thomas, Jess and Bell (1991) Biochemistry 30, 5139-5145], GLUT2 mediates the transport of fructose and galactose, and GLUT3 mediates the transport of galactose. We have examined the effects of D-glucose, D-fructose and maltose on deoxyglucose transport in oocytes expressing GLUT2, and D-glucose, D-galactose and maltose on deoxyglucose transport in oocytes expressing GLUT3, and show that each sugar is a competitive inhibitor of transport. Moreover, D-glucose and maltose competitively inhibit fructose transport by GLUT2 and galactose transport by GLUT3, indicating that the transport of the alternative substrates for these transporters is likely to be mediated by the same outward-facing sugar-binding site used by glucose. Cytochalasin B is a non-competitive inhibitor of glucose transport by the well-characterized GLUT1 isoform. We show here that cytochalasin B is also a non-competitive inhibitor of the transport of deoxyglucose and alternative substrates by GLUT2 and GLUT3 expressed in oocytes. Km and Ki values for each substrate and inhibitor are presented for each isoform, together with further analysis of the binding sites for alternative substrates for these transporter isoforms.

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“…The contribution of glucose transport sites to the observed binding site population can be determined by using (i) cytochalasin B, which competitively inhibits glucose binding to the transport sites on the erythrocyte glucose transporter (12,13) and (ii) L-glucose, which does not bind to the transport sites (14,15). The characteristic inversion of the ,B-H2 NOE (Fig.…”

Section: F1(s) = (Wo2 -+W) Vsmentioning

confidence: 99%

A proton NMR study of the mechanism of the erythrocyte glucose transporter.

Wang¹,

Falke²,

Chan³

1986

Proc. Natl. Acad. Sci. U.S.A.

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A generalizable 'H NMR technique is developed and used to monitor (3-D-glucose binding to glucose transport sites on erythrocyte membranes. This technique provides resolution of fl-D-glucose binding sites on opposite sides of the membrane, thereby enabling study of recruitment of transport sites from one side of the membrane to the other.Cytochalasin B, which competitively and specifically inhibits glucose binding to the inward-facing glucose transport site, recruits all glucose transport sites on both sides of the membrane to the inward-facing conformation. This result strongly supports a one-site model in which a single transport site alternates between distinct inward-and outward-facing conformations. The rate-limiting step in the transport process is translocation of the transport site between the two conformations, since the (3-D-glucose binding and dissociation events at both the inward-and outward-facing transport sites are shown to be fast compared to the known turnover rate of the glucose transport cycle. A model is presented for the transport machinery in which the glucose molecule binds in a cleft between channel-forming transmembrane helices, and during the transport event a sliding barrier moves past the transport site, thereby exposing the site to the opposite solution compartment.

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Zur Kinetik der Glucose‐Aufnahme in Erythrocyten

Cited by 87 publications

References 10 publications

Over-expression of glucose transporter isoform GLUT1 and hexokinase I in rat renal oncocytic tubules and oncocytomas

Over-expression of glucose transporter isoform GLUT1 and hexokinase I in rat renal oncocytic tubules and oncocytomas

Kinetic analysis of the liver-type (GLUT2) and brain-type (GLUT3) glucose transporters in Xenopus oocytes: substrate specificities and effects of transport inhibitors

A proton NMR study of the mechanism of the erythrocyte glucose transporter.

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