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PubMed1985

Characterization of a photosensitive glucose derivative. A photoaffinity reagent for the erythrocyte hexose transporter.

The photosensitive reagent 6-N-(4-azido-2-hydroxy-3,5-diiodobenzoyl)-D-glucosamine has been assessed as a potential photoaffinity label for the hexose transporter. Under zero-trans conditions, transport experiments performed in the dark reveal that the reagent inhibits the uptake of D-glucose in resealed human erythrocyte ghosts. Increasing the concentration of glucose in the transport medium has a protective effect, reducing the inhibition. Kinetic analysis indicates that the probe acts as a competitive inhibitor with high affinity for the erythrocyte hexose transporter (Ki between 0.07 and 0.2 microM). Exposure to a 280 nm filtered high intensity mercury-vapor lamp results in a rapid and efficient photolysis. At low concentrations of the probe, specific labeling of membrane preparations was observed. Autoradiograms of 10% SDS gels revealed the specific labeling of bands 4.51 and 6. This labeling was concentration-dependent and protected by D-glucose (not the L-isomer) and phloretin in the medium. When subjected to multiple exposures of low concentration of the photoaffinity reagent, apparent saturation was achieved.

Affinity Labels↗
PubMed1989

Differential labeling of the erythrocyte hexose carrier by N-ethylmaleimide: correlation of transport inhibition with reactive carrier sulfhydryl groups.

Inhibition of hexose transport by N-ethylmaleimide was studied with regard to alkylation of different types of sulfhydryl group on the hexose carrier of the human erythrocyte. Uptake of 3-O-methylglucose was progressively and irreversibly inhibited by N-ethylmaleimide, with a half-maximal effect at 10-13 mM. A sulfhydryl group known to exist on the exofacial carrier was not involved in transport inhibition by N-ethylmaleimide, since reversible protection of this group by the impermeant sulfhydryl reagent 5,5'-dithiobis(2-nitrobenzoic acid) had no effect on the ability of N-ethylmaleimide to inhibit transport, or on its ability to decrease the affinity of the exofacial carrier for maltose. Nevertheless, the exofacial sulfhydryl was quite reactive with N-ethylmaleimide, since it was possible using a differential labeling technique to specifically label this group in protein-depleted ghosts with a half-maximal effect at 0.3 mM N-[3H]ethylmaleimide, and to localize it to the Mr 19,000 tryptic carrier fragment. Transport inhibition by N-ethylmaleimide correlated best with labeling of a single cytochalasin B-sensitive internal sulfhydryl group on the glycosylated Mr 23,000-40,000 tryptic fragment of the carrier, which was half-maximally labeled at about 4 mM reagent. Whereas N-ethylmaleimide readily alkylates the exofacial carrier sulfhydryl, it inhibits transport by reacting with at least one internal carrier sulfhydryl located on the glycosylated tryptic carrier fragment.

3-O-Methylglucose↗
PubMed1982

Mouse liver microsomal hexose-6-phosphate dehydrogenase. NADPH generation and utilization in monooxygenation reactions.

Hexose-6-phosphate dehydrogenase (H6PD) activity in washed hepatic microsomes from male ICR mice, when assayed with NADP+ and deoxyglucose-6-phosphate, was partially latent. Brief sonication or detergents activated H6PD causing an approximately 4- and 8.5-fold increase in NADPH generation respectively. The sonicated microsomes exhibited H6PD-linked N-demethylase activity toward aminopyrine. This activity was best sustained in the presence of deoxyglucose-6-phosphate, while galactose-6-phosphate, glucose-6-phosphate, and glucose were less effective. Reaction media containing sonicated microsomes, NADP+ and deoxyglucose-6-phosphate also catalyzed N-demethylation of p-chloro-N-methylaniline, N,N-dimethylaniline and nicotine, O-demethylation of p-nitroanisole, p-hydroxylation of aniline, ring hydroxylation of biphenyl at the 2- and 4-positions, dearylation of parathion, and the N-oxidation of N,N-dimethylaniline. In general, the hexose-6-phosphate dehydrogenase-linked monooxygenation rates were 60% or more of those observed in the presence of exogenous NADPH.

Aminopyrine N-Demethylase↗
PubMed1995

Mono-, di- and tri-antennary D-galactose ligands as competitive inhibitors and photoaffinity labels of the hexose transporting system in erythrocytes. A model for the irreversible blocking of receptors in cell membranes.

Starting from pentaerythritol, photolabile mono-, di-, and tri-dentate galactose derivatives as well as their 3H-labelled isotopomers were synthesised. The hydrophilic chains linking the 6 position of D-galactose to pentaerythritol consist of 13 atoms in line. The mono-, di- and tri-dentate compounds, although themselves not transported, inhibit in increasing order 14C-D-galactose transport into erythrocytes. On irradiating whole cells in the presence of ligand with 350-nm UV light, these compounds also in increasing order, could irreversibly block the hexose transport system. Irradiation without ligand has no effect. By using the 3H-labelled tridentate galactose compound the hexose transporter (zone 4.5) is specifically radiolabelled, as could be shown in an SDS-PAGE of membrane proteins from erythrocytes previously photoaffinity labelled. Radiolabelling is significantly suppressed in the presence of D-glucose.

Affinity Labels↗
PubMed1984

Effects of cholesterol autoxidation derivatives on hexose transport in cultured aortic smooth muscle cells.

Several cholesterol autoxidation derivatives known to be cytotoxic to arterial smooth muscle cells both in vivo and in vitro were shown to inhibit hexose transport in these cells in culture. Cholestane-3 beta, 5 alpha, 6 beta-triol was the most potent inhibitory sterol. The rapid onset of inhibition (15 min) and the reversibility of the effect upon removal of the sterol from the tissue culture medium suggests that the effect may be due to incorporation of the sterol into the plasma membrane. 25-Hydroxycholesterol, a potent inhibitor of sterol biosynthesis in cultured arterial smooth muscle cells, did not affect hexose transport up to 8 hr of incubation. The cytotoxic effect of 25-hydroxycholesterol, therefore, may be a consequence of the reduced sterol biosynthesis caused by this sterol.

Animals↗
PubMed1984

Effects of vanadate on intracellular Ca2+ redistribution and hexose transport across plasma membrane in cultured mouse fibroblasts.

The effects of vanadate on intracellular Ca2+ sequestration and hexose transport were studied in Swiss 3T3 cells. Vanadate inhibited ATP-dependent Ca2+ uptake by saponin-permeabilized Swiss 3T3 cells at 10(-5) and 10(-7) M Ca2+ at which the Ca2+ uptake was sensitive and insensitive to oligomycin plus antimycin A, respectively. On the other hand, vanadate stimulated 2-deoxy-D-glucose (2DG) uptake in a dose- and time-dependent way. The stimulation of 2DG uptake by vanadate was inhibited by EGTA plus A23187 and the inhibition was reversed by Ca2+ restoration. These results suggest that an increase in cytosolic Ca2+ by inhibition of intracellular ATP-dependent Ca2+ sequestration by vanadate results in the stimulation of hexose transport in Swiss 3T3 cells.

Animals↗
PubMed1989

Influence of experimental diabetes on the kinetic behaviour of renal cortex hexose monophosphate dehydrogenases.

1. Short term (1-2 hr) and long-term (2 days) effects of experimental alloxan induced diabetes on the kinetics of the renal hexose monophosphate shunt dehydrogenases are reported. 2. Alloxan diabetes for 2 days significantly increased kidney weight (16%) adding about 80 mg/day per g of kidney. No significant changes were found in renal growth 1-2 hr after alloxan injection. 3. Under these experimental conditions, the activities of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase significantly increased (103 and 33% respectively) at all substrate concentrations, without affecting the KmS of either enzyme. 4. There was no effect of alloxan on the activity of these enzymes at 1-2 hr. Saturation curves show that all enzymes exhibited a M-M kinetic without evidence of sigmoidicity. 5. The results suggest that increased renal hexose monophosphate dehydrogenases activities are due to increased concentrations of the rate limiting proteins. 6. The relationship between these changes and renal hypertrophy is also discussed.

Animals↗
PubMed1986

Sindbis virus infection increases hexose transport in quiescent cells.

Sindbis virus infection of baby hamster kidney cells or chick embryo cells resulted in a significant increase in the rate of uptake of [2-3H]deoxy-D-glucose ([3H]dGlu). Stimulation of hexose transport in Sindbis virus-infected cells occurred only if the cells were rendered quiescent by culturing at high density or by serum starvation. In contrast, Sindbis virus-induced inhibition of potassium transport, measured as a decrease in the uptake of 86Rb+, was independent of cell growth state. Stimulation of [3H]dGlu uptake in Sindbis virus-infected cells was the result of an increase in the Vmax of the hexose transporter, but not a change in the Km. The stimulation of [3H]dGlu uptake induced by Sindbis virus was insensitive to the drug actinomycin D, but was blocked by cordycepin. The stimulation was also insensitive to treatment with tunicamycin, which prevented the virally induced inhibition of the plasma membrane-associated Na+/K+ ATPase and termination of host protein synthesis.

Animals↗
PubMed1975

Hydrolase and serum treatment of normal chick embryo cells: effects on hexose transport.

We have asked whether treatment of normal cultured cells with proteases, other hydrolytic enzymes, or serum can convert them into transient phenocopies of transformed cells with respect to the very high rate of hexose transport characteristic of transformed cells. Treatment of density-inhibited cultures of normal chick embryo fibroblasts with trypsin, plasmin, neuraminidase, or hyaluronidase stimulated their rate of 2-deoxyglucose uptake to a level only marginally higher than that seen in normal exponentially growing cultures, and only 35-45% of that seen in transformed cultures. Addition of the hydrolytic enzymes to growing cell cultures had little effect on 2-deoxyglucose uptake. Serum, however, could stimulate 2-deoxyglucose uptake all the way up to the transformed level. Even though the hydrolases and serum differed in their ability to stimulate 2-deoxyglucose uptake, both reagents were capable of stimulating cell division equally well. Evidence is presented suggesting that the hexose transport rate is controlled by serum factors, and that proteolysis can affect the response of the cells of these factors.

Animals↗
PubMed1995

Role of 3'-untranslated regions in the regulation of hexose transporter mRNAs in Trypanosoma brucei.

Trypanosoma brucei is a unicellular parasite that is transmitted from one mammalian host to the next by tsetse flies. The expression of many trypanosome genes is regulated during the life cycle but there is no evidence for developmental control of transcription by RNA polymerase II. T. brucei expresses at least two hexose transporter mRNAs that are developmentally regulated; we show here that specific portions of the 3'-untranslated regions are responsible for the differential expression. Different trypanosome 3'-untranslated regions, from surface protein, phosphoglycerate kinase and aldolase genes as well as the hexose transporter genes, conferred a spectrum of levels of reporter gene expression, and these activities differed between bloodstream forms and the procyclic forms that replicate in the tsetse vector. Experiments with permanently transformed cell lines showed that regulation occurs at the mRNA level. The results suggest that post-transcriptional control of mRNAs in trypanosomatids operates at several levels, and that it will not always be possible to attribute all the regulation to short RNA motifs.

Animals↗
PubMed1990

Phosphoglucoisomerase-catalyzed interconversion of hexose phosphates: a model for the interconversion of D-[2-3H]glucose 6-phosphate and D-[1-3H]fructose 6-phosphate.

Based on experimental data, a model is proposed for the interconversion of either unlabelled hexose phosphates or D-[2-3H]glucose 6-phosphate and D-[1-3H]fructose 6-phosphate in the reaction catalyzed by phosphoglucoisomerase. This model takes into account the known differences in maximal velocity and affinity for each substrate, the intramolecular transfer of tritium between C1 and C2, and the isotopic discrimination between unlabelled and tritiated esters. This model reveals that, in a close system characterized by the progressive detritiation of hexose phosphates, the concentration ratio of D-glucose 6-phosphate to D-fructose 6-phosphate is much higher with the tritiated than unlabelled esters, a paradoxical increase in the specific radioactivity of D-glucose 6-phosphate above its initial value being even observed during the initial period of exposure of D-[2-3H]glucose 6-phosphate to phosphoglucoisomerase. The extension of this model to an open system may be essential for the correct interpretation of radioactive data collected in intact cells exposed to D-[2-3H]glucose.

Fructosephosphates↗
PubMed1991

Hexose metabolism in pancreatic islets. Regulation of D-[6-14C]glucose oxidation by non-nutrient secretagogues.

In rat pancreatic islets, a rise in D-glucose concentrations increases the oxidation of hexose-derived acetyl residues relative to glycolytic flux, an effect possibly attributable, in part at least, to the activation of key mitochondrial dehydrogenases by Ca2+ accumulated in the mitochondria of glucose-stimulated islet cells. The effects of non-nutrient insulinotropic agents upon D-[6-14C]glucose oxidation and D-[5-3H]glucose utilization were investigated. At an intermediate concentration of D-glucose (6 mM), the oxidation of D-[6-14C]glucose was unaffected by hypoglycemic sulfonylureas, an organic Ca2+ agonist, a cholinergic agent, forskolin, theophylline and cytochalasin B. At a higher concentration of the hexose (17 mM), however, the 14CO2/3H2O production rate was decreased by organic and inorganic Ca(2+)-antagonists and by ouabain, whilst being increased by NH+4 (10 mM) and aminooxyacetate. These findings suggest that the preferential stimulation of oxidative events in the Krebs cycle is largely independent of the rate of insulin release, and not merely consequential to the stimulation of Ca2+ inflow into the B-cell. It might be regulated, in a feedback process, by the rate of ATP utilization and, both directly and indirectly, by the mitochondrial redox state. The glucose-induced mitochondrial accumulation of Ca2+ and subsequent activation of the Krebs cycle appear to require an increase in both cytosolic Ca2+ activity and ATP availability.

Ammonia↗
PubMed1977

Latency of microsomal hexose-6-phosphate dehydrogenase activity.

Intact microsomes isolated from rat liver showed no hexose-6-phosphate dehydrogenase activity, but the enzyme was activated by Triton X-100, deoxycholate, NH4OH, glycine/NaOH, lysophosphatidylcholine, phospholipases A and C, pancreatic lipase and cholesterol esterase, and also by sonic treatment. The enzyme activation by deoxycholate, NH4OH and sonic treatments was solely due to solubilization, while that by phospholipase A appeared to be due to the detergent action of the hydrolysis products. On the other hand, the primary effects of phospholipase C, cholesterol esterase and pancreatic lipase might be accounted for by the partial removal of membrane lipids. The results of washing and trypsin digestion experiments suggested that hexose-6-phosphate dehydrogenase is one of the most firmly bound enzymes among the microsomal proteins. The catalytic properties were the same in the solubilized and the membrane-bound, activated enzymes. Feeding the rats on a high carbohydrate diet altered the extent of enzyme activation by sonication and phospholipase C treatment, suggesting that the microsomal membrane would actually undergo changes in the conformation and/or chemical composition under certain circumstances.

Alcohol Oxidoreductases↗
PubMed2005

A new hexose transporter from Cryptococcus neoformans: molecular cloning and structural and functional characterization.

We carried out a screen for Cryptococcus neoformans genes involved in resistance to copper ion toxicity and identified a new hexose transporter (Hxt) gene, HXT1. Hxt1 consists of 520 amino acids and functions to transport hexoses such as glucose. Although Hxt1 conferred copper resistance to Saccharomyces cerevisiae, disruption of the HXT1 gene showed that Hxt1 is not necessary for copper resistance. In virulence tests, an hxt1 mutant strain showed 12% less phenoloxidase activity than the wild-type strain, and no difference in the ability to form melanin was identified. In addition, the hxt1 mutant strain showed virulence similar to that of the wild-type strain in experiments with Caenorhabditis elegans. However, the hxt1 mutant strain generated larger capsules than were generated by the wild-type strain. Thus, Hxt1 appears to be involved in capsule formation.

Animals↗
PubMed1986

Dynamic assessment of hexose monophosphate shunt activity in the intact rabbit lens by proton NMR spectroscopy.

A proton nuclear magnetic resonance technique is demonstrated for ascertaining the real-time contribution of the hexose monophosphate shunt to glucose metabolism in the intact incubated rabbit lens. This measurement requires incubation of the tissue in medium supplemented with [1-13C]glucose, and depends on the presence of the 13C label in the methyl position of lactate which creates satellite resonances by way of 13C - 1H spin-spin scalar coupling. The assumptions required to make the measurement are presented. For lenses maintained under control conditions, a basal level corresponding to 5% hexose monophosphate shunt activity was determined. An eight-fold increase in activity was observed under conditions known to stimulate the shunt.

Animals↗
PubMed1976

Synthesis of 3-amino-2,3,6-trideoxy-D-ribo-hexose hydrochloride.

The title sugar, the 5-epimer of daunosamine, was prepared in a sequence of high-yielding steps from methyl alpha-D-mannopyranoside (1). Conversion of 1 into methyl 3-acetamido-4-O-benzoyl-6-bromo-2,3,6-trideoxy-alpha-D-ribo-hexopyranoside (2), followed by reduction with hydrogen and Raney nickel, gave the 4-benzoate (3) of methyl 3-acetamido-2,3,6-trideoxy-alpha-D-ribo-hexopyranoside (4). Saponification of 3 gave 4 as an oil that gave a crystalline 4-acetate (8). N-Deacetylation of 4 was effected with barium hydroxide, and the resultant glycoside was hydrolyzed to give 3-amino-2,3,6-trideoxy-D-ribo-hexose hydrochloride (7). The 3-benzamido analogue (5) of 4 was prepared from 4 by N-deacetylation and subsequent benzoylation, and hydrolysis of 5 gave crystalline 3-benzamido-2,3,6-trideoxy-D-ribo-hexose (6). The crystalline 3-acetamido analogue (9) of 6 was obtained by acid hydrolysis of the glycoside 4.

Deoxy Sugars↗
PubMed1980

Synthesis of 4-deoxy-D-xylo-hexose and 4-azido-4-deoxy-D-glucose and their effects on lactose synthase.

Syntheses are reported of 4-deoxy-D-xylo-hexose and 4-azido-4-deoxy-D-glucose as potential inhibitors for lactose synthase [uridine 5'-(alpha-D-galactopyranosyl pyrophosphate):D-glucose 4-beta-D-galactopyranosyltransferase, EC 2.4.1.22]. These syntheses involved SN2 displacement of the 4-methylsulfonyloxy group of methyl 2,3,6-tri-O-benzoyl-4-O-methylsulfonyl-alpha-D-galactopyranoside by iodide and azide ions. In both cases, inversion in configuration was observed. The resulting intermediates, methyl 2,3,6-tri-O-benzoyl-4-deoxy-4-iodo-alpha-D-glucopyranoside and methyl 4-azido-2,3,6-tri-O-benzoyl-4-deoxy-alpha-D-glucopyranoside, were obtained in crystalline form. Both 4-deoxy-D-xylo-hexose and 4-azido-4-deoxy-D-glucose were found to be inhibitors for lactose synthase in the presence of alpha-lactalbumin, but had no effect in the absence of alpha-lactalbumin. Both D-glucose analogues bind to the enzyme system far more weakly than D-glucose, suggesting that the recognition of the 4-OH group of the acceptor substrate is an important factor in binding.

Animals↗
PubMed2001

Hexose oxidase from Chondrus crispus: improved purification using perfusion chromatography(*).

1An improved method for purifying hexose oxidase (D-hexose: O(2) 1-oxidoreductase, EC 1.1.3.5) from the marine red alga Chondrus crispus is described for obtaining enzyme suitable for structural characterization and use in bioconversion of lactose to lactobionic acid. This involved extracting enzyme from finely ground lyophilized tissue in sodium phosphate buffer (pH 7) containing 20% ammonium sulfate, eliminating the previously used solvent extraction and protease treatments, and by applying Poros perfusion chromatography media to achieve rapid separations of high resolution. Primary separation of contaminating phycobiliproteins and carrageenans was achieved using Poros DEAE-50. Sequential HPLC purification steps using Poros HP2 and Poros HQ were followed by Sephacryl S200 h chromatography. Enzyme activity was determined with a peroxidase-coupled assay using 2,2'-azino-bis (3-ethylbenzthiazoline-6 sulfonic acid) substrate. A final specific activity of 69 U/mg was obtained, representing a 100-fold purification with an activity recovery of about 10%. A native size of approximately 117,000 Da was determined by size exclusion chromatography, and SDS-PAGE revealed the presence of 38,000 and 29,000 Da polypeptides that appear to be derived from a 65,000 Da subunit. Further properties of the enzyme are described.

Journal Article↗