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PubMed1982

The simple model of adipocyte hexose transport. Kinetic features, effect of insulin, and network thermodynamic computer simulations.

Kinetic studies of the rat adipocyte hexose transport system were performed using the integrated rate approach and these compared to the simple carrier model of transport. Equilibrium exchange 3-O-methylglucose entry and exit studies showed directional symmetry with Km = overall dissociation constants = 8-10 mM. Comparison of zero-trans and equilibrium exchange entry also revealed similar Km and Vmax values. Insulin pretreatment increased the maximal rate of transport at 20 mM 3-O-methylglucose about 5- to 6-fold with each procedure. Studies of glucose-induced steady state 3-O-methylglucose countertransport provided evidence that carrier permeability and not carrier-substrate dissociation was rate limiting for overall transport. These data, therefore, indicate equal mobility of the loaded and unloaded carriers. Network thermodynamic computer simulations of the simple carrier model using kinetic parameters derived from zero-trans experiments provided good fits of actual data. The effect of insulin was best represented by an increase in total number of carrier units. It is concluded that the adipocyte hexose carrier displays bidirectional symmetry, limitation of transport by carrier movement rather than substrate-carrier interaction, equal rates of movement of loaded and unloaded carriers, and adherence to a simple carrier model in which insulin increases the total number of carrier units.

3-O-Methylglucose↗
PubMed1981

The lipopolysaccharide of escherichia coli C- studies on the anomeric configurations of the hexoses in the R1 core.

Lipopolysaccharide from E, coli C as well as lipopolysaccharides from submutants of E. coli with incomplete core structures in their lipopolysaccharides were isolated and quantitatively analyzed. Core oligosaccharides were isolated from lipopolysaccharides by acetic acid degradation and were purified by gel chromatography. The difference in molecular rotations of the core oligosaccharides from E. coli C and 6 submutants thereof with incomplete core structure were correlated to the differences in sugar compositions. The anomeric configurations have been deducted from the high or low contribution of each individual sugar to the molecular rotation of the core oligosaccharide from E. coli C. The primary structure of the hexose region of the lipopolysaccharide from E. coli C is primary structure of the hexose region of the lipopolysaccharide from E. coli C is, see formula in text. The anomeric configurations of glucoses I, II, and III were confirmed by precipitation reactions of alkali treated lipopolysaccharides from E. coli C, C23. 1, and C21 with Concanavalin A. The alpha-anomeric configurations of both the galactoses were confirmed by degradation studies with alpha-galactosidase (E.C.3.2.1.22) from green coffee beans with the isolated and purified core oligosaccharide from E. coli C71.

Carbohydrate Conformation↗
PubMed1981

Broad specificity hexose transport system with differential mobility of loaded and empty carrier, but directional symmetry, is common property of mammalian cell lines.

Rapid kinetic techniques were employed to measure the transport of the nonmetabolizable hexose, 3-O-methyl-D-glucose, in suspensions of human HeLa cells, mouse L- and P388 leukemia cells, and Chinese hamster ovary cells in zero-trans entry and exit and equilibrium exchange procedures. The kinetic parameters of transport were computed by fitting appropriate integrated rate equations to time courses of transmembrane equilibration of radiolabeled substrate. Transport of all four lines, as in Novikoff rat hepatoma cells, conformed to a simple carrier model with directional symmetry but differential mobility of loaded and empty carrier. As was apparent from a comparison of influx and exchange flux, the loaded carrier of all cell types moved between 4 and 14 times faster than the empty carrier. ATP depletion of the cells by incubation in glucose-free medium containing KCN and iodoacetate had no significant effect on the kinetic properties of the transporter. ATP-depleted cells were used to measure the transport of D-glucose, 2-deoxyglucose, D-galactose, and D-glucosamine in the absence of intracellular metabolism. The differential mobilities of empty carrier and carrier loaded with these hexoses and the efficiency of their transport were equivalent to those observed with 3-O-methylglucose, but the Michaelis-Menten constants for the transport of D-galactose and D-glucosamine were 5-8-fold higher than those for D-glucose, 2-deoxy-D-glucose, and 3-O-methylglucose, which were about equivalent.

Animals↗
PubMed1981

Influence of various hexoses and vasoactive agents on osmotically induced oncolysis.

Local destruction of malignant growths was achieved rapidly by creating around their cells a strongly hypertonic environment. Various hexoses, injected in and around tumors at 37 degrees, were utilized to produce the osmotic disturbance. Homeostatic correction of the osmotic disturbance was prevented by local ischemia, induced by vasoconstriction, and maintained soon afterwards by thrombosis. Of the few vasoactive agents tested for this purpose, serotonin was the safest and most effective. It worked better when mixed with the hexose than when injected separately s.c. at a distance. The best response to treatment was obtained from tumors which were unattached to deep structures, poorly vascularized, and resistant to an increase of internal pressure, whereas special precautions had to be taken with friable neoplasms to avoid dissemination of metastases. Under certain conditions, by causing acute tumor necrosis, a single treatment achieved a high ratio of cure; in which a favorable immune response to dramatic reduction of tumor burden and to resorbed lysed material perhaps played a part.

Animals↗
PubMedDate not supplied

[Glycoprotein hexoses in feces of infants with lactose intolerance].

A modified method for estimation of total glycoprotein hexoses in feces, based on their measurements in the blood serum, is presented. Sixty-six nursing children with lactose intolerance, breastfed or formula fed, were examined; formula fed babies were kept on mixtures with high and low lactose content. Glycoprotein hexose parameters were as follows (X +/- m): 13.51 +/- 1.93, 12.05 +/- 2.20, and 3.69 +/- 0.47 g/l feces. In control children without lactose intolerance (n = 33) this value was 3.6 +/- 0.79 g/l. Increased glycoprotein excretion is connected with glycocalix and small intestinal enterocyte alteration.

Breast Feeding↗
PubMed1981

Hexose sugar transport activity in a mouse fibroblast cell line temperature sensitive for expression of the transformed phenotype.

A temperature-sensitive mouse fibroblast cell line was used to examine the relationship between hexose sugar uptake rates and the control of cell growth. The cell line (ts-H6-15) is a derivative of SV-3T3 cells, exhibiting a transformed phenotype at 32 degrees C and a normal phenotype at 39 degrees C. For cells actively growing at either temperature, a marked decrease in the rate of 3-O-methyl-D-glucose (3-O-MeG) transport is observed as cell population density increases. At cell population densities tested, 3-O-MeG transport rates (at a common assay temperature) were greater in H6-15 cells grown at 32 degrees C than at 39 degrees C, with the enhancement being maximal at the lowest cell densities. The effect of low serum-arrest on H6-15 cells revealed that cells growing at 39 degrees C arrest in G1, while cells at 32 degrees C stop more randomly throughout their cycle. Under conditions of low serum-arrest the rate of 3-O-MeG transport remained as high as in actively growing cells at both 32 degrees C and 39 degrees C. However, 2-deoxyglucose uptake rates were growth state-dependent at 39 degrees C, indicating perhaps metabolic as well as membrane-level control of sugar accumulation. These results further demonstrate that rates of hexose sugar transport by themselves are not always absolutely correlated with rates of cell proliferation and, thus, may be reliable predictors of cell growth potential.

Animals↗
PubMed1983

Hexose uptake as an indicator of JB6 mouse epidermal cell resistance to the mitogenic activity of TPA.

JB6 mouse epidermal cells have been selected for resistance to the tumor-promoting phorbol diester TPA for (1) the plateau density mitogenic (M) response, and (2) the promotion of tumor cell phenotype (P) response. The purpose of this study was to determine the relationship of hexose uptake to the two TPA-dependent processes. Monolayers of JB6 mouse epidermal cells showing one of four different phenotypes (M+P+, M+P-, M-P+, M-P-) were exposed to 60 nM [3H(G)]2-deoxy-D-glucose (2DG) with or without TPA (10 ng/ml) stimulation. The TPA mitogen-sensitive (M+P+/-) cells, when in logarithmic growth, had a lower basal 2DG uptake rate than TPA mitogen-resistant (M-P+/-) cells. At plateau density, however, only the M+P+ cells had a significantly lower basal rate. The M+ (TPA mitogen-sensitive) cells (with low basal rates), when preincubated with TPA, exhibited a two to threefold increase in 2DG uptake, while the M- (TPA mitogen-resistant) lines, which already showed elevated rates, remained unchanged. There was also a positive association between TPA mitogen sensitivity and slower growth rate. These results suggest that low hexose sugar uptake is related to TPA mitogen sensitivity, but not to promotion sensitivity. Hence the cell's ability to increase its uptake rate may be required for the cells to respond to mitogenic stimulation by TPA.

Animals↗
PubMed1986

Regulation of hexose transporters in chicken embryo fibroblasts: stimulation by the phorbol ester TPA leads to increased numbers of functioning transporters.

As has been observed with many types of cultured cells, chicken embryo fibroblasts (CEF) when exposed to the tumor promoter 12-O-tetradecanoyl-phorbol-13-acetate (TPA) develop a 3- to 4-fold increase in hexose transport activity in 4 h. This increase in transport activity occurred despite a modest decline of 20% in [3H]leucine incorporation into acid insoluble fractions. Cycloheximide largely, but not completely, blocked the increase in transport activity during TPA exposure. The effects of TPA were somewhat similar to those of glucose starvation induced enhancement of hexose transport activity. Furthermore, with TPA there was no additive effect to that produced by glucose starvation. Plasma membrane enriched fractions were prepared from CEF treated with or without TPA. Membranes prepared from TPA exposed cells had a two-fold enhancement of stereospecific D-glucose transport activity as well as D-glucose inhibitable [3H]cytochalasin B binding as compared to the membranes from control CEF. There was no effect on transport when membranes were exposed to TPA in vitro. These results provide strong evidence that TPA exposure leads to an increase in the number of functioning transporters, an effect largely requiring protein synthesis.

5'-Nucleotidase↗
PubMed1988

Structure, biosynthesis, and function of the hexose transporter in Chinese hamster ovary cells deficient in N-acetylglucosaminyltransferase 1 activity.

We have used a Chinese hamster ovary cell line deficient in N-acetylglucosaminyltransferase 1 activity (Lec1) to study the effects of altered asparagine-linked oligosaccharides on the structure, biosynthesis, and function of glucose transporter protein. Immunoblots of membranes of Lec1 cells show a glucose transporter protein of Mr 40,000, whereas membranes of wild-type (WT) cells contain a broadly migrating Mr 55,000 form similar to that observed in several other mammalian tissues. The total content of immunoreactive glucose transporters in Lec1 cells is 3.5-fold greater than that of WT cells. Digestion with endoglycosidases, treatment with inhibitors of glycosylation, and interactions with agarose-bound lectins demonstrate that glucose transporters of both cell lines derive from a similar Mr 38,000 core polypeptide and that both contain asparagine-linked oligosaccharide. Transporters in Lec1 cells contain primarily "undecorated" but "trimmed" mannose-type asparagine-linked oligosaccharides, while the protein in WT cells contains a mixture of "decorated" and "trimmed" asparagine-linked oligosaccharides. Biosynthetic and turnover studies demonstrate that Lec1 cells, in contrast to WT cells, are unable fully to process the core asparagine-linked oligosaccharides of maturing glucose transporters. When radiolabeled in methionine-deficient medium both Lec1 and WT cells show similar rates of synthesis and turnover of glucose transporter proteins. It should be noted, however, that starvation for a critical amino acid may alter the ability of the cell to synthesize or degrade proteins. The abilities of Lec1 and WT cells to transport hexoses and to interact with the inhibitor cytochalasin B are very similar. The results indicate that, although altered asparagine-linked glycosylation can affect the content and biogenesis of glucose transporters, these changes do not greatly modify cellular hexose uptake. The possibility that alterations in asparagine-linked glycosylation may change the cell surface localization or acquisition of a "functional conformation" of the glucose transporter is also suggested.

Animals↗
PubMed1990

Regulation of hexose transport in L8 myocytes by glucose: possible sites of interaction.

Previous work demonstrated that glucose controls its own transport rate in rat skeletal muscle: exposure to high glucose levels down-regulates muscle hexose transport, while glucose withdrawal results in elevated transport rates (J. Biol. Chem. 261:16827-16833, 1986). The present study investigates the mechanism of this autoregulatory system. Preincubation of L8 myocytes at 16 mM glucose reduced subsequent 2-deoxy-D-glucose (dGlc) uptake by 40% within 3 h. Cycloheximide (1 microM) mimicked the action of glucose; the effects of glucose and cycloheximide were not additive. At 50 microM, cycloheximide prevented the modulations of glucose transport induced by exposure of muscle cells to high or low glucose concentrations. Inhibition of glycosylation with tunicamycin A1 reduced the basal dGlc uptake, but did not prevent its up-regulation following glucose withdrawal. Inhibition of RNA synthesis by actinomycin D prevented the down-regulatory effect of glucose. These results indicate that continuous protein synthesis and protein glycosylation are required for the maintenance of the steady-state dGlc uptake. We suggest that glucose exerts its autoregulatory effect on hexose transport by modifying the incorporation of active glucose transporters into the plasma membrane rather than changing their rate of degradation. It is hypothesized that this effect is mediated by a non-glycosylated protein involved in the translocation or activation of glucose transporters.

Animals↗
PubMed2006

Hexose transporters GLUT1 and GLUT3 are colocalized with hexokinase I in caveolae microdomains of rat spermatogenic cells.

Postmeiotic spermatogenic cells, but not meiotic spermatogenic cells respond differentially with glucose-induced changes in [Ca2+]i indicating a differential transport of glucose via facilitative hexose transporters (GLUTs) specifically distributed in the plasma membrane. Several studies have indicated that plasma membrane in mammalian cells is not homogeneously organized, but contains specific microdomains known as detergent-resistant membrane domains (DRMDs), lipid rafts or caveolae. The association of these domains and GLUTs isoforms has not been characterized in spermatogenic cells. We analyzed the expression and function of GLUT1 and GLUT3 in isolated spermatocytes and spermatids. The results showed that spermatogenic cells express both glucose transporters, with spermatids exhibiting a higher affinity glucose transport system. In addition, spermatogenic cells express caveolin-1, and glucose transporters colocalize with caveolin-1 in caveolin-enriched membrane fractions. Experiments in which the integrity of caveolae was disrupted by pretreatment with methyl-beta-cyclodextrin, indicated that the involvement of cholesterol-enriched plasma membrane microdomains were involved in the localization of GLUTs and uptake of 2-deoxyglucose. We also observed cofractionation of GLUT3 and caveolin-1 in low-buoyant density membranes together with their shift to higher densities after methyl-beta-cyclodextrin treatment. GLUT1 was found in all fractions isolated. Immunofluorescent studies indicated that caveolin-1, GLUT1, and hexokinase I colocalize in spermatocytes while caveolin-1, GLUT3, and hexokinase I colocalize in spermatids. These findings suggest the presence of hexose transporters in DRMDs, and further support a role for intact caveolae or cholesterol-enriched membrane microdomains in relation to glucose uptake and glucose phosphorylation. The results would also explain the different glucose-induced changes in [Ca2+]i in both cells.

3-O-Methylglucose↗
PubMed1981

A comparison of the toxic effects of 2-deoxy-D-glucose and 2-deoxy-2-fluoro-D-hexoses on Saccharomyces cerevisiae cells and protoplasts.

The toxicity to the cells and protoplasts of Saccharomyces cerevisiae of the sugar analogues modified at carbon 2 increases in the order 2-deoxy-D-glucose (DG), 2-deoxy-2-fluoro-D-glucose (FG) and 2-deoxy-2-fluoro-D-mannose (FM). The fluorohexoses, similarly as DG, behave generally as analogues of both glucose and mannose, depending on the hexose used as a carbon source in the medium. Relative inhibitions of glucan and mannan synthesis in protoplasts were found to be dependent more on glucose and mannose used as the growth support than on the type of the sugar analogue. Certain degree of structural relationship of fluorohexoses to the corresponding natural hexoses was reflected in their effects on growth of intact cells. Growth on glucose was inhibited most effectively by FM, growth on mannose by FG. The data obtained support the view that the sugar analogues interfere mainly with the glucose-mannose interconversion catalyzed by hexosephosphateisomerases. A comparison of the effects of fluorohexoses and DG on the synthesis of extracellular invertase an intracellular alpha-glucosidase and alkaline phosphatase in protoplasts pointed to the fact that all three sugar analogues tested also participate in metabolic control of enzyme synthesis.

Cell Wall↗
PubMed2004

Characterization of the effectiveness of hexose transporters for transporting xylose during glucose and xylose co-fermentation by a recombinant Saccharomyces yeast.

We have developed recombinant Saccharomyces yeasts that can effectively co-ferment glucose and xylose to ethanol. However, these yeasts still ferment glucose more efficiently than xylose. The transport of xylose could be one of the steps limiting the fermentation of xylose. In this study, we characterized the changes in the expression pattern of the hexose transporter and related genes during co-fermentation of glucose and xylose using one of our recombinant yeasts, Saccharomyces cerevisiae 424A(LNH-ST). The transcription of the hexose transporter and related genes was strongly influenced by the presence of glucose; HXT1, HXT2 and HXT3 were greatly activated by glucose and HXT5, HXT7 and AGT1 were significantly repressed by glucose. We also examined the effectiveness of individual transporters encoded by HXT1, HXT2, HXT4, HXT5, HXT7 and GAL2 genes for transporting xylose during co-fermentation of glucose and xylose in a Saccharomyces hxt degrees mutant (RE700A). We compared these hxt degrees derivatives to RE700A wild-type strain (S. cerevisiae MC996A) where all of them contained the same xylose metabolizing genes present in our xylose-fermenting yeasts such as 424A(LNH-ST). Our results showed that recombinant RE700A containing the cloned HXT7 or HXT5 were substantially more effective for fermenting xylose to ethanol. In addition, we found that the efficiency of transporters for intracellular accumulation of xylose was as follows: HXT7 > HXT5 > GAL2 > WT > HXT1 > HXT4 > > > RE700A. Furthermore, we provided evidence that the Saccharomyces galactose transporter system could be a highly effective xylose transporter. The information reported here should be of great importance for improving the Saccharomyces yeast transport of xylose.

Fermentation↗
PubMed2002

The hexose transporters of Saccharomyces cerevisiae play different roles during enological fermentation.

We investigated the role of hexose transporters in a Saccharomyces cerevisiae strain derived from an industrial wine strain by carrying out a functional analysis of HXT genes 1-7 under enological conditions. A strain in which the sugar carrier genes HXT1-HXT7 were deleted was constructed and the HXT genes were expressed individually or in combination to evaluate their role under wine alcoholic fermentation conditions. No growth or fermentation was observed in winemaking conditions for the hxt1-7 delta strain. The low-affinity carriers Hxt1 and Hxt3 were the only carriers giving complete fermentation of sugars when expressed alone, indicating that these carriers play a predominant role in wine fermentation. However, these two carriers have different functions. The Hxt3 transporter is thought to play a major role, as it was the only carrier that gave an almost normal fermentation profile when produced alone. The hxt1 carrier was much less effective during the stationary phase and its role is thought to be restricted to the beginning of fermentation. The high-affinity carriers Hxt2, Hxt6 and/or Hxt7 were also required for normal fermentation. These high-affinity transporters have different functions: hxt2 is involved in growth initiation, whereas Hxt6 and/or Hxt7 are required at the end of alcoholic fermentation. This work shows that the successful alcoholic fermentation of wine involves at least four or five hexose carriers, playing different roles at various stages in the fermentation cycle.

Carbon Dioxide↗
PubMed1999

Differences in the time course of the metabolic response of B and non-B pancreatic islet cells to D-glucose and metabolized or non-metabolized hexose esters.

The early (min </= 1) and late (min 45) changes in NAD(P)H fluorescence caused by alpha-D-glucose pentaacetate, beta-L-glucose pentaacetate, and beta-D-galactose pentaacetate (1.7 mM each), alone or together with either L-leucine (10.0 mM) or D-glucose (8.3 mM), were monitored in purified pancreatic B and non-B rat islet cells. Whilst D-glucose caused a rapid increase in the NAD(P)H signal in B-cells, but not so in non-B cells, alpha-D-glucose pentaacetate, but not the two other monosaccharide esters, rapidly augmented the NAD(P)H signal in both B and non-B cells. After 45 min, the NAD(P)H signal was increased by either D-glucose in both B and non-B islet cells or alpha-D-glucose pentaacetate. At this late time, beta-L-glucose pentaacetate also increased the NAD(P)H signal in B cells exposed to L-leucine. These findings emphasize the relevance of differences in the time course of D-glucose uptake by B and non-B islet cells as a determinant of rapid changes in redox state. They also provide further support for the role of intracellular Ca(2+) regulating the activity of key Ca(2+)-responsive mitochondrial dehydrogenases. Last, they reinforce the view that the effects of hexose pentaacetates upon insulin and glucagon release entail a dual modality, linked either to the catabolism of their hexose moiety or to a direct effect of the esters themselves upon a stereospecific receptor system.

Animals↗
PubMed1982

Possible role of oxidized glutathione for the regulation of the myocardial hexose monophosphate shunt.

Infusion of the isolated perfused Langendorff rat heart with tert-butyl hydroperoxide (3 X 10(-4) M) resulted in a marked enhancement of the concentration of oxidized glutathione, in an increase of the NADP+/NADPH ratio, and in an elevation of the available pool of 5-phosphoribosyl-1-pyrophosphate, which is one of the end products of the hexose monophosphate shunt. Since it has been shown that oxidized glutathione overcomes the inhibition of glucose-6-phosphate dehydrogenase exerted by NADPH, these results suggest that the myocardial hexose monophosphate shunt can be stimulated rapidly and markedly through this control mechanism.

Animals↗
PubMed1984

Fatty acyl-CoAs as feedback regulators of hexose monophosphate shunt in rat adipocytes.

The high basal glucose utilization through hexose monophosphate shunt found in our experimental conditions were almost completely inhibited by oleate, octanoate and caproate. However, the inhibition of glucose oxidation due to butyrate was about 50% whereas ketone bodies and acetate did not inhibit. The rate of triacylglycerol formation was not significantly modified with the above organic acids except oleate that presented a 5-fold increase on labeling incorporation into lipids. Oleate inhibition of glucose oxidation was completely prevented by the NADPH oxidant menadione. There was no inhibition by octanoate, caproate, butyrate or ketone bodies of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase or malic enzyme in adipose tissue homogenates. In contrast, specifically glucose-6-phosphate dehydrogenase was inhibited by oleoyl-CoA. The oleoyl-CoA inhibition was prevented by enzyme preincubation with low NADP concentration. The data lend further support for the hypothesis that fatty acids and NADP fulfill an important role in the modulation of the hexose monophosphate shunt activity.

Acyl Coenzyme A↗
PubMed1978

Effect of haemolysis on the hexose monophosphate pathway in normal and in glucose-6-phosphate dehydrogenase-deficient erythrocytes.

The hexose monophosphate pathway of human glucose-6-phosphate dehydrogenase (EC 1.1.1.49) - deficient erythrocytes is under a severe and unexplained restraint (Gaetani, G.D., Parker, J.C. and Kirkman, H.N. (1974) Proc. Natl. Acad. Sci. U.S. 71, 3584-3587). In this study the hexose monophosphate pathway activity and the NADPH level of normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes were measured soon after haemolysis. The results indicate a prompt increase in 14CO2 evolution and a rise in MADPH levels. Since, in this study, the concentration of the haemolysate is comparable to that of intact erythrocytes, the relief of the restraint on glucose-6-phosphate dehydrogenase through dilution-dependent dissociation from inactivator or inhibitor is excluded. The possibility that the intracellular restraint may result from compartmentalization of glucose-6-phosphate dehydrogenase and substrates or from properties of the intact membrane of the erythrocytes is suggested.

Carbon Dioxide↗