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PubMed1995

Regulation of GLUT5 gene expression in rat intestinal mucosa: regional distribution, circadian rhythm, perinatal development and effect of diabetes.

1. GLUT5 gene expression was studied in small intestine under a variety of conditions characterized by altered intestinal absorption of monosaccharides. 2. RNA-blotting studies showed that GLUT5 mRNA was abundantly expressed in rat and rabbit intestine and kidney, but it was not detected in heart or brown adipose tissue. GLUT5 mRNA levels were higher in the upper segments of the small intestine (duodenum and proximal jejunum) than in the lower segments (distal jejunum and ileum). 3. The intestinal expression of GLUT5 mRNA in rat proximal jejunum showed circadian rhythm. A 12-fold increase in GLUT5 mRNA levels was detected at the end of the light cycle and at the beginning of the dark cycle when compared with the early light period. In keeping with this, GLUT5 protein content in brush-border membranes was also increased at the beginning of the dark cycle compared with that in the light period. 4. In streptozotocin-induced diabetes an 80% increase in GLUT5 mRNA levels in mucosa from the proximal jejunum was detected under conditions in which enhanced intestinal absorption of monosaccharides has been reported. 5. The intestinal expression of GLUT5 mRNA showed regulation during perinatal development. Levels of GLUT5 mRNA were low during fetal life, increased progressively during the postnatal period and reached levels comparable with the adult state after weaning. Weaning on to a high-fat diet partially prevented the induction of GLUT5 gene expression. 6. Our results indicate that GLUT5 gene expression is tightly regulated in small intestine. Regulation involves maximal expression in the upper part of the small intestine, circadian rhythm, developmental regulation dependent on the fat and carbohydrate content in the diet at weaning and enhanced expression in streptozotocin-induced diabetes. Furthermore, changes observed in intestinal GLUT5 expression correlate with reported alterations in intestinal absorption of fructose. This suggests a regulatory role for GLUT5 in fructose uptake by absorptive enterocytes.

Animals↗
PubMed2005

Expression of sweet taste receptors of the T1R family in the intestinal tract and enteroendocrine cells.

The composition of the intestinal luminal content varies considerably with diet. It is important therefore that the intestinal epithelium senses and responds to these significant changes and regulates its functions accordingly. Although it is becoming evident that the gut epithelium senses and responds to luminal nutrients, little is known about the nature of the nutrient sensing molecule and the downstream cellular events. A prototype example is the modulation in the capacity of the gut to absorb monosaccharides via the intestinal luminal membrane Na(+)/glucose cotransporter, SGLT1. The experimental evidence suggests that luminal sugar is sensed by a glucose sensor residing on the luminal membrane of the gut epithelium and linked to a G-protein-coupled receptor, cAMP/PKA (protein kinase A) pathway, resulting ultimately in modulation of intestinal monosaccharide absorption. Here we report the expression, at mRNA and protein levels, of members of the T1R sweet taste receptors, and the alpha-subunit of the G-protein gustducin, in the small intestine and the enteroendocrine cell line, STC-1. In the small intestine, there is a highly coordinated expression of sweet taste receptors and gustducin, a G-protein implicated in intracellular taste signal transduction, throughout the gut. The potential involvement of these receptors in sugar sensing in the intestine will facilitate our understanding of intestinal nutrient sensing, with implications for better nutrition and health maintenance.

Animals↗
PubMed1993

A sink-specific H+/monosaccharide co-transporter from Nicotiana tabacum: cloning and heterologous expression in baker's yeast.

A cDNA clone for a monosaccharide transporter (MST1) was isolated from tobacco, which is most strongly expressed in the various sink tissues of mature tobacco plants: roots, flowers, and young leaves. An open reading frame of 1569 bp codes for a protein with 523 amino acids and a calculated molecular weight of 57,717 Da. The protein is homologous to a group of other plant monosaccharide transport proteins from Arabidopsis thaliana and Chlorella kessleri, to human glucose transporters and to Saccharomyces cerevisiae and several bacterial sugar transport proteins. As with these other transporters, the MST1 protein is extremely lipophilic and has 12-putative membrane-spanning domains. Heterologous expression of the MST1 cDNA clone in Saccharomyces cerevisiae allowed its characterization as a putative H+/monosaccharide co-transporter, catalyzing the uptake of hexoses (e.g. D-glucose and D-galactose) or pentoses (e.g. D-xylose) and the energy dependent and uncoupler sensitive accumulation of non-metabolizable substrates (e.g. D-xylose or 3-O-methyl-glucose). Polyclonal antibodies were raised against a fusion protein of beta-galactosidase and the last 27 amino acids of the C-terminus of the MST1 protein. In SDS extracts of transformed yeast cells these antibodies recognize a polypeptide with an apparent molecular weight of 42 kDa, which is absent in extracts from untransformed control cells.

Amino Acid Sequence↗
PubMed2000

Structure/thermodynamics relationships of lectin-saccharide complexes: the Erythrina corallodendron case.

Molecular dynamics (MD) simulations of Erythrina corallodendron lectin binding to a monosaccharide, alpha-galactose, and a disaccharide, N-acetyl lactosamine, have been performed in order to investigate the relationship between structure and thermodynamics. A simulated annealing protocol has been used to generate ensembles of structures for the two complexes, from which both qualitative and quantitative information on binding dynamics have been extracted. The ensembled averaged lectin-saccharide interaction enthalpy is equivalent for both sugars, whereas the calculation based on the X-ray structures does show a difference. Within large statistical errors, the calculated 'binding enthalpy' is also the same for the two systems. These errors arise largely from terms involving solvent and are a typical limitation of current MD simulations. Significant qualitative differences in binding between the two complexes are, however, observed over the ensembles. These could be important for unraveling the structure/thermodynamic relationship. Stated simply, there are a greater number of binding options available to the disaccharide compared to the monosaccharide. The implications of alternative binding states on thermodynamic parameters and the 'breaking of enthalpy-entropy compensation' are discussed. The role of solvent in lectin-saccharide complex formation is suggested to be significant.

Amino Sugars↗
PubMed2000

Na(+)-dependent transport of D-xylose by bovine intestinal brush border membrane vesicles (BBMV) is inhibited by various pentoses and hexoses.

To detect whether pentoses and hexoses occurring in rumen bacteria or in hemicellulose ingested with feed and partly released in the small intestine have an affinity for the Na(+)-dependent glucose transporter of the bovine intestinal brush border membrane (BBM), we investigated whether these monosaccharides inhibit Na(+)-dependent transport of 14C-labelled D-xylose across the BBM using brush border membrane vesicles (BBMV) isolated from the mid-jejunum of cows. We used D-xylose as the transport substrate, because it has a low affinity for the Na(+)-dependent glucose transporter and thus its uptake into BBMV is more efficiently competitively inhibited by other sugars than that of D-glucose. D-Ribose, D-mannose and L-rhamnose occurring in rumen bacteria significantly inhibited Na(+)-dependent uptake of D-xylose into BBMV, but their inhibitory effect was less than that of D-glucose, D-xylose and phlorizin. This also applied to L-arabinose (and D-arabinose), which is, like D-xylose and D-galactose, a constituent of hemicellulose, and to 2-deoxy-D-glucose. Of all monosaccharides tested, only D-fructose did not affect Na(+)-dependent D-xylose transport. It is concluded that some pentoses and hexoses occurring in rumen bacteria (D-ribose, D-mannose and L-rhamnose) or hemicellulose (L-arabinose and D-xylose) have a low affinity for the Na(+)-dependent glucose transporter of the bovine BBM and may therefore be absorbed from the jejunum when released in the small intestine.

Animals↗
PubMed2002

Changing the lactose permease of Escherichia coli into a galactose-specific symporter.

N-ethylmaleimide (NEM) modification of a lactose permease mutant containing a single-Cys in place of Ala-122 (helix IV) abolishes active lactose transport. Moreover, lactose, melibiose, and beta,d-galactopyranosyl 1-thio-beta,D-galactopyranoside protect against NEM inactivation of lactose transport and/or alkylation of Cys-122 by [(14)C]NEM. Remarkably, however, D-galactose transport is relatively unaffected by NEM, and the monosaccharide affords no protection against NEM inactivation of lactose transport. Consistently, competitive inhibition of [(14)C]galactose transport by lactose, melibiose, or beta,D-galactopyranosyl 1-thio-beta,D-galactopyranoside is drastically reduced after NEM modification, whereas inhibition by unlabeled galactose is unaffected. The results indicate that alkylation of Cys-122 selectively inhibits binding and transport of disaccharides, whereas transport of the monosaccharide galactose remains largely unaffected. In addition, although the conservative mutation Ala-122 --> Ser causes only mild inhibition of lactose transport, the mutations Ala-122 --> Phe and Ala-122 --> Tyr lead to marked inhibition. In contradistinction, none of these replacements has a marked effect on galactose transport. The results demonstrate that Ala-122 is a component of the ligand-binding site and provide a strong indication that the side chain at position 122 abuts on the non-galactosyl moiety of D-galactopyranosides. This is in contrast to Cys-148, a neighboring residue in helix V, that interacts with the hydrophobic face of the galactosyl moiety of D-galactopyranosides.

Alanine↗
PubMed1995

Nonreducing end structures of chondroitin sulfate chains on aggrecan isolated from Swarm rat chondrosarcoma cultures.

Chondrocyte cultures derived from the Swarm rat chondrosarcoma were metabolically labeled with [35S]sulfate or [6-3H]GlcN. Radiolabeled aggrecan was purified from the cell layer and exhaustively digested with chondroitin ABC lyase. Digestion products were resolved into disaccharide and monosaccharide residues using Toyopearl HW40S chromatography. The separated saccharide pools were reduced with NaBH4 and applied onto a CarboPac PA1 column to resolve all of the internal disaccharide alditols (unsaturated) from the nonreducing end disaccharide (saturated) and monosaccharide alditols. Mercuric acetate treatment was used prior to carbohydrate analysis to identify unambiguously the saturated from the unsaturated disaccharides. The chondroitin sulfate (CS) chains from these aggrecan preparations contained: (a) an internal disaccharide composition of unsulfated (3-4 per chain), 4-sulfated (approximately 32 per chain), 6-sulfated (approximately 1 per 14 chains), and 4,6-sulfated disaccharides (approximately 1 per 6 chains) and (b) a nonreducing terminal composition of 4-sulfated GalNAc (approximately 4 out of every 7 chains), 4,6-disulfated GalNAc (approximately 2 out of every 7 chains), and GlcUA adjacent to a 4-sulfated GalNAc residue (approximately 1 out of every 7 chains). Thus, the vast majority of these CS chains terminated with a sulfated GalNAc residue. The presence of 4,6-disulfated GalNAc at nonreducing termini is 60-fold more abundant than 4,6-disulfated GalNAc in interior disaccharides. This observation is consistent with the suggestion that disulfation of terminal GalNAc residues is involved in chain termination.

Aggrecans↗
PubMed2000

Nitrogen monoxide (no) and glucose: unexpected links between energy metabolism and no-mediated iron mobilization from cells.

Nitrogen monoxide (NO) affects cellular iron metabolism due to its high affinity for this metal ion. Indeed, NO has been shown to increase the mRNA binding activity of the iron-regulatory protein 1, which is a major regulator of iron homeostasis. Recently, we have shown that NO generators increase (59)Fe efflux from cells prelabeled with (59)Fe-transferrin (Wardrop, S. L., Watts, R. N., and Richardson, D. R. (2000) Biochemistry 39, 2748-2758). The mechanism involved in this process remains unknown, and in this investigation we demonstrate that it is potentiated upon adding d-glucose (d-Glc) to the reincubation medium. In d-Glc-free or d-Glc-containing media, 5.6 and 16.5% of cellular (59)Fe was released, respectively, in the presence of S-nitrosoglutathione. This difference in (59)Fe release was observed with a variety of NO generators and cell types and was not due to a change in cell viability. Kinetic studies showed that d-Glc had no effect on the rate of NO production by NO generators. Moreover, only the metabolizable monosaccharides d-Glc and d-mannose could stimulate NO-mediated (59)Fe mobilization, whereas other sugars not easily metabolized by fibroblasts had no effect. Hence, metabolism of the monosaccharides was essential to increase NO-mediated (59)Fe release. Incubation of cells with the citric acid cycle intermediates, citrate and pyruvate, did not enhance NO-mediated (59)Fe release. Significantly, preincubation with the GSH-depleting agents, l-buthionine-[S,R]-sulfoximine or diethyl maleate, prevented NO-mediated (59)Fe mobilization. This effect was reversed by incubating cells with N-acetyl-l-cysteine that reconstitutes GSH. These results indicate that GSH levels are essential for NO-mediated (59)Fe efflux. Hence, d-Glc metabolism via the hexose monophosphate shunt resulting in the generation of GSH may be essential for NO-mediated (59)Fe release. These results have important implications for intracellular signaling by NO and also NO-mediated cytotoxicity of activated macrophages that is due, in part, to iron release from tumor target cells.

Animals↗
PubMed2002

Orientation of bound ligands in mannose-binding proteins. Implications for multivalent ligand recognition.

Mannose-binding proteins (MBPs) are C-type animal lectins that recognize high mannose oligosaccharides on pathogenic cell surfaces. MBPs bind to their carbohydrate ligands by forming a series of Ca(2+) coordination and hydrogen bonds with two hydroxyl groups equivalent to the 3- and 4-OH of mannose. In this work, the determinants of the orientation of sugars bound to rat serum and liver MBPs (MBP-A and MBP-C) have been systematically investigated. The crystal structures of MBP-A soaked with monosaccharides and disaccharides and also the structure of the MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides or alpha1-6-linked mannose bind to MBP-A in one orientation, whereas alpha1-2- or alpha1-3-linked mannose binds in an orientation rotated 180 degrees around a local symmetry axis relating the 3- and 4-OH groups. In contrast, a similar set of ligands all bind to MBP-C in a single orientation. The mutation of MBP-A His(189) to its MBP-C equivalent, valine, causes Man alpha 1-3Man to bind in a mixture of orientations. These data combined with modeling indicate that the residue at this position influences the orientation of bound ligands in MBP. We propose that the control of binding orientation can influence the recognition of multivalent ligands. A lateral association of trimers in the cross-linked crystals may reflect interactions within higher oligomers of MBP-A that are stabilized by multivalent ligands.

Amino Acid Sequence↗
PubMed2004

Purification, characterization, and sugar binding specificity of an N-Glycolylneuraminic acid-specific lectin from the mushroom Chlorophyllum molybdites.

A carbohydrate-binding protein was isolated from the carpophores of the mushrooms and designated the Chlorophyllum molybdites lectin (CML) based on its origin. The molecular mass of CML was 32 kDa, and it was composed of two 16-kDa monomers with no disulfide bonds. Monosaccharide analysis indicated that 12% of the mass of CML was carbohydrate and consisted of GlcNAc:GalNAc:Gal:Man:l-Fuc in a molar ratio of 1.5:1.9: 4.4:4.8:1.0. In the hemagglutination inhibition assay, CML exhibited the strongest binding specificity toward N-glycolylneuraminic acid (NeuGc) among the monosaccharides tested, whereas NeuAc did not inhibit the hemagglutination at all. GalNAc and Mealpha-GalNAc were also inhibitory at much higher concentrations than NeuGc. Among the glycoproteins, asialobovine submaxillary mucin (BSM) and porcine stomach mucin (PSM) showed strong inhibitory effects. In surface plasmon resonance analysis, asialo-BSM and PSM exhibited the strongest binding affinity. After co-injection of CML and NeuGc or GalNAc onto the asialo-BSM- or PSM-immobilized chip, the dissociation of CML from the immobilized PSM was accelerated by NeuGc and GalNAc, but the dissociation of CML from the immobilized asialo-BSM was only promoted by GalNAc. These results and the other surface plasmon resonance experiments allowed us to conclude that the binding of asialo-BSM to CML was because of an interaction between the lectin and the GalNAc residues of asialo-BSM, and both the NeuGc and GalNAc residues were responsible for the binding of PSM to CML. The results also suggested that CML had two different carbohydrate binding domains, one specific for NeuGc and the other for GalNAc.

Agaricales↗
PubMed1976

A single column packing for the gas-liquid chromatographic separation of various biologically important compounds.

The use of a single, commercially available column packing, TabsorbR, is described for the g.l.c. separation of a large number of different compounds. The resolution of the homologous members of the following series of compounds was achieved: (1) saturated fatty acids (C1-C18), (2) normal aliphatic saturated dicarboxylic acids (C2-C14), (3) normal aliphatic saturated alcohols (C1-C24), (4) normal aliphatic saturated amines (C1-C12), (5) the common amino acids except arginine, histidine and cysteine, (6) aliphatic hydrocarbons (C10-C20) and (7) monosaccharides. It should be noted that twenty-two monosaccharides including three hexosamines and two anhydrohexoses, could be resolved as alditol acetates in a single run. In addition, galacturonic, glucuronic and iduronic acids could be separated from one another as their 1,4-lactones. The resolution achieved in these series of compounds was found to be consistent and highly reproducible. It is of further interest that certain isomers of the higher fatty acids and hydrocarbons with one double bond could also be separated from the normal and saturated compounds, respectively. The applicability of "Tabsorb" for the g.l.c. separation, although noted above to be considerably broad, is by far not yet exhausted. These procedures which form the basis for the quantitative determinations of the various compounds studied as demonstrated by analysis of glycopeptides for neutral hexoses and proteins for the amino acids, can readily be adapted to preparative methods. From the biochemical point of view "Tabsorb" is an extremely versatile column packing in that it can be used for the identification of many of the common building blocks of natural products.

Alcohols↗
PubMed2005

Automated interpretation of MS/MS spectra of oligosaccharides.

MOTIVATION: The emerging glycomics and glycoproteomics projects aim to characterize all forms of glycoproteins in different tissues and organisms. Tandem mass spectrometry (MS/MS) is the key experimental methodology for high-throughput glycan identification and characterization. Fragmentation of glycans from high energy collision-induced dissociation generates ions from glycosidic as well as internal cleavages. The cross-ring ions resulting from internal cleavages provide additional information that is important to reveal the type of linkage between monosaccharides. This information, however, is not incorporated into the current programs for analyzing glycan mass spectra. As a result, they can rarely distinguish from the mass spectra isomeric oligosaccharides, which have the same saccharide composition but different types of sequences, branches or linkages. RESULTS: In this paper, we describe a novel algorithm for glycan characterization using MS/MS. This algorithm consists of three steps. First, we develop a scoring scheme to identify potential bond linkages between monosaccharides, based on the appearance pattern of cross-ring ions. Next, we use a dynamic programming algorithm to determine the most probable oligosaccharide structures from the mass spectrum. Finally, we re-evaluate these oligosaccharide structures, taking into account the double fragmentation ions. We also show the preliminary results of testing our algorithm on several MS/MS spectra of oligosaccharides. AVAILABILITY: The program GLYCH is available upon request from the authors.

Algorithms↗
PubMed1995

Abnormal synthesis of dolichol-linked oligosaccharides in carbohydrate-deficient glycoprotein syndrome.

Carbohydrate-deficient glycoprotein syndrome (CDGS) is a rare metabolic disorder presenting in infancy with severe neurologic involvement and variable multisystemic abnormalities. Diagnosis relies upon the detection of abnormal serum glycoprotein isoforms on isoelectric focusing (IEF) gels. Carbohydrate structural analyses were performed on the N-linked oligosaccharides of serum alpha 1-antitrypsin (alpha-1AT) from two Danish children with classical type I CDGS. Following preparative gel electrophoresis of alpha-1AT isoforms, oligosaccharide charge and monosaccharide composition analyses revealed increased glycosylation heterogeneity in CDGS compared with normal alpha-1AT. CDGS alpha-1AT isoforms bore N-glycans co-migrating with monosialylated standards, while normal alpha-1AT oligosaccharides co-migrated with both mono- and disialylated standards. While the monosaccharide contents of normal alpha-1AT isoforms were relatively uniform, those of CDGS alpha-1AT isoforms varied widely, and many were relatively mannose enriched. The mannose-rich oligosaccharides of CDGS alpha-1AT were not typical oligomannose structures since they were not released by endo-beta-N-acetylglucosaminidase H (endo H) digestion. Metabolic labelling of CDGS fibroblasts with [3H]mannose showed lower than normal intracellular total mannose, free mannose and phosphorylated mannose species, as well as diminished [3H]mannose incorporation into dolichol-linked and protein-linked oligosaccharides. In addition, the glycans liberated from CDGS dolichol-linked oligosaccharides were significantly truncated compared with those from normal fibroblasts. These data suggest that our type I CDGS patients produce abnormal N-linked oligosaccharides due to impaired biosynthesis of dolichol-oligosaccharide precursors.

Congenital Disorders of Glycosylation↗
PubMed1998

Concanavalin A distorts the beta-GlcNAc-(1-->2)-Man linkage of beta-GlcNAc-(1-->2)-alpha-Man-(1-->3)-[beta-GlcNAc-(1-->2)-alpha-Man- (1-->6)]-Man upon binding.

Carbohydrate recognition by proteins is a key event in many biological processes. Concanavalin A is known to specifically recognize the pentasaccharide core (beta-GlcNAc-(1-->2)-alpha- Man-(1-->3)-[beta-GlcNAc-(1-->2)-alpha-Man-(1-->6)]-Man) of N-linked oligosaccharides with a Ka of 1.41 x 10(6 )M-1. We have determined the structure of concanavalin A bound to beta-GlcNAc-(1-->2)-alpha-Man-(1-->3)-[beta-GlcNAc-(1-->2)-alpha-Man- (1-->6)]-Man to 2.7A. In six of eight subunits there is clear density for all five sugar residues and a well ordered binding site. The pentasaccharide adopts the same conformation in all eight subunits. The binding site is a continuous extended cleft on the surface of the protein. Van der Waals interactions and hydrogen bonds anchor the carbohydrate to the protein. Both GlcNAc residues contact the protein. The GlcNAc on the 1-->6 arm of the pentasaccharide makes particularly extensive contacts and including two hydrogen bonds. The binding site of the 1-->3 arm GlcNAc is much less extensive. Oligosaccharide recognition by Con A occurs through specific protein carbohydrate interactions and does not require recruitment of adventitious water molecules. The beta-GlcNAc-(1-->2)-Man glycosidic linkage PSI torsion angle on the 1-->6 arm is rotated by over 50 degrees from that observed in solution. This rotation is coupled to disruption of interactions at the monosaccharide site. We suggest destabilization of the monosaccharide site and the conformational strain reduces the free energy liberated by additional interactions at the 1-->6 arm GlcNAc site.

Animals↗
PubMed2003

Molecular characterization of the rat Kupffer cell glycoprotein receptor.

The Kupffer cell receptor for glycoproteins has been reported to have a role in clearance of galactose- and fucose-terminated glycoproteins from circulation. Although the gene and a cDNA encoding the receptor have been described, there has been little study of the receptor protein. To address some questions about possible ligands and functions for this receptor, fragments representing portions of the extracellular domain have been expressed and characterized. The extracellular domain consists of a trimer stabilized by an extended coiled-coil of alpha-helices. The receptor displays monosaccharide-binding characteristics similar to the hepatic asialoglycoprotein receptor, but with somewhat less selectivity. The two best monosaccharide ligands are GalNAc and galactose. alpha-Methyl fucoside is a particularly poor ligand. Analysis of Kupffer cell receptor binding to glycoproteins and oligosaccharides released from them reveals highest affinity for desialylated, complex N-linked glycans. The best glycoprotein ligands contain multiple highly branched oligosaccharides. A human ortholog of the rat receptor gene does not encode a full-length protein and is not expressed in liver. These characteristics suggest that the receptor may have functions parallel to those of the hepatocyte asialoglycoprotein receptor in some (but not all) mammalian species.

Amino Acid Sequence↗
PubMed1986

Intake and gastric emptying of mono- versus disaccharides by rats.

Eating and gastric emptying of mono- versus disaccharides were measured in rats which consumed each day a carbohydrate solution and, 5 h later, a restricted amount of a nutritionally adequate dry diet. When Wistar rats were offered 30% (wt/vol) sugar solutions for 60 min a day, energy intakes were smaller for glucose than for maltose or dextrin and smaller for invert sugar (fructose + glucose) than for sucrose. Sprague-Dawley rats consumed less energy from glucose than maltose when fed 60%, but not 15%, solutions of these sugars. Among Wistar rats accustomed to hypotonic carbohydrate meals, gastric emptying (kilocalories/minute) was slower for 30% glucose than 30% maltose and for 63% maltose than 21% maltose. These differences became obscured with continued exposure to highly hypertonic meals. Monosaccharides, being small, highly soluble molecules, can impart great osmolality to stomach contents. It appears that this osmotic property of monosaccharides tends to slow eating and gastric emptying.

Animals↗
PubMed1988

Short-chain fatty acid production from mono- and disaccharides in a fecal incubation system: implications for colonic fermentation of dietary fiber in humans.

An in vitro fecal incubation system was used to demonstrate how lactose, lactulose and monosaccharides (mainly constituents of dietary fiber) influence short-chain fatty acid production in colon. Short-chain fatty acids were formed from all mono- and disaccharides tested (except L-glucose): D-glucose, D-galactose, D-fructose, D-mannose, L-rhamnose, D-sorbitol, D-arabinose, D-xylose, D-ribose, D-galacturonate, D-glucuronate, lactose and lactulose. All saccharides increased acetate formation; propionate production was increased from rhamnose, arabinose, xylose, ribose, galacturonic and glucuronic acid, whereas the synthesis of butyrate was elevated in assays incubated with sorbitol, galacturonic and glucuronic acid, and to a lesser degree ribose. Isobutyrate, valerate, isovalerate and hexanoate were produced in increased amounts in assays incubated with albumin, but in fact decreased in many incubations with saccharides. It is speculated that saccharide fermentation always results in formation of acetate, and that the relative production of acetate, propionate and butyrate is related to the monosaccharide composition of dietary fiber available for colonic bacteria. However, the production of isobutyrate, valerate, isovalerate and hexanoate is probably not due to saccharide fermentation, but is rather of polypeptide origin.

Acetates↗
PubMed2004

Analysis of the participation of N-acetylglucosamine in the different steps of sperm-zona pellucida interaction in hamster.

Glycoproteins and lectin-like proteins mediate sperm-zona pellucida interaction. The present study analysed the participation of carbohydrates in the different stages of sperm interaction with the zona pellucida in hamster, by determining the effects of different monosaccharides. N-acetylglucosamine (GlcNAc, 1 mM) reduced sperm ability to bind to the zona pellucida. Surprisingly, spontaneous acrosome reaction (AR) was also inhibited by this sugar. In order to analyse the effect of GlcNAc on sperm-zona pellucida binding, independent of its effect on the AR, strontium (Sr) was used as a calcium (Ca) replacement in the sperm capacitation and co-incubation medium. Sr seemed to be able to replace Ca for sperm capacitation, at least when measured as the ability to bind to the zona pellucida, and undergo AR when Ca is provided. Moreover, sperm-zona pellucida binding could also take place in a Sr-modified medium. When binding assays were carried out in the Sr medium, GlcNAc also produced an inhibitory effect. This could be reproduced when sperm, but not oocytes, were pre-incubated with the monosaccharide. IVF assays were also carried out to analyse the participation of GlcNAc in the different steps of sperm-oocyte interaction. Taken together, the results support the involvement of the GlcNAc residues of the zona pellucida in the early steps of the interaction with sperm.

Acetylglucosamine↗