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PubMed2006

System-wide genomic and biochemical comparisons of sialic acid biology among primates and rodents: Evidence for two modes of rapid evolution.

Numerous vertebrate genes are involved in the biology of the oligosaccharide chains attached to glycoconjugates. These genes fall into diverse groups within the conventional Gene Ontology classification. However, they should be evaluated together from functional and evolutionary perspectives in a "biochemical systems" approach, considering each monosaccharide unit's biosynthesis, activation, transport, modification, transfer, recycling, degradation, and recognition. Sialic acid (Sia) residues are monosaccharides at the outer end of glycans on the cell-surface and secreted molecules of vertebrates, mediating recognition by intrinsic or extrinsic (pathogen) receptors. The availability of multiple genome sequences allows a system-wide comparison among primates and rodents of all genes directly involved in Sia biology. Taking this approach, we present further evidence for accelerated evolution in Sia-binding domains of CD33-related Sia-recognizing Ig-like lectins. Other gene classes are more conserved, including those encoding the sialyltransferases that attach Sia residues to glycans. Despite this conservation, tissue sialylation patterns are shown to differ widely among these species, presumably because of rapid evolution of sialyltransferase expression patterns. Analyses of N- and O-glycans of erythrocyte and plasma glycopeptides from these and other mammalian taxa confirmed this phenomenon. Sia modifications on these glycopeptides also appear to be undergoing rapid evolution. This rapid evolution of the sialome presumably results from the ongoing need of organisms to evade microbial pathogens that use Sia residues as receptors. The rapid evolution of Sia-binding domains of the inhibitory CD33-related Sia-recognizing Ig-like lectins is likely to be a secondary consequence, as these inhibitory receptors presumably need to keep up with recognition of the rapidly evolving "self"-sialome.

Amino Acid Sequence↗
PubMed2006

Functional characterization of PmHS1, a Pasteurella multocida heparosan synthase.

Heparosan synthase 1 (PmHS1) from Pasteurella multocida Type D is a dual action glycosyltransferase enzyme that transfers monosaccharide units from uridine diphospho (UDP) sugar precursors to form the polysaccharide heparosan (N-acetylheparosan), which is composed of alternating (-alpha4-GlcNAc-beta1,4-GlcUA-1-) repeats. We have used molecular genetic means to remove regions nonessential for catalytic activity from the amino- and the carboxyl-terminal regions as well as characterized the functional regions involved in GlcUA-transferase activity and in GlcNAc-transferase activity. Mutation of either one of the two regions containing aspartate-X-aspartate (DXD) residue-containing motifs resulted in complete or substantial loss of heparosan polymerizing activity. However, certain mutant proteins retained only GlcUA-transferase activity while some constructs possessed only GlcNAc-transferase activity. Therefore, it appears that the PmHS1 polypeptide is composed of two types of glycosyltransferases in a single polypeptide as was found for the Pasteurella multocida Type A PmHAS, the hyaluronan synthase that makes the alternating (-beta3-GlcNAc-beta1,4-GlcUA-1-) polymer. However, there is low amino acid similarity between the PmHAS and PmHS1 enzymes, and the relative placement of the GlcUA-transferase and GlcNAc-transferase domains within the two polypeptides is reversed. Even though the monosaccharide compositions of hyaluronan and heparosan are identical, such differences in the sequences of the catalysts are expected because the PmHAS employs only inverting sugar transfer mechanisms whereas PmHS1 requires both retaining and inverting mechanisms.

Glutamine↗
PubMed2001

Glycosylated rat prolactin: isolation and structural characterization.

Isolation of glycosylated 26 kDa rat prolactin and subsequent proper carbohydrate characterization has so far not been reported. In the present work the hormone isoform was isolated to 95% homogeneity by preparative electrophoretic separation on Mini Prep Cell of rat pituitary homogenate. The isoform was then investigated by 2-mercaptoethanol gradient electrophoresis, Cleveland's sequential SDS-PAGE, digestion with endoproteinase Asp-N and N-glycanase. The glycosidic part of the isoform was examined in O-profiling and its monosaccharide composition obtained by FACE and HPAE-PAD analysis. The outcome of the experimental data is: 1) in contrast to unglycosylated 23 kDa rat prolactin, intra-chain S-S bridging is not affected in 26kDa rat prolactin, neither by transiting through a thiol gradient nor in sequential nonreducing/reducing SDS-PAGE; 2) the conformational availability of Asp residues involved in the endoproteinase Asp-N attack is the same in 23- and 26 kDa rat prolactin; the glycan moiety apparently does not cause steric hindrance at this level; 3) no glycosidic N-linkage could be detected, only O-linkage(s); 4) 26 kDa rat prolactin is no glycosyl-phosphaditylinositol-anchored protein; 5) in O-profiling an oligosaccharide chain of Mr +/- 1.4 kDa was recorded; 6) the monosaccharide composition obtained in FACE is peculiar in the sense that next to Fuc, Man, GalNac, GlcNac and NeuAc also Rib was determined; 7) HPAE-PAD analysis identified NeuAc subtypes; 8) in vitro, glycosylation of rat prolactin modulates immune recognition through steric hindrance of the access to the epitope sites.

Animals↗
PubMed2002

Effects of feed enzymes on nutritive value of soyabean meal fed to broilers.

1. The effects of two enzyme products on the nutritive value of soyabean meal (SBM) were investigated with the emphasis on changes in composition of non-starch polysaccharides (NSP) along the digestive tract. Enzyme A was a commercially available product containing mainly hemicellulase, pectinase, beta-glucanase and some protease activities and Enzyme B was an experimental product with mainly beta-galactanase activity. 2. Enzymes were added at the recommended dosage (normal) and at 5 times the recommended dosage (high) to a semi-purified diet based on maize with SBM as the sole protein source. 3. The enzymes had no effect on digesta viscosity in the jejunum or ileum. 4. Enzyme A at the high dosage significantly (P<0.05) improved AMEN, reduced excreta moisture content and improved ileal protein digestibility. The addition of the same enzyme at the recommended dosage had no effect on any of the above parameters. 5. Analysis of the monosaccharide composition revealed that Enzyme A tended to reduce the amounts of rhamnose and galactose in the soluble and insoluble NSP fractions in thejejunal and ileal digesta. The reduction was significant (P<0.05) when the same enzyme was added at the high dosage. 6. Enzyme B significantly (P<0.05) improved AMEN of the diet but not the growth or the feed conversion ratio (FCR) of the birds. Enzyme B at the high dosage significantly reduced (P<0.05) ileal protein digestibility. 7. Enzyme B significantly (P<0.05) increased the amount of free sugars in thejejunum and reduced (P<0.05) the concentration of soluble NSP in the ileum. 8. Analysis of the monosaccharide composition in the jejunal and ileal digesta showed that this enzyme was highly effective in releasing galactose from both the soluble and insoluble NSP fractions. 9. It is concluded that glycanases with galactanase and pectinase activities supplemented at appropriate dosages can improve the digestibility of the NSP in SBM and increase the metabolisable energy content of the diet containing high levels of SBM. 10. Furthermore, the addition of Enzyme B at the high dosage significantly (P<0.05) reduced protein digestibility without any measurable reduction in growth performance.

Animal Feed↗
PubMed1986

The effect of the digestion products of lactose (glucose and galactose) on its intraintestinal, in vivo hydrolysis by exogenous microbial beta-D-galactosidase.

Exogenous, microbial beta-D-galactosidases are capable of effecting hydrolysis of lactose in situ in the gastrointestinal tract of lactase-deficient subjects when given as replacement therapy at mealtime. As its digestion products-glucose and galactose-are known to inhibit lactose hydrolysis in vitro, the effect of adding excess monosaccharide to milk on the hydrolytic efficiency of a beta-galactosidase from Aspergillus niger in adult lactose-malabsorbers was tested. Subjects were studied with 360-ml volumes of milk containing 18 g of carbohydrate. This was administered as intact milk, as lactose-prehydrolyzed milk, and as milk to which 399 mg of Lactase N was added within 5 minutes of consumption. This latter Lactase N-treated milk was administered alone and with graded levels of glucose-9, 18, and 36 g-and with similar doses of galactose. The Lactase N enzyme alone at mealtime reduced breath H2 production by 68% as compared to intact milk. The addition of monosaccharides produced no change in the apparent hydrolytic efficiency of the Lactase N in situ. Thus, product inhibition is unlikely to be the basis for the limited efficiency of intraintestinal hydrolysis of milk lactose by the enzyme from A niger.

Adult↗
PubMed1986

Radiolysis of human gastric glycopolypeptides in aqueous solution.

The degradation of human gastric glycopolypeptides by hydroxyl radicals formed in irradiated N2O-saturated aqueous solution has been investigated. Gel exclusion chromatography shows the formation of lower molecular weight degradation products after irradiation and the appearance of unsaturated carbonyl-containing products which absorb in the ultra-violet. The radiation-induced destruction of individual monosaccharides in three human glycopolypeptides having different oligosaccharide chains has been measured. The results indicate that the structure of the oligosaccharide chain determines the extent of destruction of each type of monosaccharide present.

Cobalt Radioisotopes↗
PubMed2006

Cryoprotective effects of saccharides on the freeze-drying of sonicated vesicles of the novel lipid A analog, E5531.

A sonicated dispersion of the novel lipid A analog, E5531, was feeze-dried in the presence of various additives such as saccharides and polyalcohols, and their cryoprotective effects were investigated. Fusion of the vesicles was examined by measuring fluorescence energy transfer and size distribution. Cryoprotective ability differed among the addtive species. The addition of polyalcohols led to considerable fusion. Although monosaccharides, similar to disaccharides, completely prevented the fusion of the vesicles during lyophilization, they showed far less ability to retain the entrapped calcein in the vesicles compared to disaccharides. Differential scanning calorimetry heating profiles of vesicles that had been lyophilized with various additives were obtained. Disaccharides and monosaccharides again resulted in markedly different thermal properties of the vesicles. This variety in cryoprotective ability of saccharide species can be attributed to differences in their interaction with the E5531 head group.

Calorimetry, Differential Scanning↗
PubMed1953

A study of the fluid uptake of rat kidney slices in vitro.

Rat renal cortical and medullary tissues show a marked elevation of relative water content when immersed in "physiological solutions" containing sodium and chloride ions, or in equally concentrated solutions of monosaccharides. In contrast to this, no increase in relative water content occurs in isosmotic solutions of three disaccharides studied. It appears to be unlikely that the fluid uptake is a result of intracellular hypertonicity existing either physiologically or pathologically. A more satisfactory alternative hypothesis is that ingress of water accompanies entrance of solutes (ions, monosaccharide molecules) into the tissue cells.

Animals↗
PubMed1960

Tracer exchange vs. net uptake of glucose through human red cell surface. New evidence for carrier-mediated diffusion.

Previous kinetic studies of net sugar movements through the human erythrocyte surface (in response to concentration gradients) have led to postulation of a special "carrier" system for transfer of monosaccharides in these cells. But alternatively some sort of non-specific depression of cell permeability at high sugar concentrations has been suggested as a possible basis for the saturation kinetics and the competitive phenomena observed. New theoretical calculations show that these two interpretations predict entirely different orders of magnitude for the relative rate of tracer glucose exchange at such high sugar levels. Therefore, the speeds of gross chemical equilibration and of tracer glucose equilibration were compared by means of serial analyses on quickly separated cells and media, in thick red cell suspensions. Glucose was first added to glucose-free suspensions, and its entry into the cells followed; then C14-glucose was added after attainment of chemical equilibrium, and the tracer equilibration similarly followed. The speed of the tracer movement in relation to the speed of net uptake was on the order of 50 to 100 times greater than would be found in an uncomplicated diffusion process, regardless of what depressant effect might be occasioned by the high sugar levels. In contrast, the comparative rates observed are predicted by the previously proposed facilitated-diffusion mobile-carrier model for monosaccharide transfer, if the glucose-carrier complex is assigned a dissociation constant (at 20 degrees C.) in the neighborhood of 1 mM.

Biological Transport↗
PubMed2006

Vancomycin-resistant Enterococci may obtain nutritional support by scavenging carbohydrate fragments generated during mucin degradation by the anaerobic microbiota of the colon.

Vancomycin-resistant Enterococcus (VRE) is an important nosocomial pathogen that colonizes the intestinal tract. The substrates that provide nutritional support for VRE in the colon are not known. We tested the hypothesis that enzymatic breakdown of complex polysaccharides and glycoconjugates by other members of the indigenous microbiota could provide a source of nutrients for VRE. Nine vancomycin-resistant E. faecium strains were unable to ferment complex plant polysaccharides or hog gastric or bovine submaxillary mucin; however, each of the strains was able to ferment monosaccharides that are components of mucins and plant polysaccharides. Preincubation of hog gastric mucin with partially purified enzyme mixtures obtained from supernatants of Ruminococcus torques or a human stool specimen resulted in release of monosaccharides that supported growth of VRE. These results suggest that enzymatic breakdown of complex polysaccharides such as mucin by members of the indigenous microbiota may provide a source of nutritional support for VRE.

Bacteroides↗
PubMed1978

The effect of chain length on glucose absorption and the related metabolic response.

The relative absorption of saccharides on different chain length has been reexamined. Whether glucose is administered as a monosaccharide, a disaccharide (maltose), an intermediate polysaccharide mixture with a mean chain length of five glucose units (Caloreen), or a polysaccharide (starch), the rate of rise and fall in blood glucose concentration is similar in healthy subjects. In a maturity onset diabetic, peak blood glucose is similar whether monosaccharide or Caloreen is ingested. Plasma insulin and plasma free fatty acid responses to glucose saccharide ingestion do not appear to be affected by chain length. The dietary form in which starch is administered, rather than chain length, is probably important.

Absorption↗
PubMed1993

Fructose absorption.

Fructose found in modern diets as a constituent of the disaccharide sucrose is absorbed by a well-characterized absorptive system integrating enzymatic hydrolysis of the disaccharide and transfer of the resulting two monosaccharides through the apical membrane of the epithelial cell. The increasing use of high-fructose syrups and crystalline fructose prompted new studies aimed at the determination of the absorptive capacity for free fructose in the human gut. Results indicate that the capacity for fructose absorption is small compared with that for sucrose and glucose and is much less than previously estimated. The unexpected finding that the simultaneous ingestion of glucose can prevent fructose malabsorption suggests that the pair of monosaccharides might be absorbed by the disaccharidase-related transport system as if they were the product of the enzymatic hydrolysis of sucrose. This absorptive mechanism might not be able to transport fructose when ingested without glucose.

Animals↗
PubMed2002

Selective growth of mucolytic bacteria including Clostridium perfringens in a neonatal piglet model of total parenteral nutrition.

BACKGROUND: Compromised barrier function and intestinal inflammation are common complications of total parenteral nutrition (TPN). OBJECTIVE: We tested the hypothesis that the lack of enteral nutrients in TPN might select commensal or pathogenic bacteria that use mucus as a substrate, thereby weakening the protection provided by the intestinal mucus layer. DESIGN: Ileal microbiota profiles of piglets fed by total enteral nutrition (TEN; n = 6) or TPN (n = 5) were compared with the use of 16S ribosomal DNA polymerase chain reaction (PCR)-denaturing gradient gel electrophoresis and with a PCR-based method developed to specifically measure Clostridium perfringens concentrations. Ileal bacteria from TEN and TPN piglets were also examined for their ability to grow on mucin or sulfated monosaccharides. RESULTS: Bacterial community structure was equally complex in the ileum of TEN and TPN piglets, but profiles clustered according to mode of nutrition. Sixty-two percent of total mucus-associated bacteria (100 colonies tested) in TPN compared with 33% of mucus-associated bacteria (100 colonies tested) in TEN ileal samples grew on mucin. Bacteria capable of using sulfated monosaccharides were also enriched in TPN samples. C. perfringens, an opportunistic pathogen, was specifically enriched in the TPN ileum (P < 0.05). These results were corroborated by cultivation-based studies that showed rapid growth of C. perfringens on mucin-based substrates. CONCLUSIONS: Mucolytic potential is widespread among intestinal bacteria. Mucolytic bacteria in general and C. perfringens in particular were selected when enteral nutrients were withheld in this TPN piglet model. Similar enrichment processes may occur in humans nourished by TPN and may thereby contribute to intestinal dysfunction.

Animals↗
PubMed2006

ProfilePSTMM: capturing tree-structure motifs in carbohydrate sugar chains.

MOTIVATION: Carbohydrate sugar chains, or glycans, are considered the third major class of biomolecules after DNA and proteins. They consist of branching monosaccharides, starting from a single monosaccharide. They are extremely vital to the development and functioning of multicellular organisms because they are recognized by various proteins to allow them to perform specific functions. Our motivation is to study this recognition mechanism using informatics techniques from the data available. Previously, we introduced a probabilistic sibling-dependent tree Markov model (PSTMM), which we showed could be efficiently trained on sibling-dependent tree structures and return the most likely state paths. However, it had some limitations in that the extra dependency between siblings caused overfitting problems. The retrieval of the patterns from the trained model also involved manually extracting the patterns from the most likely state paths. Thus we introduce a profilePSTMM model which avoids these problems, incorporating a novel concept of different types of state transitions to handle parent-child and sibling dependencies differently. RESULTS: Our new algorithms are more efficient and able to extract the patterns more easily. We tested the profilePSTMM model on both synthetic (controlled) data as well as glycan data from the KEGG GLYCAN database. Additionally, we tested it on glycans which are known to be recognized and bound to proteins at various binding affinities, and we show that our results correlate with results published in the literature.

Algorithms↗
PubMed2001

Responses of the ant Lasius niger to various compounds perceived as sweet in humans: a structure-activity relationship study.

A behavioural study on the ant Lasius niger was performed by observing its feeding responses to 85 compounds presented in a two-choice situation (tested compound versus water control or sucrose solution). Among these compounds, only 21 were phagostimulating: six monosaccharides (D-glucose, 6-deoxy-D-glucose, L-galactose, L-fucose, D-fructose, L-sorbose), four derivatives of D-glucose (methyl alpha-D-glucoside, D-gluconolactone and 6-chloro- and 6-fluoro-deoxy-D-glucose), five disaccharides (sucrose, maltose, palatinose, turanose and isomaltose), one polyol glycoside (maltitol), three trisaccharides (melezitose, raffinose and maltotriose) and two polyols (sorbitol and L-iditol). None of the 16 non-carbohydrate non-polyol compounds tested, although perceived as sweet in humans, was found to be active in ants. The molar order of effectiveness of the major naturally occuring compounds (melezitose > sucrose = raffinose > D-glucose > D-fructose = maltose = sorbitol) is basically different from the molar order of their sweetness potency in humans (sucrose > D-fructose > melezitose > maltose > D-glucose = raffinose = sorbitol). On a molar basis melezitose is in L. niger about twice as effective as sucrose or raffinose, while D-glucose and D-fructose are three and four times less effective, respectively, than sucrose or raffinose. From a structure-activity relationship study it was inferred that the active monosaccharides and polyols should interact with the ant receptor through only one type of receptor, through the same binding pocket and the same binding residues, via a six-point interaction. The high effectiveness of melezitose in L. niger mirrors the feeding habits of these ants, which attend homopterans and are heavy feeders on their honeydew, which is very rich in this carbohydrate.

Animals↗
PubMedDate not supplied

Immunochemistry of Pseudomonas aeruginosa lipopolysaccharides and high-molecular-weight polysaccharides.

A comparison was made of the immunochemical properties of high-molecular-weight polysaccharide (PS) and lipopolysaccharides (LPS) from Pseudomonas aeruginosa immunotype 1 and 2 (IT-1 and IT-2) strains. High-molecular-weight PS was found to be an immunogenic, nontoxic form of the LPS serotype determinant found on the O side chain of the LPS. PS and O side chains were serologically identical. Immunization of animals with either whole bacterial cells or purified PS or LPS resulted in comparable levels of antibody directed at PS or O side chains. Chemical analysis of PS and LPS indicated the presence of monosaccharides in PS preparations that are not present in LPS, while PS and LPS share other monosaccharides. PS also lacks core-type sugars found in LPS such as 2-keto-3-deoxyoctulosonic acid, heptose, and glucosamine. PS from IT-1 P. aeruginosa is immunogenic in humans, with essentially no toxicity noted.

Adult↗
PubMed2002

Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds.

Formation of the sugar-amino acid linkage is a crucial event in the biosynthesis of the carbohydrate units of glycoproteins. It sets into motion a complex series of posttranslational enzymatic steps that lead to the formation of a host of protein-bound oligosaccharides with diverse biological functions. These reactions occur throughout the entire phylogenetic spectrum, ranging from archaea and eubacteria to eukaryotes. It is the aim of this review to describe the glycopeptide linkages that have been found to date and specify their presence on well-characterized glycoproteins. A survey is also made of the enzymes involved in the formation of the various glycopeptide bonds as well as the site of their intracellular action and their affinity for particular peptide domains is evaluated. This examination indicates that 13 different monosaccharides and 8 amino acids are involved in glycoprotein linkages leading to a total of at least 41 bonds, if the anomeric configurations, the phosphoglycosyl linkages, as well as the GPI (glycophosphatidylinositol) phosphoethanolamine bridge are also considered. These bonds represent the products of N- and O-glycosylation, C-mannosylation, phosphoglycation, and glypiation. Currently at least 16 enzymes involved in their formation have been identified and in many cases cloned. Their intracellular site of action varies and includes the endoplasmic reticulum, Golgi apparatus, cytosol, and nucleus. With the exception of the Asn-linked carbohydrate and the GPI anchor, which are transferred to the polypeptide en bloc, the sugar-amino acid linkages are formed by the enzymatic transfer of an activated monosaccharide directly to the protein. This review also deals briefly with glycosidases, which are involved in physiologically important cleavages of glycopeptide bonds in higher organisms, and with a number of human disease states in which defects in enzymatic transfer of saccharides to protein have been implicated.

Disease↗
PubMed1992

Homonuclear three-dimensional NMR methods for the complete assignment of proton NMR spectra of oligosaccharides--application to Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3Gal beta 1-4Glc.

Two new homonuclear three-dimensional NMR techniques are described for the simplification of proton resonance assignment in oligosaccharides, namely HOHAHA-COSY and ROESY-COSY. The former technique is of value in the resonance assignment of gluco-configuration monosaccharide residues, whereas the latter is more suited to resonance assignment of galacto-configuration monosaccharide residues. The value of these techniques is illustrated by application to the proton resonance assignment of the pentasaccharide Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3 Gal beta 1-4Glc, a compound which exhibits a variety of assignment problems due to severe cross-peak overlap in conventional COSY or HOHAHA spectra.

Carbohydrate Conformation↗