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PubMed2000

Microanalysis of enzyme digests of hyaluronan and chondroitin/dermatan sulfate by fluorophore-assisted carbohydrate electrophoresis (FACE).

Hyaluronan and chondroitin/dermatan sulfate are glycosaminoglycans that play major roles in the biomechanical properties of a wide variety of tissues, including cartilage. A chondroitin/dermatan sulfate chain can be divided into three regions: (1) a single linkage region oligosaccharide, through which the chain is attached to its proteoglycan core protein, (2) numerous internal repeat disaccharides, which comprise the bulk of the chain, and (3) a single nonreducing terminal saccharide structure. Each of these regions of a chondroitin/dermatan sulfate chain has its own level of microheterogeneity of structure, which varies with proteoglycan class, tissue source, species, and pathology. We have developed rapid, simple, and sensitive protocols for detection, characterization and quantitation of the saccharide structures from the internal disaccharide and nonreducing terminal regions of hyaluronan and chondroitin/dermatan sulfate chains. These protocols rely on the generation of saccharide structures with free reducing groups by specific enzymatic treatments (hyaluronidase/chondroitinase) which are then quantitatively tagged though their free reducing groups with the fluorescent reporter, 2-aminoacridone. These saccharide structures are further characterized by modification through additional enzymatic (sulfatase) or chemical (mercuric ion) treatments. After separation by fluorophore-assisted carbohydrate electrophoresis, the relative fluorescence in each band is quantitated with a cooled, charge-coupled device camera for analysis. Specifically, the digestion products identified are (1) unsaturated internal Deltadisaccharides including DeltaDiHA, DeltaDi0S, DeltaDi2S, DeltaDi4S, DeltaDi6S, DeltaDi2,4S, DeltaDi2,6S, DeltaDi4,6S, and DeltaDi2,4,6S; (2) saturated nonreducing terminal disaccharides including DiHA, Di0S, Di4S and Di6S; and (3) nonreducing terminal hexosamines including glcNAc, galNAc, 4S-galNAc, 6S-galNAc, and 4, 6S-galNAc.

Acetylgalactosamine↗

PubMed2002

Microbial glycosaminoglycan glycosyltransferases.

Glycosaminoglycans, a class of linear polysaccharides composed of repeating disaccharide units containing a hexosamine, are important carbohydrates found in many organisms. Vertebrates utilize glycosaminoglycans in structural, recognition, adhesion, and signaling roles. Certain pathogenic bacteria produce extracellular capsules composed of glycosaminoglycans or glycosaminoglycan-like polymers that enhance the microbes' ability to infect or to colonize the host. In the period from 1993 to 2001, bacterial enzymes were discovered that catalyze the polymerization of the repeating unit of hyaluronan, chondroitin, or N-acetylheparosan (unsulfated, unepimerized heparin). Depending on the specific carbohydrate and the microorganism, either a dual-action enzyme (synthase) that transfers two distinct monosaccharides or a pair of single-action transferases are utilized to synthesize the glycosaminoglycan polymer. Current views on the enzymology, structures, potential evolution, and the roles of the known glycosyltransferases from Streptococcus, Pasteurella, and Escherichia are discussed.

Bacteria↗

PubMed1992

A new method for sequence analysis of glycosaminoglycans from heavily substituted proteoglycans reveals non-random positioning of 4- and 6-O-sulphated N-acetylgalactosamine in aggrecan-derived chondroitin sulphate.

We have developed a new procedure for the sequence analysis of glycosaminoglycans, which is particularly suitable for the analysis of chains from heavily substituted proteoglycans. The procedure has been applied to various aggrecan-derived chondroitin sulphates. The glycans are released from the core protein by alkaline scission of the xylose-serine bond, subjected to reductive amination using p-aminobenzoic acid and finally radioiodinated at an acidic pH. Sequence analysis is performed by using various enzymic degradations, partial or complete, followed by high-resolution polyacrylamide gel electrophoresis, blotting and autoradiography to identify segments extending from the labelled reducing end to the point of cleavage. By using chondroitin C lyase to identify the location of 6-O-sulphated hexosamines, we find that chondroitin sulphate from tracheal cartilage has its 6-O-sulphated repeats concentrated to the extreme non-reducing terminal portion of the chain. In chondroitin sulphates derived from intervertebral discs (nucleus pulposus), the 6-O-sulphated repeats have a biphasic distribution; they occur mostly near the linkage region (i.e. the reducing end), but also in the non-reducing portion of the chain. Chondroitin sulphate from nasal cartilage, which is mostly 4-O-sulphated, displays considerable heterogeneity in the linkage region. Three or possibly more charge variants are observed.

4-Aminobenzoic Acid↗

PubMed1999

Gas-liquid chromatography of the heptafluorobutyrate derivatives of the O-methyl-glycosides on capillary columns: a method for the quantitative determination of the monosaccharide composition of glycoproteins and glycolipids.

We have developed a method involving the formation of hepta-fluorobutyrate derivatives of O-methyl-glycosides liberated from glycoproteins and glycolipids following methanolysis. The stable derivatives of the most common monosaccharides of these glycoconjugates (Ara, Rha, Xyl, Fuc, Gal, Man, Glc, GlcNAc, GalNAc, Neu5Ac, KDN) can be separated and quantitatively and reproducibly determined with a high degree of sensitivity level (down to 25 pmol) in the presence of lysine as an internal standard. The GlcNAc residue bound to Asn in N-glycans is quantitatively recovered as two peaks. The latter were easily distinguished from the other GlcNAc residues of N-glycans, thus allowing a considerable improvement of the data on structure of N-glycans obtained from a single carbohydrate analysis. The most common contaminants present in buffers commonly used for the isolation of soluble or membrane-bound glycoproteins (SDS, Triton X-100, DOC, TRIS, glycine, and polyacrylamide or salts, as well as monosaccharide constituents of proteoglycans or degradation products of nucleic acids) do not interfere with these determinations. A carbohydrate analysis of glycoproteins isolated from a SDS/PAGE gel or from PDVF membranes can be performed on microgram amounts without significant interferences. Since fatty acid methyl esters and sphingosine derivatives are separated from the monosaccharide peaks, the complete composition of gangliosides can be achieved in a single step starting from less than 1 microg of the initial compound purified by preparative Silicagel TLC. Using electron impact ionization mass spectrometry, reporter ions for the different classes of O-methyl-glycosides (pentoses, deoxy-hexoses, hexoses, hexosamines, uronic acids, sialic acid, and KDN) allow the identification of these compounds in very complex mixtures. The mass of each compound can be determined in the chemical ionization mode and detection of positive or negative ions. This method presents a considerable improvement compared to those using TMS derivatives. Indeed the heptafluorobutyrate derivatives are stable, and acylation of amino groups is complete. Moreover, there is no interference with contaminants and the separation between fatty acid methyl-esters and O-methyl glycosides is achieved.

Acylation↗

PubMed2003

Analysis of the two active sites of the hyaluronan synthase and the chondroitin synthase of Pasteurella multocida.

Type A Pasteurella multocida produces a hyaluronan (HA) capsule to enhance infection. The 972-residue HA synthase, pmHAS, polymerizes the linear HA polysaccharide composed of alternating beta3N-acetylglucosamine (GlcNAc)-beta4glucuronic acid (GlcUA). We demonstrated previously that pmHAS possesses two independent glycosyltransferase sites. Here we further define the sites and putative motifs. Deletion of residues 1-117 does not affect HA polymerizing activity. The carboxyl-terminal boundary of the GlcUA-transferase resides within residues 686-703. Both transferase sites contain a DXD motif essential for HA synthase activity. D247N or D249N mutants possessed only GlcUA-transferase activity, whereas D527N or D529N mutants possessed only GlcNAc-transferase activity, further confirming our assignment of the two active sites within the synthase polypeptide. A potential role of the DXD motif in substrate binding was supported by experiments utilizing high UDP-sugar concentrations that partially rescued the activity of certain mutants. The WGGED sequence motif is involved in GlcNAc-transferase activity because mutants with substitutions at E369 or D370 possessed only GlcUA-transferase activity. Type F P. multocida synthesizes an unsulfated chondroitin (beta3GalNAc-beta4GlcUA) capsule. A chimeric enzyme consisting of residues 1-427 of pmHAS and residues 421-704 of pmCS, the homologous chondroitin synthase, was an active HA synthase. The converse chimeric enzyme consisting of residues 1-420 of pmCS and residues 428-703 of pmHAS was a functional chondroitin synthase. Analyses of a panel of pmHAS/pmCS chimeric enzymes identified a 44-residue region, corresponding to pmHAS residues 225-265, involved in UDP-hexosamine selectivity. Overall, these findings further support the model of two independent transferase sites within a single polypeptide.

Amino Acid Motifs↗

PubMed2004

Involvement of gangliosides in glucosamine-induced proliferation decrease of retinal pericytes.

The hexosamine pathway (HP) is a biochemical hypothesis recently proposed explaining cellular alterations occurring during diabetic microvascular complications. Diabetic retinopathy is a common microvascular complication of diabetes, and it is known that cell proliferation is severely affected during the development of the disease. Particularly, early stages are characterized by death of the retinal microvascular cells, pericytes. Gangliosides have often been described to regulate cell growth; however, very few studies focused on the potential role of gangliosides in diabetic microvascular alterations. The aim of this article was to investigate the effect of the HP activation on pericyte proliferation and determine the potential implication of gangliosides in this process. Results indicate first that HP activation, mimicked by glucosamine treatment, decreased pericyte proliferation. Second, glucosamine treatment induced a modification of gangliosides pattern, particularly GM1 and GD3 were significantly increased. Next, results showed that exogenous addition of a-series gangliosides (GM3, GM2, GM1, GD1a) and b-series ganglioside (GD3) caused a decrease of pericyte proliferation, whereas nonsialylated precursors glucosylceramide and lactosylceramide were without effect. Furthermore, when ganglioside biosynthesis was blocked using PPMP, a glucosylceramide synthase inhibitor, the effects of glucosamine on pericyte proliferation were partially reversed. Our results suggest that in retinal pericytes, gangliosides and particularly GM1 and GD3 that are increased in response to glucosamine, are involved in the antiproliferative effect of glucosamine. These observations also underlie the potential involvement of gangliosides in a pathological context, such as diabetic microvascular complications.

Animals↗

PubMed2005

A defect in exodegradative pathways provides insight into endodegradation of heparan and dermatan sulfates.

Within cells, dermatan sulfate (DS) and heparan sulfate (HS) are degraded in two steps. The initial endohydrolysis of these polysaccharides is followed by the sequential action of lysosomal exoenzymes to reduce the resulting oligosaccharides to monosaccharides and inorganic sulfate. Mucopolysaccharidosis (MPS) type II is a lysosomal storage disorder caused by a deficiency of the exoenzyme iduronate-2-sulfatase (I2S). Consequently, partially degraded fragments of DS and HS have been shown to accumulate in the lysosomes of affected cells and are excreted in the urine. Di- to hexadecasaccharides, isolated from the urine of a MPS II patient using anion exchange and gel filtration chromatography, were identified using electrospray ionization-tandem mass spectrometry (ESI-MS/MS). These oligosaccharides were shown to have non-reducing terminal iduronate-2-sulfate residues by digestion with recombinant I2S. A pattern of growing oligosaccharide chains composed of alternating uronic acid and N-acetylhexosamine residues was identified and suggested to originate from DS. A series of oligosaccharides consisting of hexosamine/N-acetylhexosamine alternating with uronic acid residues was also identified and on the basis of the presence of unacetylated hexosamine; these oligosaccharides are proposed to derive from HS. The presence of both odd and even-length oligosaccharides suggests both endo-beta-glucuronidase and endo-N-acetylhexosaminidase activities toward both glycosaminoglycans. Furthermore, the putative HS oligosaccharide structures identified indicate that heparanase activities are directed toward regions of both low and high sulfation, while the N-acetylhexosaminidase activity acted only in regions of low sulfation in this polysaccharide.

Carbohydrate Conformation↗

PubMed1979

Lipopolysaccharide-derived serotype polysaccharides from Neisseria meningitidis group B.

Three immunologically distinct types of polysaccharides have been isolated by diethylaminoethyl (DEAE) chromatography from the lipopolysaccharide extracts of group B Neisseria meningitidis. All types contain a set of common determinants, as well as distinct ones; all of these determinants are detectable by either immunodiffusion or enzyme-linked immunosorbent assay (ELISA). The polysaccharides elute from a Sepharose 4B column in the range of 2-3 x 10(5) daltons and have isoelectric points from 4.2 to 4.3. Their antigenicity is destroyed by oxidation but is unaffected by neuraminidase, lysozyme, or trypsin. One type of polysaccharide cross-reacts with the Gc2 polysaccharide of Neisseria gonorrhoeae in immunodiffusion systems. Chemical analysis indicates that these polysaccharides contain hexoses, hexosamines, 2-keto-3-deoxyoctonate, ethanolamine, and heptose; analysis of amino acids indicates protein contents of less than 0.05%. In contrast to the lipopolysaccharide from which they are derived, these polysaccharides contain no lipid A and less than 0.5% fatty acids. All three types are precipitated by wheat germ agglutinin but not by concanavalin A or fucose-binding protein. Specific inhibition of this precipitation can be achieved with N-acetyl glucosamine. These antigens may be the bases of a lipopolysaccharide-derived typing system for group B N. meningitidis.

Animals↗

PubMed1995

Characterization of the hemagglutinin of Staphylococcus epidermidis.

Adherence to biomaterials and production of biofilm is thought to be pivotal in the pathogenesis of prosthetic device infection by Staphylococcus epidermidis. In this study a strong association (P < .001) of hemagglutination with adherence and biofilm production was observed. Hemagglutination was not associated with cell surface hydrophobicity (P = .906). Hemagglutination inhibition studies revealed that hemagglutination was not affected by heat, pH, cation concentration, proteolytic enzymes, biologic detergent, serum proteins, or subinhibitory antibiotics. Hemagglutination was abolished by periodate oxidation and digestion with glycosidases. It was markedly inhibited by beta-lactose and its monosaccharide constituents in a concentration-dependent fashion. Hemagglutinin expression depended on the presence of glucose. Chemical analysis of a partially purified hemagglutinin preparation and cell-free hemagglutinating supernatants revealed little or no protein and small quantities of reducing sugars, pentose, ketose, hexosamine, uronic acid, and phosphate. Hemagglutinin of S. epidermidis appears to be a polysaccharide distinct from other known adhesins of S. epidermidis.

Anti-Inflammatory Agents, Non-Steroidal↗

PubMed2000

Matrix polymers of Candida biofilms and their possible role in biofilm resistance to antifungal agents.

Extracellular polymeric material (EP), comprising the matrix of Candida albicans biofilms, was isolated and its composition was compared with that of EP obtained from culture supernatants of planktonically grown (suspended) organisms. Both preparations consisted of carbohydrate, protein, phosphorus and hexosamine, but biofilm EP contained significantly less total carbohydrate (41%) and protein (5%) than planktonic EP. It also had a higher proportion of glucose (16%) and contained galactose, suggesting that it might possess components unique to biofilms. To investigate whether the EP matrix plays a role in the resistance of biofilms to antifungal agents, susceptibility profiles of biofilms incubated statically (which have relatively little matrix) were compared with those for biofilms incubated with gentle shaking (which produce much more matrix material). Biofilms grown with or without shaking did not exhibit significant differences in susceptibility to any of the drugs tested, indicating that drug resistance is unrelated to the extent of matrix formation. However, biofilms formed on two different types of polyvinyl chloride catheter, obtained from different manufacturers, showed differences in susceptibility to amphotericin B, suggesting that drug resistance may arise as a result of highly specific, surface-induced gene expression.

Antifungal Agents↗

PubMed1980

A silicon requirement for normal skull formation in chicks.

Studies were undertaken to investigate the effect of feeding a silicon (Si) -deficient diet containing a natural protein in place of the crystalline amino acid-based diets used in earlier studies. Feeding this Si-deficient basal diet with or without supplemental Si to day-old cockerels under trace element-controlled conditions resulted in the production of skull abnormalities in the deficient chicks under conditions of near optimal growth. On macropathological examination, gross changes were found in the architecture of the skulls of the deficient chicks; the frontal area was narrower and the dorsal median line at the frontal parietal junction was depressed with a narrowing both posterior and laterally, forming a stunted parietal, occipital and temporal bone area. X-ray and histological examination of this area showed less trabeculae and calcification. Biochemical analyses of the skull frontal bones for bone mineral, non-collagenous protein, hexosamine and collagen demonstrated that the frontal bones from the Si-deficient chicks had a significantly reduced collagen content. In this study, the major effect of Si appears to be on the collagen content of the connective tissue matrix, a deficiency resulting in abnormal skull matrix formation. Support is given to the earlier postulate that Si is involved in an early stage of bone formation.

Animals↗

PubMed1981

Effects of high glucose and high lard diets on the activities of rat liver glycosyltransferases.

The activities of several enzymes involved in glycoprotein synthesis were measured in the livers of rats (L) fed diets with 67% of calories as lard and compared with those of rats (G) fed 67% glucose diets for 5-9 days. Glucosamine synthetase activity was not influenced by diet, but the activities of UDP-N-acetylglucosaminyl, galactosyl and sialyltransferases were significantly greater in the livers of the rats fed the glucose diet than in L rat livers. The content of UDP-N-acetylglucosamine was also higher in G livers than in the L group. Activities of glycosidases and of sugar nucleotide pyrophosphatases and phosphatases were the same on both diets. Serum total hexosamine was higher in L than in G rats. These findings are discussed in relation to earlier reports that liver plasma membranes from G rats contained more glycoprotein carbohydrate than L membranes.

Animals↗

PubMed2003

Inadequate copper intake reduces serum insulin-like growth factor-I and bone strength in growing rats fed graded amounts of copper and zinc.

This study examined the effects of graded intakes of zinc (Zn) and copper (Cu) on serum insulin-like growth-factor-I (IGF-I) concentration and bone quality in growing rats. Using a 3 x 4 factorial design, weanling male Sprague-Dawley rats were randomly assigned to 12 groups (n = 7 per group) and were fed one of nine modified AIN-93G basal diets with varying amounts of Cu (0.3, 3 and 10 micro g/g) and Zn (5, 15 and 45 micro g/g) for 6 wk. A group of rats was pair-fed to each low Zn group. Although dietary Zn mainly influenced body weights (P < 0.0001), dietary Cu was the main determinant of most of the variables related to bone quality. Low Cu intake reduced serum IGF-I and femur breaking force and ultimate stress (by 27, 14 and 7%, respectively; P < 0.05) and increased bone IGF-I concentration (by 62%; P < 0.0001). Low Cu intake also increased femur nitrogen, hydroxyproline, hexosamine and calcium (Ca) concentrations of long bones (P < 0.05). Lumbar vertebrae dry weight and density were the lowest in the rats fed the low Cu diets (P < 0.001) and were higher in the rats fed high amounts of both Cu and Zn (P < 0.01). In summary, growing rats fed low and marginal Cu had lower serum IGF-I than those fed high dietary Cu. Bone strength was also reduced with low dietary Cu, despite compensatory changes in the bone matrix. In the presence of graded intakes of Cu, the effects of low dietary Zn were more pronounced on the spinal bones than the long bones.

Analysis of Variance↗

PubMed2006

Glucosamine supplementation accelerates early but not late atherosclerosis in LDL receptor-deficient mice.

Glucosamine, commonly consumed for the treatment of osteoarthritis, is classified as a nutritional supplement; however, there are few data regarding its metabolic or vascular effects. Glucosamine is a component of the hexosamine pathway, which has been implicated in the development of insulin resistance. Anecdotal reports suggest that glucosamine consumption can increase circulating cholesterol concentrations. To investigate the metabolic and vascular effects of glucosamine supplementation, we studied male and female LDL receptor-deficient mice fed a Western diet (21% fat, 0.15% cholesterol). Three groups of 6-10 mice of each gender received either no supplement, 15 mg . kg(-1) . d(-1) glucosamine (equivalent to an average human dose), or 50 mg . kg(-1) . d(-1) glucosamine added to their drinking water for 5, 10, or 20 wk. Plasma cholesterol and triglyceride concentrations increased in all mice with the addition of the Western diet. However, after 20 wk of treatment, cholesterol and triglyceride concentrations increased further in male mice consuming glucosamine compared with control groups. Glucosamine-supplemented mice had increased initiation of atherosclerosis after 5 wk; however, there was no effect on progression of atherosclerosis in either gender after longer periods of glucosamine supplementation (10 or 20 wk). Although long-term glucosamine supplementation exacerbated the hyperlipidemia in male mice, no increase in atherosclerosis occurred. Thus, glucosamine supplementation appears to be safe, with no adverse vascular consequences.

Animals↗

PubMed2000

Renin inhibits N-acetyl-D-glucosamine 2-epimerase (renin-binding protein).

Renin-binding protein (RnBP) is a highly specific renin inhibitor first isolated from porcine kidney. Our recent studies demonstrated that the human RnBP is the enzyme N-acetyl-D-glucosamine (GlcNAc) 2-epimerase [Takahashi, S. et al. (1999) J. Biochem. 125, 348-353]. We have developed a new assay method for GlcNAc 2-epimerase activity using a system of N-acyl-D-hexosamine oxidase coupled with peroxidase and employed this method to study the effects of renin on GlcNAc 2-epimerase activity. The recombinant human (rh) RnBP existed as a dimer and its GlcNAc 2-epimerase activity was strongly inhibited by the purified renin concomitant with the formation of RnBP-renin heterodimer, so-called high molecular weight (HMW) renin. The renin activity was also inhibited by rhRnBP in a dose-dependent manner. These results indicate that renin is an inhibitor of GlcNAc 2-epimerase, and the renin-RnBP heterodimer HMW renin is an inactive form of both renin and GlcNAc 2-epimerase activities.

Carbohydrate Epimerases↗

PubMed1987

Purification of a young age-related glycoprotein (Ugl-Y) from normal human urine.

Ugl-Y is a glycoprotein that is detected in normal urine samples from young men and women aged 0 to 17 years. It was purified by ammonium sulfate precipitation and various column chromatographies including affinity chromatography using anti-adult urine antibody coupled to Sepharose 4B. The homogeneity of the glycoprotein was confirmed by polyacrylamide gel electrophoresis, isoelectric focusing, column chromatography on Sephadex G-75, and the precipitation reaction with anti-Ugl-Y antibody. It was shown to have a molecular weight of 29,000 by gel filtration, and to contain 5.2% neutral sugars (mannose and galactose) and 4% hexosamine (glucosamine). Amino acid analysis of the glycoprotein indicated high contents of acidic and hydroxylic amino acids. Its origin is unknown.

Aging↗

PubMed1978

A compound possessing antitumor and interferon-inducing activities derived from the common antigen (OEP) of Pseudomonas aeruginosa.

OEP, a component consisting mainly of protein with small amounts of lipids and sugars, has been isolated from the autolysate of Pseudomonas aeruginosa and purified by physicochemical methods. It possesses remarkable biological properties, showing antitumor and interferon-inducing activities. As regards the antitumor activity of the sample, the ED50 value against ascites sarcoma-180 was 1 microgram/kg mouse/day, and its interferon-inducing activity amounted to 15 units at a concentration of 0.01 microgram/ml. Both activities increased after protease digestion, reaching about ten times those of the sample which had not undergone digestion. The protease-treated OEP contained 17% protein, 14.5% total sugars, 31% lipids, 12.5% hexosamine, 3.8% KDO, and 2.7% phosphorus. Neutral sugars consisted of 12.4% rhamnose, 2.7% mannose, 66.9% glucose, and other unidentified material. Total lipids derived from OEP consisted of 65% loosely-bound and 35% covalently-bound lipids; the former contained C14:10, C16:0, C16:1, C18:0, and C15:1 acids and the latter, beta-OH C10:0, C12:0, alpha-OH C12:0, beta-OH C12:0, C16:0, and C16:1 acids. The antitumor and interferon-inducing activities of OEP remained after the removal of loosely-bound lipids from OEP.

Amino Acids↗

PubMed1978

Structural studies on glycolipid of shellfish. II. Occurrence of 3-O-methylgalactosamine in oyster glycolipid.

3-O-Methyl hexosamine was found for the first time and characterized as one of the sugar components of oyster glycolipid. The alditol acetate of this sugar was identified as 3-O-methyl-N-acetylgalactosaminitol acetate by comparing its retention time on gas chromatography and mass spectrum with those of the authentic sample synthesized in this laboratory. The new sugar, 3-O-methylgalactosamine, occupied the non-reducing terminal position of the carbohydrate moiety of the lipid and was linked to the penultimate hexose by a (1 leads to 3) bond.

Animals↗