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PubMed1981

Isolation and structural studies of the neutral oligosaccharide units from bovine glycophorin.

The O-glycosidically linked carbohydrate units of glycophorin from bovine erythrocyte membranes were released as reduced oligosaccharides by alkaline borohydride treatment. These oligosaccharides were separated by ion-exchange chromatography followed by gel filtration. Three oligosaccharides, a penta- a hepta- and a decasaccharide were obtained as the major components from the neutral fraction, and seven fractions were separated from the acidic fractions. All of the fractions were found to contain galactose and N-acetylglucosamine in variable amounts, as well as N-acetylgalactosaminitol. Studies of the neutral oligosaccharides by methylation analyses, nitrous acid deamination and Smith degradation, indicated the structure of the pentasaccharide to be Gal(1 leads to 3)Gal(1 leads to 4)GlcNAc(1 leads to 3)GalNAcol and that of the heptasaccharide to be Gal(1 leads to 3)Gal(1 leads to 4)GlcNAc(1 leads to 3)Gal(1 leads to 4)GlcNAc(1 leads to 3)Gal(1 leads to 3)GalNAcol. The highest molecular weight fraction, decasaccharide in the neutral fraction had a branching point at C-6 of a galactose residue.

Animals↗
PubMed1982

O-Linked oligosaccharides of human articular cartilage proteoglycan.

O-linked oligosaccharides and keratan sulphate chains have been isolated from the proteoglycan subunits of human articular cartilage. The oligosaccharides possessed a size and chemical composition similar to the equivalent moieties present in the proteoglycan subunits of the Swarm rat chondrosarcoma. Furthermore, the size and chemical composition of the oligosaccharides showed little change with the age of the individual from whom the proteoglycan was obtained. In contrast, the keratan sulphate chains appeared to increase in chain length with increased age of the individual. The total number of keratan sulphate and oligosaccharide chains per core protein decreased with age, but it was not clear whether there was any change in the ratio of the two components with respect to one another.

Adolescent↗
PubMed1982

Structural studies of the acidic oligosaccharide units from bovine glycophorin.

The O-glycosidically-linked carbohydrate units of glycophorin from bovine erythrocyte membrane were released by alkaline borohydride treatment. These oligosaccharides were separated into the neutral fractions and the acidic fractions by ion-exchange chromatography followed by gel filtration. The two acidic fractions (fractions 10 and 13) which have the smallest molecular weight in acidic oligosaccharides, were further purified by gel filtration on Bio-Gel P-4 column. Two acidic oligosaccharides (fractions 10-I and 10-II), heptasaccharides, were separated by gel filtration on a Bio-Gel P-4 column from fraction 10. These structures were determined by methylation analyses, nitrous acid deamination after hydrazinolysis and Smith degradation after desialylation. In addition, the structures were also analyzed by direct-probe mass spectrometry of the permethylated derivatives before and after desialylation. These studies indicated that one of them (fraction 10-I) was NeuNGc alpha(2 leads to 3)Gal beta(1 leads to 4)GlcNac beta(1 leads to 3)Gal beta(1 leads to 4)GlcNAc beta (1 leads to 3)Gal beta(1 leads to 3)GalNAcol and another heptasaccharide (fraction 10-II) was Gal beta (1 leads to 4)GlcNAc beta (1 leads to 3)Gal beta (1 leads to 3)[NeuNGc alpha(2 leads to 3)Gal beta(1 leads to 4)GLcNAc beta(1 leads to 6)]GalNAcol. Although another acidic fraction (fraction 13, was obtained as a single peak on a Bio-Gel P-4 column, it appeared to be the mixture of a heptasaccharide, NeuNGc alpha(2 leads to 3)Gal beta(1 leads to 4)GlcNAc beta(1 leads to 3 or 6)[Gal beta (1 leads to 4)GLcNAc beta (1 leads to 6 or 3)]Gal beta (1 leads to 3)GalNAcol and an oligosaccharide similar to fraction 10-II, by analysis of two products obtained by Smith degradation after desialylation.

Animals↗
PubMed1983

Structural analysis of the major caprine beta-mannosidosis urinary oligosaccharides.

Urinary oligosaccharides were studied in beta-mannosidosis, a newly identified, inherited glycoprotein catabolic disorder associated with severe neonatal neurological deficits, widespread lysosomal storage vacuoles and a deficiency of plasma and tissue beta-mannosidase. A preliminary analysis of the oligosaccharides was obtained by gel-permeation chromatography and mass chromatography. The major urinary oligosaccharides were then isolated by gel-permeation chromatography, DEAE-Sephadex column chromatography and preparative paper chromatography, and were analyzed by carbohydrate composition analysis, methylation studies, mass spectrometry and glycosidase digestion. As a result of these studies, beta-mannosyl-(1 leads to 4)-N-acetylglucosamine and beta-mannosyl-(1 leads to 4)-beta-N-acetylglucosaminyl-(1 leads to 4)-N-acetylglucosamine were identified as the major abnormal oligosaccharides. Galactosaminyl-(alpha 1 leads to 3)-[fucosyl-(alpha 1 leads to 2)]-galactose was also found in affected goat urine, while lactose was present in the urine of both control and affected goats.

Animals↗
PubMed1994

Glycosylation of yeast exoglucanase sequons in alg mutants deficient in the glucosylation steps of the lipid-linked oligosaccharide. Presence of glucotriose unit in Dol-PP-GlcNAc2Man9Glc3 influences both glycosylation efficiency and selection of N-linked sites.

The major exoglucanase (Exg) from Saccharomyces cerevisiae has a short N-linked oligosaccharide attached to each of the potential glycosylation sites present in the primary translation product. We have studied the Exg glycoforms secreted by alg mutants deficient in the final steps of the assembly of dolichol-P-P-GlcNAc2-Man9-Glc3. These mutants synthesize and transfer to nascent proteins truncated oligosaccharides lacking two (alg8) or three (alg5 and alg6) glucoses. In addition to the enzyme carrying both sugar chains (ExgII), all three mutants secreted underglycosylated forms containing one oligosaccharide attached to either the first (ExgII'1/2) or the second (ExgII1/2) potential glycosylation site, and nonglycosylated enzyme (ExgTuni). As compared with alg5 and alg6, alg8 secreted a higher proportion of ExgII, which was paralleled by a significant drop in the proportion of ExgTuni and, to a lesser extent, of ExgII1/2. The presence of a single glucose attached to Dol-P-P-GlcNAc2-Man9 therefore increases the efficiency of transfer of the that oligosaccharide to the protein acceptor in vivo. Moreover, whereas ExgII'1/2 was never secreted by wild type cells, it was the most abundant underglycosylated form secreted by all three mutants. These mutants are affected in the efficiency at which the individual sequons that are glycosylated, and this suggests a role for the glucotriose unit in the selection of the sequons are to be occupied in glycoproteins synthesized by wild type.

Binding Sites↗
PubMed1983

Biosynthesis of pulmonary glycoconjugates--V. Biosynthesis of oligosaccharide inner core region of N-glycoprotein in lung microsomes.

Lung microsomes are able to synthesize dolichyl-mannosyl-phosphate, which stimulates the biosynthesis of a product (P1), soluble in chloroform/methanol/water (10:10:3, v/v). In presence of pulmonary dolichyl-mannosyl-phosphate, liver microsomes synthesized 3 mannosylated products: X1 product recovered in chloroform/methanol extract, X2 and X3 products soluble in chloroform/methanol/water (10:10:3, v/v). Mild acid hydrolysis of P1 product released one mannosylated oligosaccharide which remained at the origin in our solvent system, since two mannosylated oligosaccharides, released from products synthesized in liver, moved very slowly. Addition of N,N'-diacetyl [14C]chitobiosyl-pyrophosphoryl-dolichol to lung microsomes incubated with GDP-[3H]mannose stimulated the synthesis of a [3H, 14C]product extracted with chloroform/methanol (2:1, v/v). Mild acid hydrolysis of this product released [3H, 14C]oligosaccharide which moved very slowly on paper chromatography, in our solvent system. These results demonstrate that lung tissue can synthesize the oligosaccharide inner core region of N-glycoprotein with the sequence (Man)x-(GlcNac)2. But pulmonary dolichol pool is probably involved in other lipid biosynthesis pathways.

Animals↗
PubMed1990

Immunochemical studies of oligosaccharides obtained from the lipopolysaccharide of Brucella ovis.

Brucella ovis rough lipopolysaccharide (R-LPS) was studied with respect to its heterogeneity, chain length, sugar composition and immunological activity. R-LPS was mildly hydrolysed and oligosaccharides were recovered in the upper phase after partition with chloroform-methanol. Gel-filtration of the upper phase in a column of Bio-Gel P-2 yielded oligosaccharides of 2, 4, 6 and 7 monosaccharide units, 2-keto-deoxy-octulosonic acid (KDO), and monosaccharides. Strong acid hydrolysis followed by paper chromatography showed that the hexa- and heptasaccharides are both composed of glucose, KDO and an unidentified sugar while tetrasaccharide is composed of glucose, mannose and glucosamine. These three oligosaccharides were able to inhibit the LPS-antibody reaction in a solid phase radioimmunoassay, suggesting the oligosaccharides bear antigenic determinants of LPS.

Animals↗
PubMed1991

Determination of neutral oligosaccharide fractions from human milk by gel permeation chromatography.

A gel permeation chromatographic method for quantifying neutral oligosaccharide fractions from human milk has been developed. Oligosaccharides from monofucosyllactoses to trifucosyllacto-N-hexaoses were separated according to size on a Fractogel TSK HW 40 (S) column. Refractive index detection of monofucosyllactoses to difucosyllacto-N-tetraoses yielded a constant mass response factor of ca. 1 relative to glucose. After the addition of glucose as an internal standard, oligosaccharides were isolated from human milk by ethanol precipitation or two ultrafiltration procedures. The oligosaccharide concentrations found by the ultrafiltration procedures were significantly lower (significance level 0.05) than those determined by the ethanol precipitation procedure.

Carbohydrate Sequence↗
PubMed1994

The use of lipid-linked oligosaccharides (neoglycolipids) in the identification of carbohydrate receptors for microbial pathogens.

Specific oligosaccharide chains on the host cell surface act as receptors for many microbial pathogens. Identification of receptor structures is an important step in the understanding of the pathogenesis of infection. Glycolipid receptors have been identified by direct binding assays. However, technical difficulties have prevented demonstration of bacterial binding to the oligosaccharides of glycoproteins; these have been identified mainly by inhibition assays. By a novel technique developed in our laboratory, oligosaccharides released from glycoproteins are linked to lipids to form neoglycolipids. These can be used in bacterial binding assays. The feasibility of this approach has been demonstrated using type 1 fimbriated Escherichia coli binding specifically to neoglycolipids rich in mannose residues. The application of the method has resulted in a demonstration of a new type of adhesive specificity for E. coli and differences in the binding specificities of E coli and Pseudomonas aeruginosa. Further application of this technique by generating oligosaccharides purified from mucus glycoproteins from patients with cystic fibrosis to use in binding assays with P aeruginosa is currently being undertaken. The basic knowledge gained by this approach may in time see the development of novel therapy in the form of receptor blocking agents.

Bacteria↗
PubMed1991

Removal of N-linked oligosaccharides of presumptive ectoderm impairs neural induction in Pleurodeles waltl.

Studies were carried out on the embryo of the amphibian Pleurodeles waltl to investigate the potential role of the N-linked oligosaccharides of the ectodermal cell membrane in the neural induction process. Glycopeptidase F (GPase F) was used to cleave N-linked oligosaccharides on presumptive ectoderm. Removal of oligosaccharide moieties from ectoderm membrane glycoconjugates completely inhibited natural neural induction in vitro. On the other hand, Swainsonine (Sw) and 1-deoxynojirimycin (dNM), specific inhibitors of enzymes involved in glycosylation, provoked strong and persistent changes in the structure of the N-linked oligosaccharides of presumptive ectoderm but did not prevent neuralisation of treated ectoderm. We conclude that N-linked carbohydrates are implicated in the phenomenon of neural induction. However, the structural integrity of N-linked carbohydrates of target tissue is not itself critical in this process. The existence of specific carbohydrates on presumptive ectoderm was still questioned as receptors of neural signal.

1-Deoxynojirimycin↗
PubMed2004

N-linked oligosaccharide analysis of glycoprotein bands from isoelectric focusing gels.

Glycoproteins often display a complex isoelectric focusing profile because of the presence of negatively charged carbohydrates, such as sialic acid, phosphorylated mannose, and sulfated GalNAc. Until now, understanding the role of these charged carbohydrates in determining the isoelectric focusing profile has been limited to observing pattern shifts following complete removal of the sugars in question. We have developed a simple and sensitive method for analyzing N-linked oligosaccharides from the individual isoelectric focusing bands of a glycoprotein using recombinant human thyroid-stimulating hormone as a model system. N-linked oligosaccharides were released and profiled from individual bands following electroblotting of isoelectric focusing gels. As might be predicted, high-pH anion-exchange chromatography-pulsed amperometric detection and matrix-assisted laser desorption/ionization-time of flight analyses indicated that the bands that migrated closer to the positive electrode contained more sialylated N-linked oligosaccharides. The sialic acid content of these bands correlated with that predicted from the corresponding oligosaccharide analyses.

Chromatography, Ion Exchange↗
PubMed2006

Enzymatic and chemical methods for the generation of pure hyaluronan oligosaccharides with both odd and even numbers of monosaccharide units.

Hyaluronan oligosaccharides display physiological activities not associated with the polymer and are widely used to characterize hyaluronan-binding proteins. They can also be used as biocompatible starting blocks for chemical derivatization. Here we present methods for generating milligram quantities of unusual odd- and even-numbered oligosaccharides, greatly increasing the diversity of reagents for use in such studies. These methods are based upon protocols from the 1960s, at which time it was very difficult to assess the stereochemical purity of the products. To address this, products were analyzed with modern high-field nuclear magnetic resonance spectroscopy. Alkaline beta-elimination conditions previously used to remove reducing-terminal N-acetylglucosamine residues in fact introduce a significant ( approximately 30%) level of stereoisomerism in the products by alkali-catalyzed keto-enol tautomerizations. Milder alkaline conditions were used to overcome this problem, reducing the contamination to <5%. The elimination by-products from this reaction were isolated and characterized, allowing the mechanism of alkaline degradation of hyaluronan to be investigated for the first time. beta-Glucuronidase was used to remove nonreducing-terminal glucuronic acid residues from oligosaccharides. Odd-numbered oligosaccharides with terminal glucuronic acid residues isolated from hyaluronidase digests are shown to originate from acid-catalyzed acetal hydrolysis during boiling denaturation and also have significant levels of stereochemical impurities.

Alkalies↗
PubMed2004

Fluorous-tagged compound: a viable scaffold to prime oligosaccharide synthesis by cellular enzymes.

Fluorous-tagged saccharide primers could be viable scaffolds for the synthesis of oligosaccharides. This research demonstrates that a fluorine-containing saccharide derivative could actually be taken up by the cell, the saccharide chain elongated by cellular enzymes, and the elongated product released by the cells to the culture medium. A fluorous-tagged lactoside primer, 6-(perfluorohexyl)hexyl-4-O-(beta-D-galactopyranosyl)-beta-D-glucopyranoside, was chemically synthesized and introduced in mouse B16 cells to prime oligosaccharide synthesis. Uptake of the primer by B16 cells resulted in the sialylation of the terminal galactose residue to afford an oligosaccharide with the same glycan structure as ganglioside GM3. The presence of many fluorine atoms did not have any adverse effects to the cells. Moreover, the number of fluorine atoms did not pose a steric barrier and instead, their presence possibly increased the hydrophobicity of the primer and enhanced membrane permeability. This strategy of using a fluorous-tagged primer and cells can pave the way for an easier way of preparing oligosaccharides via an environment-friendly approach that eliminates the use of large amounts of organic solvents.

Animals↗
PubMed2005

Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins.

Arylphorin is an insect hexameric storage protein. The structures of the oligosaccharides attached to this protein have recently been determined. However, their precise functions remain to be established. Proteolysis and MALDI MS studies disclose that the amino acid residues Asn196 and Asn344 are N-glycosylated with Glc(1)Man(9)GlcNAc(2) and Man(5-6)GlcNAc(2) oligosaccharides, respectively. Interestingly, significant variations in the amounts of glycans involving Glc(1)Man(9)GlcNAc(2) are evident in arylphorins purified from larvae reared at different seasons. The data suggest that the metabolism of larvae and local protein structure contribute to glycan development. Three-dimensional model of the protein speculated that N-glycosidic linkage to Asn196 in the Glc(1)Man(9)GlcNAc(2) structure was buried inside the twofold axis of the hexamer, whereas oligosaccharide linkages to Asn344 were completely exposed to solvent. This finding is in agreement with previous biochemical data showing that limited Glc(1)Man(9)GlcNAc(2) was released by protein-N-glycosidase F under non-denaturing conditions, in contrast to Man(5-6)GlcNAc(2) oligosaccharides.

Amino Acid Sequence↗
PubMed2006

Reactive oxygen species modify oligosaccharides of glycoproteins in vivo: a study of a spontaneous acute hepatitis model rat (LEC rat).

The Long-Evans Cinnamon (LEC) rat, an animal model of Wilson's disease, spontaneously develops hepatitis as the result of abnormal copper accumulation in liver. The findings of this study show that copper, hydrogen peroxide, and lipid peroxides accumulate to drastically high levels in LEC rat serum in acute hepatitis but not chronic hepatitis. The effect of these reactive oxygen species (ROS) on oligosaccharides of glycoproteins in the LEC rat serum was examined. Lectin blot and lectin ELISA analyses showed that sialic acid and galactose residues of serum glycoproteins including transferrin were decreased in acute hepatitis. Further analyses of oligosaccharide structures of transferrin demonstrated that di-sialylated and asialo-agalacto biantennary sugar chains, but not tri-sialylated sugar chain, exist on transferrin in the acute hepatitis rats. In addition, treatment of non-hepatitis rat serum with copper ions and hydrogen peroxide decreased tri-sialylated sugar chain of the normal transferrin and increased di-sialylated and asialo-agalacto biantennary sugar chains. This is the first evidence to show that ROS result in the cleavage of oligosaccharides of glycoproteins in vivo, and indicate this cleavage of oligosaccharides may contribute the development of acute hepatitis.

Acute Disease↗
PubMed2006

Degradation of cellulosome-produced cello-oligosaccharides by an extracellular non-cellulosomal beta-glucan glucohydrolase, BglA, from Clostridium cellulovorans.

Clostridium cellulovorans degrades cellulose efficiently to small oligosaccharides, which are used as an energy source. To characterize enzymes related to degrading small oligosaccharides, a gene was cloned for an extracellular non-cellulosomal beta-glucan glucohydrolase (BglA) classified as a family-1 glycosyl hydrolase in C. cellulovorans. Recombinant BglA (rBglA) had higher activity on long glucooligomers than on cellobiose. When cellulosomes and rBglA were incubated with cellulose, the oligosaccharides produced were degraded more effectively to cellobiose and glucose, than with cellulosomes alone, indicating that BglA facilitated the degradation of accessible cello-oligosaccharides produced from cellulose by C. cellulovorans cellulosomes. Thus, this is an example of an extracellular non-cellulosomal enzyme working in a cooperative manner with cellulosomes to degrade cellulose to sugars.

Carbohydrates↗
PubMed2005

Oligosaccharide structures of von Willebrand factor and their potential role in von Willebrand disease.

Oligosaccharides make up approximately 20% of the mass of VWF and although their structures are well established, their functional role remains unclear. Modification of the VWF oligosaccharide structures has been shown to result in increased plasma clearance of the protein. A mutation which alters cell type-specific expression of the Galgt2 glycosyltransferase gene in the RIIIS/J mouse results in an autosomal dominant partial quantitative deficiency of VWF. Increased plasma clearance of VWF has been demonstrated in some individuals with a partial quantitative deficiency of the protein and it is possible that variation in VWF glycosylation may contribute towards this. ABH antigens occur within the oligosaccharide component of VWF and may account for the variation in plasma VWF:Ag levels observed between individuals of different ABO blood groups. The structures and functional roles of the oligosaccharide side chains of VWF and possible pathogenetic mechanisms by which they may contribute towards VWD are reviewed in this article.

ABO Blood-Group System↗
PubMed2004

Interaction assay of oligosaccharide with lectins using glycosylasparagine.

Glycosyl amino acids having natural glycan were useful for the interaction assay of oligosaccharides. A glycochip containing the whole structure of an oligosaccharide was easily prepared by the immobilization of the glycosyl amino acid. Furthermore, fluorescence probes were introduced into the glycosyl amino acid while maintaining the whole structure of oligosaccharide. By using these labeled oligosaccharides, fluorescence polarization (FP) and fluorescence correlation spectroscopy (FCS) analyzed the carbohydrate-lectin interaction in a solution assay system.

Animals↗