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PubMed1994

Isolation and characterization of a novel 20-kDa sulfated polysaccharide from the extracellular slime layer of Staphylococcus epidermidis.

Slime-producing coagulase-negative staphylococci have emerged as important pathogens especially in immunocompromised hosts and patients with implanted devices. Although the extracellular slime layer is considered an important virulence factor, the chemical composition of the slime polysaccharide(s) remains unknown. The crude slime product derived from two reference Staphylococcus epidermidis strains (ATCC 35983 and 35984) and two clinical isolates was found to contain protein (11-20.5%), hexosamines (8-19%), neutral sugars (12.2-14%), phosphates (4-9.5%), uronic acids (1-13%), and small amounts of sulfates (0.5-3%). Preparative anion-exchange chromatography separated a main carbohydrate component which was isolated by combined chromatographies on DEAE-Sephacel and Sepharose CL-6B. HPLC and electrophoreses on polyacrylamide gel and cellulose acetate membrane revealed the presence of one species of low-sulfated polysaccharide with a relative molecular mass of 20-kDa. Chemical analyses of the polysaccharide showed that it is rich in glucosamine (46%) and neutral sugars (30-34%) with small amounts of sulfates (5.7-6.5%) and glucuronic acid (2.9-3.4%). Ten percent of the glucosamine is sulfated at the amino group. The neutral monosaccharides present are glucose, fucose, and xylose with glucose as the predominant one. It is estimated that the polysaccharide consists of 61-65 molecules of glucosamine (6-7 of which are N-sulfated), 30-35 neutral monosaccharides, 3-4 molecules of glucuronic acid, and 1-3 of fucose and xylose. Isolation and characterization of such a polysaccharide from the extracellular slime layer of S. epidermidis has not been previously reported. Its role to pathogenicity remains to be elucidated.

Bacterial Proteins↗
PubMed1997

Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1.

A bacterium-producing polysaccharide lyase (gellan lyase) was isolated from soil samples and identified to be Bacillus sp. The lyase was purified from the culture fluid of the bacterium (designated Bacillus sp. GL1) grown in the presence of gellan as a carbon source. The purified gellan lyase depolymerized deacetylated gellan and gave a single oligosaccharide product with a molecular weight of 646, which was determined by fast atom bombardment mass spectrometry. The structure of the product was determined by the combination of mass spectrometry, HPLC analysis, and high-resolution proton nuclear magnetic resonance spectroscopy to be a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminal. When incubated in cell extracts of Bacillus sp. GL1, the tetrasaccharide was first converted to trisaccharide without unsaturated glucuronyl residue, and the trisaccharide was then converted to hydrolyzed monosaccharides glucose and rhamnose. These results show that, in the bacterium Bacillus sp. GL1, gellan is first depolymerized to give a tetrasaccharide, a repeating unit in gellan molecule, by an extracellular gellan lyase and then the tetrasaccharide is hydrolyzed to monosaccharides by successive actions of intracellular exoglycosidases.

Bacillus↗
PubMed1995

Rapid quantitative determination of sialic acids in glycoproteins by high-performance liquid chromatography with a sensitive fluorescence detection.

Sialic acids were specifically labeled with o-phenylenediamine-2HCl (OPD) to yield stable fluorescent quinoxaline derivatives. The sialic acids were released from the glycoprotein in a NaHSO4 solution (0.25 M 80 degrees C, 20 min) and derivatized in the same solution with the OPD (10 mg/ml (final conc.) 80 degrees C, 40 min). Various sialic acids derivatized with the OPD were separated on a C-18 reversed-phase Ultrasphere-ODS column using the solvent systems and the detector conditions used for the determination of monosaccharides derivatized with anthranilic acid as reported earlier. The common N-acetyl- and N-glycolylneuraminic acids were separated within 20 min, and the other N- and O-acylated sialic acids were separated in 40 min. The OPD derivatives of mono-, di-, and triacylated sialic acid were separated into their respective groups in the present separation. The fluorescence maxima for the OPD-N-acetylneuraminic acid were 232 nm excitation and 420 nm emission and the limit of quantitation was < 2 pmol. The relative standard deviation was less than 3.0% for the sialic acid determinations using the glycoproteins. A common single HPLC system is used for complete carbohydrate composition analysis of glycoproteins, since both the sialic acid and the monosaccharide methods use the same solvent systems, column, and detector settings. Furthermore, in contrast to high-performance anion-exchange chromatography with pulsed amperometric detection, these methods are easy to set up for an analysis and offer the highest sensitivity for analyzing samples available in microgram amounts.

Chromatography, High Pressure Liquid↗
PubMed1998

High-resolution polyacrylamide gel electrophoresis of carbohydrates derivatized with a visible dye.

A technique for carbohydrate analysis that is both inexpensive and easily performed is currently unavailable. In this communication we address the problem and have outlined a method for labeling saccharides with a visible dye, 4-amino-1,1'-azobenzene-3, 4'-disulfonic acid, which has an absorption maximum of 489 nm and an extinction coefficient of 37,615, to facilitate visible detection at low levels. The visible dye was coupled by a reductive amination to different sugars. The sugar-dye adducts were then separated by electrophoresis on alkaline polyacrylamide gels. The gels were scanned with a densitometer, and visible sugar-dye adducts were qualitatively analyzed by identifying them according to their mobilities. The sugar-dye adducts were quantified by determining their densitometric volume. The kinetics of the reductive amination reactions, performed at 37 degrees C, were different for each of three saccharides tested. The rate constants for glucose and fucose were 1.31 times greater and 1.8 times greater, respectively, than that of maltotriose. The reductive amination reactions were essentially complete after approximately 16 h under the given experimental conditions. A linear dose-response relationship was observed between the amount of sugar (monosaccharide, trisaccharide, or heptasaccharide) in the reductive amination reaction. The quantity of saccharide-dye adduct that could be visually detected for glucose, maltotriose, and maltoheptaose, was 25, 25, and 50 nmol, respectively. Sugar-dye adducts were separated from one another by varying the acrylamide concentration in the polyacrylamide gels. Sugar-dye adducts of monosaccharides, disaccharides, trisaccharides, and heptasaccharides were separated on alkaline 30% polyacrylamide gels with mobilities of 0.778, 0.667, 0.639, and 0.375. Adducts of glucose, fucose, galactose, and mannose were separated with mobilities of 0.844, 0.833, 0.820, and 0.810, respectively, on a 30 to 40% gradient polyacrylamide gel. Adducts of glucose and glucose derivatives were separated on a 35% polyacrylamide gel. This technique provides an inexpensive and easily performed method of carbohydrate analysis to laboratories that do not have the highly trained personnel nor the expensive equipment needed for other methods of carbohydrate analysis. The method is most applicable to research problems where sensitivity (20 pmol) is not a problem. The simplicity of the method also makes it easily incorporated into teaching laboratories.

Carbohydrates↗
PubMed1999

Characterization of carbohydrates using highly fluorescent 2-aminobenzoic acid tag following gel electrophoresis of glycoproteins.

Application of the most sensitive fluorescent label 2-aminobenzoic acid (anthranilic acid, AA) for characterization of carbohydrates from the glycoproteins ( approximately 15 pmol) separated by polyacrylamide gel electrophoresis is described. AA label is used for the determination of both monosaccharide composition and oligosaccharide map. For the monosaccharide determination, bands containing the glycoprotein of interest are excised from the polyvinylidene fluoride (PVDF) membrane blots, hydrolyzed in 20% trifluoroacetic acid, derivatized, and analyzed by C-18 reversed-phase high-performance liquid chromatography. For the oligosaccharide mapping, bands were digested with peptide N-glycosidase F (PNGase F) in order to release the N-linked oligosaccharides, derivatized, and analyzed by normal-phase anion-exchange chromatography. For convenience, the PNGase F digestion was performed in 1:100 diluted ammonium hydroxide overnight. The oligosaccharide yield from ammonium hydroxide-PNGase F digestion was better or equal to all the other reported procedures, and the presumed "oligosaccharide-amine" product formed in the reaction mixture did not interfere with labeling of the oligosaccharides under the conditions used for derivatization. Sequencing of oligosaccharides can be performed using the same mapping method following treatment with an array of glycosidases. In addition, the mapping method is useful for determining the relative and simultaneous distribution of sialic acid and fucose.

Animals↗
PubMed2002

Carbohydrate analysis of bacterial polysaccharides by high-pH anion-exchange chromatography and online polarimetric determination of absolute configuration.

A significant problem in structure determination of complex carbohydrates, especially for bacterial polysaccharides, is determination of the absolute configuration of the component monosaccharides. A number of analytical methods have been used for this purpose but, as a result of the wide variety of chemical properties of sugars found in complex polysaccharides, no single method is universally applicable. High-resolution gas chromatography of volatile derivatives with chiral reagents is the most widely used method. Optical activity, although direct and simple, lacks sensitivity generally requiring a large quantity of pure monosaccharide. We report a combination of high-performance anion-exchange chromatography (HPAEC) with combined electrochemical pulsed amperometric detection and in-line detection of optical rotation with an in-line laser polarimeter for analysis of a number of sugars found in complex polysaccharides. We show that application of the method for analysis of capsular polysaccharides of several gram-positive and gram-negative pathogenic bacteria provides useful information simultaneously on carbohydrate composition and the enantiomeric configuration of component sugars.

Bacteria↗
PubMed1999

The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D -galactose.

C-type lectins are calcium-dependent carbohydrate-recognising proteins. Isothermal titration calorimetry of the C-type Polyandrocarpa lectin (TC14) from the tunicate Polyandrocarpa misakiensis revealed the presence of a single calcium atom per monomer with a dissociation constant of 2.6 microM, and confirmed the specificity of TC14 for D -galactose and related monosaccharides. We have determined the 2.2 A X-ray crystal structure of Polyandrocarpa lectin complexed with D -galactose. Analytical ultracentrifugation revealed that TC14 behaves as a dimer in solution. This is reflected by the presence of two molecules in the asymmetric unit with the dimeric interface formed by antiparallel pairing of the two N-terminal beta-strands and hydrophobic interactions. TC14 adopts a typical C-type lectin fold with differences in structure from other C-type lectins mainly in the diverse loop regions and in the second alpha-helix, which is involved in the formation of the dimeric interface. The D -galactose is bound through coordination of the 3 and 4-hydroxyl oxygen atoms with a bound calcium atom. Additional hydrogen bonds are formed directly between serine, aspartate and glutamate side-chains of the protein and the sugar 3 and 4-hydroxyl groups. Comparison of the galactose binding by TC14 with the mannose binding by rat mannose-binding protein reveals how monosaccharide specificity is achieved in this lectin. A tryptophan side-chain close to the binding site and the distribution of hydrogen-bond acceptors and donors around the 3 and 4-hydroxyl groups of the sugar are essential determinants of specificity. These elements are, however, arranged in a very different way than in an engineered galactose-specific mutant of MBPA. Possible biological functions can more easily be understood from the fact that TC14 is a dimer under physiological conditions.

Amino Acid Sequence↗
PubMed1988

Induction of erythroid differentiation by the anthracycline antitumor antibiotic pyrromycin.

The oligosaccharide-anthracyclines, aclacinomycin A, marcellomycin and musettamycin, are potent inducers of erythroid differentiation in hemopoietic cells lines of rodent and human origin. The present studies revealed that pyrromycin, a closely related monosaccharide-anthracycline, induced erythroid differentiation in Friend leukemia cells and in the human leukemia cell line K 562. Pyrromycin, marcellomycin and musettamycin, which possess an identical aglycone structure containing a Cl-hydroxyl group, exhibited relatively low optimal inductive concentrations. In contrast, the optimal inductive concentration of aclacinomycin A, which lacks the Cl-hydroxyl group, was markedly higher, i.e., the differentiation inducing capacity was lower. It should be noted, however, that the yield of differentiated cells following treatment with the monosaccharide-anthracycline pyrromycin was distinctly lower than that after treatment with the oligo-saccharide-anthracyclines, aclacinomycin A, marcellomycin or musettamycin. Thus, our data indicate that the efficacy of anthracyclines to induce erythroid differentiation is related to a) the presence of a Cl-hydroxyl group in the aglycone and b) the presence of an oligosaccharide side chain.

Aclarubicin↗
PubMed1982

Autoradiographic studies of protein and polysaccharide synthesis during vitellogenesis in Drosophila.

Quantitative light- and electron-microscopic autoradiography was used to evaluate metabolic processes that occur during late developmental stages (10-14) of oogenesis in Drosophila melanogaster. Major differences in radiolabelling patterns were found after in vivo (10-45 min) uptake of [3H]-monosaccharides and [3H]-L-lysine. Several different methods of data analysis were required to facilitate interpretation of these patterns. [3H]-L-lysine produced extensive cytoplasmic labelling at all developmental stages. In addition, about 15% of alpha yolk spheres were intensely labelled at stage 10, reflecting the incorporation of radiolabelled vitellogenins synthesized during the incubation period. Subsequent stages showed low silver grain density over alpha yolk spheres until stage 14, when a burst of [3H]-L-lysine incorporation by most alpha spheres was observed, possibly indicative of a maturation process for embryogenesis. [3H]-D-glucose and [3H]-D-galactose (10 min, in vivo) both induced intense labelling of the beta yolk spheres in a manner suggesting in situ assembly beginning at early stage 13. Inasmuch as the polysaccharide of beta yolk spheres has the properties of glycogen (e.g., rosette structure digested by alpha-amylase) and the radiolabelled monosaccharides were introduced intra-abdominally, it is evident that transport systems as well as enzymes utilizing glucose and galactose for glycogenesis must be readily available. It is notable that wide-spread labelling of egg chambers was elicited by [3H]-D-glucose and [3H]-D-galactose (e.g., nurse cells, follicle cells, chorion, vitelline membrane), but the labelling induced by [3H]-N-acetylmannosamine was restricted mainly to the endochorion. A possible role of microtubules in distribution and assembly of yolk spheres was inferred when colchicine, admixed to the culture medium (2-5 ppm), produced abnormal distribution and diminution in number of both alpha and beta yolk spheres. In addition to revealing previously unknown metabolic events of vitellogenesis, the results provide additional criteria for stage characterization as well as a means to specifically label certain macromolecules for purposes of isolation.

Animals↗
PubMed1992

A critical evaluation of neoglycoprotein binding sites in vivo and in sections of mouse tissues.

Endogenous lectins are reported to play a vital role in cell to cell communication. Their distribution in tissues has been widely studied by the use of labelled neoglycoproteins. In the present study, labelled neoglycoproteins were used on fixed and unfixed tissue sections and the results were compared with those observed after i.v. application of neoglycoproteins in mice. The study indicates that neoglycoprotein binding to tissue sections is not inhibited by application of the simple monosaccharides that were used to synthesize them. Furthermore the binding of neoglycoproteins following i.v. application into mice is rather limited. It is concluded that neoglycoproteins, which are synthesized using simple monosaccharides, do not provide a sensible tool to detect endogenous lectins in animal tissue sections. This is in sharp contrast to the results of most other studies reported in the literature.

Animals↗
PubMed1975

[Alpha-1-antitrypsin deficiency in children: liver ultrastructure and speculations (author's transl)].

Fourteen liver biopsies from twelve young patients with liver diseases associated with homozygous, PiZZ phenotype, alpha-1-antitrypsin deficiency in their sera were examined by electron microscopy. In all these biopsies characteristic homogeneous material was found in some hepatocytes and corresponded, when observed on adjacent semithin sections by light microscopy, to the deposit stained by periodic acid Schiff reaction. The accumulation in perinuclear spaces resulted in intranuclear invaginations, but the major deposit was located in lumens of the endoplasmic reticulum. The limiting membranes were rough and smooth but the extent of the latter was so large that only this type of reticulum seemed peculiarly involved in the accumulating process. On the contrary, Golgi complexes did not seen obligatorily involved by this process because, when observed, they appeared almost normal even in heavily overloaded liver cells. At least for the PiZZ phenotype, the abnormal substance would be an asialo form of normal alpha-1-antitrypsin. Thus the subject of this study is the morphologic translation of an impairment in the synthesis of a glycoprotein. In the light of data concerning the synthesis of such proteins our findings lead us to suggest: The ultrastructural patterns observed in alpha-1-antitrypsin deficiency cannot give the expected morphologic evidence of the biochemical data which locate the first binding steps of monosaccharide residues in the rough endoplasmic reticulum. The absence of sialic acid could not result from an enzymatic defect primarily located in Golgi complexes but could be secondary to an impairment in the binding of one monosaccharide residue which improves subsequent fixation of sialic acid, in the smooth endoplasmic reticulum. Finally it seems necessary to emphasize that the relationship between the abnormal substance and various important non specific lesions is largely unknown and that we don't know the significance of polymorphous dense bodies observed in ductular cells during the cholestatic period.

Cell Nucleus↗
PubMed1981

Interval breath hydrogen test in glucose-galactose malabsorption.

A simple test is described for the diagnosis of monosaccharide malabsorption in infancy caused by a congenital defect of glucose and galactose transport. Increased hydrogen (H2) excretion in expired air after ingestion of sugar was used to diagnose this condition in an infant with severe diarrhoea after breast feeding. Abnormal amounts of H2 were excreted after oral administration of glucose and galactose, but not after fructose. A carbohydrate free diet supplemented with fructose resulted in rapid weight gain and disappearance of diarrhoea. The diagnosis of glucose-galactose malabsorption was confirmed by 14C-glucose transport studies on a jejunal mucosal biopsy specimen. These findings indicate that interval breath H2 estimation in mixed expired air is a non-invasive, reliable procedure for detection of monosaccharide malabsorption in infancy.

Air↗
PubMed1988

Chemical signals of fish skin for the attachment response of Acanthostomum brauni cercariae.

The chemical signals of the skin surface of fish, which stimulate the attachment responses of Acanthostomum brauni cercariae, were identified by offering chemicals and fish-skin extracts in agarose substrates to the cercariae. Smaller molecules such as amino acids, fatty acids, monosaccharides, electrolytes, urea, and carbonate solutions did not stimulate attachments, but hyaluronic acid had some effects. Bovine submaxillary glycoproteins had a strong stimulating activity that disappeared after neuraminidase digestion. The stimulating components of the skin surface of fish were hydrophilic substances with molecular weights of more than 10,000. They were sensitive to neuraminidase digestion but not to hyaluronidase digestion and thus can be identified as glycoproteins. A. brauni cercariae respond only to the complete glycoprotein molecules and not to their monosaccharide components. The known attachment triggers of other cercariae are small molecules. Large glycoproteins as host signals for A. brauni cercariae may be an adaptation to muddy habitats, where various substances with low molecular weights may interfere with the host identification.

Amino Acids↗
PubMed1996

Enhancement of glycosylation of cellular glycoconjugates in the squamous carcinoma cell line MDA886Ln by beta-all-trans retinoic acid.

Retinoids have been shown to inhibit the growth and modulate the glycosylation of head and neck squamous cell carcinoma (HNSCC) cells including the MDA886Ln cells. To examine the effects of beta-all-trans retinoic acid (RA) on glycoconjugates in HNSCC MDA886Ln cells, the cells were grown in the absence or presence of 1 microM RA and then labeled with tritiated monosaccharides, extracted and analysed by polyacrylamide gel electrophoresis and fluorography. RA increased markedly the incorporation of [3H]-glucosamine, [3H]-galactose, and [3H]-mannose into numerous cellular glycoconjugates, however, the incorportion of [3H]-fucose and [3H]-leucine was almost unaffected by RA. RA increased the incorporation of glucosamine and galactose but not mannose into high molecular weight (HMW) glycoconjugates of about 220 and 500-600 kDa. To analyse the steady state level of glycoconjugates by lectin blotting, extracts of unlabeled cells were separated by gel electrophoresis and the gels were probed with 125I-labeled wheat germ agglutinin (WGA) and Maackia amurensis (MA) agglutinin. Both lectins were found to bind to numerous glycoconjugates including the HMW glycoconjugates, whereas 125I-peanut agglutinin bound only to the HMW glycoconjugates RA treatment increased the binding of all three lectins to the HMW glycoconjugates. These findings demonstrate that RA enhanced the incorporation of specific monosaccharides into a variety of glycoconjugates and in particular into HMW mucin-like glycoconjugates. This effect of RA may be the result of induction of a more normal differentiation state of the HNSCC cells.

Agglutinins↗
PubMed1989

Changes in Na,K-ATPase, sodium ion, and glucose transport in isolated enterocytes in an experimental model of malabsorption.

Nippostrongylus brasiliensis infection of the rat resulted, at day 10 of infection, in decreased levels of jejunal enterocyte sodium-potassium-activated adenosine triphosphatase (Na,K-ATPase) and potassium-activated p-nitrophenyl phosphatase (K-pNPPase) activities. Parallel decreases occurred in active sodium efflux from jejunal enterocytes in the presence and absence of actively transported monosaccharides. Ileal enterocyte Na,K-ATPase and K-pNPPase activities were significantly increased, as was active sodium efflux. In contrast to controls, the presence of monosaccharides produced a stimulation of active sodium efflux from ileal enterocytes derived from infected rats. Enzyme and sodium transport changes in the jejunal enterocytes probably reflect cellular immaturity. Functional changes in ileal enterocytes probably represent a compensatory phenomenon.

Animals↗
PubMed1976

Polyisoprenoid glycolipids involved in glycoprotein biosynthesis.

Until five years ago, it was believed that the oligosaccharide chains of most, if not all, glycoproteins were assembled by the stepwise transfer of single sugar residues from their nucleotide derivatives to growing oligosaccharide chains attached to a polypeptide core. It is now becoming widely accepted that polyisoprenol-linked mono- and oligosaccharides function as activated glycosyl carriers in the biosynthesis of some glycoproteins in animal tissues. The lipophilic glycosyl carrier of monosaccharides is the phosphomonoester of dolichol, the C(80-100)-polyisoprenol, containing a saturated terminal isoprene unit. In this biosynthetic process, sugars are initially transferred to dolichol monophosphate from their nucleotide derivatives by membrane-associated glycosyltransferases. These dolichol-linked monosaccharides serve as glycosyl donors in the glycosylation of oligosaccharide phospholipids. It appears likely that dolichol is also the lipid moity of the oligosaccharide intermediates. Detailed enzymatic studies with oligosaccharide phospholipids formed by rat liver, a mouse myeloma tumor and hen oviduct have revealed that these intermediates function as oligosaccharide donors in the assembly of at least one class of glycoproteins. The exact nature of the glycoproteins glycosylated by lipid intermediates and the sub-cellular site(s) of this assembly process remain to be established. The possibility, that the mannose and GlcNAc-containing core found in many glycoproteins, is assembled at the lipid-level is now being investigated. At the current rate of progress in this area of research, the identity of the glycoproteins glycosylated via lipid intermediated and the subcellular site of this assmebly process will soon be known.

Acetylglucosamine↗
PubMed1982

Membrane transport during erythroid differentiation.

Transport, unidirectional flux, of a monosaccharide, a nucleoside and three amino acids, all of which enter cells by independent, discrete carriers, was compared at three stages of erythroid maturation, the normal (anucleate) mouse erythrocyte, and in differentiated and undifferentiated Friend erythroleukemia cells. We found specific transport alterations during this developmental program. Transport of 3-O-methylglucose increased with each successive developmental stage. Aminoisobutyrate transport was maintained during Friend cell differentiation, but fell slightly in erythrocytes. Leucine, lysine and uridine transport began to fall two days after dimethylsulfoxide exposure, and diminished further in red cells. These studies of transport are not directly comparable to uptake studies reported by others. Median cell volume and thus surface area decreased more during differentiation than amino acid transport declined, so flux, transport past a unit area of membrane, actually increased. Monosaccharide flux also increased. Only uridine transport fell in parallel to surface area. Perhaps sites for nutrient transport required for energy production are preferentially maintained.

Aminoisobutyric Acids↗
PubMed1975

D-glucose permeability of black lipid membranes modified by human erythrocyte membrane fractions.

The D-glucose permeabilities of bimolecular lipid membranes formed from egg lecithin, cholesterol and human erythrocyte membrane fractions obtained using several fractionation procedures have been measured in order to assess their monosaccharide transport activity. The electrical properties of the bilayers containing the membrane fractions have also been measured and the bilayer thicknesses calculated. The observed D-glucose permeability coefficients are several orders of magnitude lower than that of the human erythrocyte membrane, indicating that none of the membrane fractions possessed significant glucose carrier activity. It is concluded that more refined techniques for incorporating membrane fractions into BLMs will be necessary before the monosaccharide transport system can be simulated in vitro.

Animals↗