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PubMed1996

Isolation, biochemical and immunological characterisation of two sea urchin glycoproteins bearing sulphated poly(sialic acid) polysaccharides rich in N-glycolyl neuraminic acid.

Two different sialoproteins were isolated from the sea urchin shell by guanidine hydrochloride extraction in the presence of Triton X-100. The sialoproteins (SP I and SP II) were purified on DEAE-Sephacel and Sepharose CL-6B and separated from each other by density gradient centrifugation. The ratio between recovered SP I and SP II was 1:4.5 and their M(r)s 650 and 600 kDa, respectively. They were degraded by neuraminidase, endoglycosidase F and peptide N-glycosidase F resulting in fragments of similar relative molecular mass (M(r)s). Although their protein cores have approximately the same relative molecular mass of 500 kDa, they differ markedly in their contents of aspartic acid/asparagine, glycine, leucine and phenylalanine, as well as in the primary amino acid sequence of their N-terminal peptides. Carbohydrate analyses showed that the sialic acid content was higher in SP I (11.4% of dry tissue weight) than in the more prominent SP II (5.3%). Two types of carbohydrates, O-glycosidically-linked polysaccharides and N-glycosidically-linked oligosaccharides are present in both sialoproteins. SP I contains 10-11 polysaccharide chains whereas SP II contains 5-6. The polysaccharides are linked to protein cores via galactosamine, have approximately the same M(r) of 12 kDa and contain 32-33 N-glycolyl neuraminic acid, 10-11 glucosamine, 6-7 sulphate and 6-8 neutral monosaccharide residues. Sialic acid residues are organized in a poly(sialic acid) unit which is present in the non-reducing terminal of the polysaccharides and degraded by neuraminidase. Hexosamines, sulphates and neutral monosaccharides are all constituents of the sialic acid free region of the chain near the reducing end. Two oligosaccharide populations were isolated from SP I, one major (70% of the total oligosaccharides) with M(r) of approximately 3 kDa and the other with M(r) of 1.5 kDa. In SP II, however, only a 3-kDa oligosaccharide population was present. The oligosaccharides from both sialoproteins are N-glycosidically linked to asparagine via the glucosamine and contain mannose, glucosamine, galactosamine and sialic acids. Antibodies against SP II were raised in rabbits and it was shown that the antigenicity of SP II was lost on either neuraminidase or trypsin digestion, indicating that both the poly(sialic acid) units of the polysaccharide and the protein core are antigenically active. As expected, SP II showed considerable cross-reactivity with SP I due to the common poly(sialic acid) structure. There were no significant reactivities of SP II and SP I with antibodies to bovine bone sialoprotein and osteopontin. The biological role of the two sea urchin sialoproteins as developmentally regulated products of the tissue remains to be elucidated.

Amino Acid Sequence↗
PubMed1990

A new sialic acid analogue, 9-O-acetyl-deaminated neuraminic acid, and alpha -2,8-linked O-acetylated poly(N-glycolylneuraminyl) chains in a novel polysialoglycoprotein from salmon eggs.

A new polysialoglycoprotein, designated PSGP(On), was isolated from the unfertilized eggs of the kokanee salmon, Oncorhynchus nerka adonis. 400-MHz 1H NMR analyses showed the O. nerka adonis PSGP contained alpha -2,8-linked oligo- and polysialic acid (polySia) chains that were made up of 4-O-Ac-, 7-O-Ac-, and 9-O-Ac esters of N-glycolylneuraminic acid (Neu5Gc) residues. The presence of a new sialic acid derivative, identified by 1H NMR as 9-O-acetyl-2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (trivial name, 9-O-acetyldeaminated neuraminic acid; 9-O-Ac-KDN), was also shown to be present as a minor component. The O-acetylated KDN residues appear to cap the nonreducing termini of the O-acetylated poly(Neu5Gc) chains. The O-acetylated polySia chains were resistant to depolymerization by bacterial exosialidases and a bacteriophage-derived endo-N-acylneuraminidase that is specific for catalyzing the hydrolysis of alpha -2,8-linkages in polySia containing either N-acetylneuraminic acid or Neu5Gc residues. After de-O-acetylation by mild alkali, the polySia chains were sensitive to digestion by endo-N-acylneuraminidase, yet partially resistant to exosialidase. These data confirm the alpha -2,8-ketosidic linkage in these chains and the nonreducing terminal location of the KDN residues. These results extend further the range of structural diversity in polySia-containing glycoconjugates, and in the family of naturally occurring sialic acids. They also suggest that the O-acetylated Neu5Gc and 9-O-Ac-KDN residues may have an important role during oogenesis.

Amino Acids↗
PubMed2002

Biological properties of N-acyl and N-haloacetyl neuraminic acids: processing by enzymes of sialic acid metabolism, and interaction with influenza virus.

Several unnatural N-acyl neuraminic acids (N-propionyl, N-hexanoyl, N-benzoyl, N-trifluoroacetyl, N-chloroacetyl, N-difluoroacetyl) were prepared enzymatically using immobilised sialic acid aldolase. N-Trifluoroacetyl-, N-chloroacetyl- and N-difluoroacetyl neuraminic acids were shown to enhance up to 10-fold the rate of association of influenza virus A to a sialoglycolipid neomembrane by surface plasmon resonance, and were found to act as weak inhibitors (K(iapp) 0.45-2.0 mM) of influenza virus neuraminidase. The N-propionyl, N-chloroacetyl- and N-difluoroacetyl neuraminic acids were found to be substrates for recombinant Escherichia coli CMP sialate synthase, to give the corresponding CMP-N-acyl-neuraminic acids. CMP-N-propionyl neuraminic acid was found not to be a substrate for CMP-N-acetyl neuraminic acid hydroxylase from pig submandibular gland.

Animals↗
PubMed1998

Further characterization of equine brain gangliosides: the presence of GM3 having N-glycolyl neuraminic acid in the central nervous system.

Equine brain gangliosides were isolated and their structures were characterized, to examine whether equine brain has N-glycolyl neuraminic acid in gangliosides, since other mammals predominantly possess N-acetyl neuraminic acid in brain gangliosides, and equine erythrocytes and organs except the brain have gangliosides exclusively containing N-glycolyl neuraminic acid. The gangliosides purified from the brain were identified by proton NMR spectroscopy and mass spectrometry, as well as GLC, resulting in their identification as GM4, GM3, GM2, GM1, GD1a, GD1b, and GT1b. Of these gangliosides, GM3 possessed N-glycolyl neuraminic acid as a minor component (18% of the total GM3), whereas other gangliosides exclusively contained N-acetyl neuraminic acid. The N-glycolyl neuraminic acid residue of the GM3 was confirmed by TLC immunostaining. The possibility of contamination of the GM3 by erythrocytes was eliminated based on the finding that the lipid compositions were characteristic of brain gangliosides. The presence, even as a minor component, of the N-glycolyl neuraminic acid in equine brain gangliosides is exceptional among the sialic acid species in mammalian central nervous system.

Animals↗
PubMed1986

[Value of neuraminic acid as a clinical parameter in 42 patients with small-cell bronchial cancer].

The serum concentrations of neuraminic acid, CEA, gamma-Gt, 5-nucleotidase, haptoglobin, and alkaline phosphatase were determined before therapy and three and six months after the initiation of therapy in 42 patients with small cell bronchial carcinomas. Before therapy, a significantly increased serum concentration as compared to normal values was found for neuraminic acid in 97% of patients (43/44), for CEA in 54.7% (23/42), for gamma-Gt in 19% (8/42), for 5-nucleotidase in 11.9% (5/42), for haptoglobin in 36.3% (14/44), and for alkaline phosphatase in 9.5% of all patients (4/42). Three and six months later, these laboratory investigations did not give any valuable hint with respect to therapy results, with the exception of neuraminic acid (p less than 0.05). Prior to therapy, the concentrations of neuraminic acid were considerably increased in patients (mean = 3.16 +/- 0.47 mumol/ml) with regard to normal values (mean = 1.90 +/- 0.14 mumol/ml). Within the total group of 42 patients suffering from small cell bronchial carcinomas, there was no significant difference between the serum concentrations of neuraminic acid of eleven patients with localized tumors (mean = 3.12 +/- 0.53) and those of 31 advanced tumor patients (mean = 3.16 +/- 0.45) (p less than 0.05). During the six months' treatment period, the concentration of neuraminic acid was valuable as clinical parameter in 36 patients, i.e. 85% of all cases (0.001 less than p less than 0.01). It was shown that the serum concentration of neuraminic acid indicated a regression of the disease in 23 patients (p less than 0.001), a progression in 8 patients (0.02 less than p less than 0.05), and a regression with subsequent progression of the tumor in 5 patients (0.001 less than p less than 0.01).

Adult↗
PubMed1993

Methyl alpha-glycoside of N-thioacetyl-D-neuraminic acid: a potential inhibitor of influenza A virus. A 1H NMR study.

The binding of influenza A virus hemagglutinin to its cell surface receptor, alpha-linked 5-N-acetylneuraminic acid (sialic acid), was studied in solution. The effect of structural modifications introduced into the N-acetyl group of the sialic acid on the binding was monitored by determining the dissociation constants by proton nuclear magnetic resonance (1H NMR) spectroscopy. Methyl alpha-glycoside of N-thioacetylneuraminic acid showed high, whereas the corresponding N-methylcarbamoylneuraminic acid exhibited relatively low binding affinity towards the hemagglutinin.

Electrophoresis, Polyacrylamide Gel↗
PubMed1991

CMP-N-acetylneuraminic acid synthetase of Escherichia coli: high level expression, purification and use in the enzymatic synthesis of CMP-N-acetylneuraminic acid and CMP-neuraminic acid derivatives.

The gene encoding CMP-N-acetylneuraminic acid (CMP-NeuAc) synthetase (EC 2.7.7.43) in Escherichia coli serotype O7 K1 was isolated and overexpressed in E.coli W3110. Maximum expression of 8-10% of the soluble E.coli protein was achieved by placing the gene with an engineered 5'-terminus and Shine-Dalgarno sequence into a pKK223 vector derivative behind the tac promoter. The overexpressed synthetase was purified to greater than 95% homogeneity in a single step by chromatography on high titre Orange A Matrex dye resin. Enzyme purified by this method was used directly for the synthesis of CMP-NeuAc and derivatives. The enzymatic synthesis of CMP-NeuAc was carried out on a multigram scale using equimolar CTP and N-acetylneuraminic acid as substrates. The resultant CMP-NeuAc, isolated as its disodium salt by ethanol precipitation, was prepared in an overall yield of 94% and was judged to be greater than 95% pure by 1H NMR analysis. N-Carbomethoxyneuraminic acid and N-carbobenzyloxyneuraminic acid were also found to be substrates of the enzyme; 5-azidoneuraminic acid was not a substrate of the enzyme. N-Carbomethoxyneuraminic acid was coupled to CMP at a rate similar to that observed with NeuAc, whereas N-carbobenzyloxyneuraminic acid was coupled greater than 100-fold more slowly. The high level of expression achieved with the E.coli synthetase, together with the high degree of purity readily obtainable from crude cell extracts, make the recombinant bacterial enzyme the preferred catalyst for the enzymatic synthesis of CMP-N-acetylneuraminic acid.

Amino Acid Sequence↗
PubMed1988

Generation of two murine monoclonal antibodies that can discriminate N-glycolyl and N-acetyl neuraminic acid residues of GM2 gangliosides.

Since the preliminary analyses of the glycolipids of small cell carcinomas of the lung showed an increase of GM2 ganglioside, we generated new murine monoclonal antibodies directed to GM2 to identify the molecular species of the glycolipid. The monoclonal antibodies MK2-34 and MK1-16 (both IgM), which specifically detect N-glycolyl GM2 and N-acetyl GM2, respectively, were generated by immunizing mice with liposomes containing monophosphoryl lipid A, trehalose dimycolate, and the antigenic ganglioside. Among the glycolipid preparations extracted from the cancer tissues of 39 patients with lung cancer, a significant amount of N-acetyl GM2 was detected with MK1-16 antibody in 70% of the squamous cell carcinoma cases, 50% of the lung adenocarcinoma cases, 33% of the large cell carcinoma cases, and 100% of the cases of small cell carcinoma of the lung. On the other hand, N-glycolyl GM2 which was defined by the monoclonal MK2-34 was not found in any of the glycolipid fractions prepared from the lung cancer tissues examined in this study. Immunohistochemical studies of the lung cancer tissues with the MK1-16 antibody showed that the N-acetyl GM2 was present not only in small cell carcinoma tissues as one of the antigens related to tumors of neuroectodermal origin, but also in the squamous cell carcinoma and adenocarcinoma of the lung with a comparable frequency. The appearance of the N-acetyl GM2 antigen correlated well with the degree of differentiation of the cancer cells in patients with squamous cell carcinoma and adenocarcinoma of the lung.

Animals↗