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PubMed1976

Effects of uridine nucleotides and nucleotide pyrophosphatase on glycolipid alpha and beta-N-acetylgalactosaminyltransferase activities in guinea pig microsomes.

Membrane-bound alpha and beta-N-acetylgalactosaminyltransferases (EC 2.4.1.0) which catalyze formation of non-reducing terminal linkages of Forssman hapten and globoside, respectively, could be differentiated with respect to the different effects of UDP on the two enzyme activities. UDP markedly inhibited the alpha-transferase activity, in contrast to its stimulatory action on the beta-transferase. These effects of UDP were similar to those of UDPglucose, which was demonstrated to be a competitive inhibitor (Ki, 3.3 - 10(-5) M for UDP-N-acetylgalactosamine) for the alpha-transferase reaction. Other uridine derivatives tested suppressed both the transferase activities, being more inhibitory for the alpha-transferase than for the beta-transferase. Under the synthetic conditions of these aminoglycolipids, UDP-N-acetylgalactosamine as a donor was simultaneously degraded into N-acetylgalactosamine-1-phosphate and finally into N-acetylgalactosamine by UDP-N-acetylgalactosamine pyrophosphatase, which is part of the membrane system. UDPglucose was confirmed as being able to prevent the enzymatic hydrolysis of UDP-N-acetylgalactosamine. UDPglucose, therefore, acts to suppress both the alpha-N-acetylgalactosaminyltransferase (but not the beta-transferase) and the pyrophosphatase activities. The inhibitory effect of UDPglucose on the alpha-transferase activity was most probably due to its direct action on the transferase rather than its function in protecting UDP-N-acetylgalactosamine donor from pyrophosphatase action.

Animals↗

PubMed1978

Hydrolysis of sugar nucleotides in chicken egg white in response to embryonic development.

The egg white of newly laid chicken egg was found to contain about 45 mumol of UDP-N-acetylgalactosamine 4-sulfate, 34 mumole of GDP-mannose, 6 mumol of UDP-N-acetylhexosamine, and 1 mumol of UDP-N-acetylgalactosamine 4,6-bissulfate per liter. There was no significant difference between infertile and fertile eggs in the initial levels of the sugar nucleotides. During incubation for 4 days, the nucleotide levels in infertile eggs showed little change while those in fertile eggs fell continuously until the complete disappearance of the nucleotides on the fourth day. Initial removal of the blastoderm from fertile eggs resulted in cessation of the reduction in nucleotide levels in the 2- to 4-day period after the operation. The decrease of UDP-N-acetylgalactosamine 4-sulfate was followed by an increase of 1-phospho-N-acetylgalactosamine 4-sulfate then N-acetylgalactosamine 4-sulfate in the egg white. When UDP-N-acetylgalactosamine 4-[35S]sulfate or GDP-[14C]mannose was injected into the egg white of a fertile egg, the main feature of the metabolism of the labeled compounds was the successive hydrolysis of their pyrophosphate and phosphate bonds, with the formation of sugar 1-phosphate and sugar. A significant activity of nucleotide pyrophosphatase was detected in the egg white in newly laid eggs (0-day egg). However, no such activity could be detected in egg-white specimens from 1-, 2-, and 3-day eggs. The results suggest that although the decrease of sugar nucleotides in the first day could be ascribed to the hydrolytic action of the enzyme originally present in the egg white, the decrease in the subsequent 3 days results from a more complex process in which the hydrolysis of the sugar nucleotides is related to the development of the embryo.

Acetylgalactosamine↗

PubMed1976

Dermatan sulfate-chondroitin sulfate copolymers from ambilical cord. Isolation and characterization.

Dermatan sulfate-chondroitin sulfate copolymers have been isolated from human umbilical cord as a major galactosaminoglycan component of this tissue. The galactosaminoglycan fraction was obtained from this tissue by papain [EC 3.4.22.2] digestion followed by precipitation with cetylpyridinium chloride in a yield of 700 mg per 100 g of dry tissue. Ethanol fractionation resolved 4-5 subfractions differing in relative content of L-iduronic acid and D-glucuronic acid. No galactosaminoglycan containing either solely L-iduronic acid or D-glucuronic acid was obtained. The copolymeric structure of the material in each subfraction was demonstrated by analysis of oligosaccharide fragments obtained by chondroitinase-AC [EC 4.2.2.5] digestion. All the polymers contained repeating disaccharide units, D-glucuronosyl-N-acetylgalactosamine, D-glucuronosyl-N-acetylgalactosamine 4-sulfate, D-glucuronosyl-N-acetyl-galactosamine 6-sulfate, and L-iduronosyl-N-acetylgalactosamine 4-sulfate, of which D-glucuronosyl-N-acetylgalactosamine 6-sulfate and L-iduronosyl-N-acetylgalactosamine 4-sulfate were predominant. Both iduronic acid- and glucuronic acid-containing units were arranged in clusters. The presence of a considerable amount of nonsulfated disaccharide units was noted. The copolymers show extensive polydispersity in electrophoresis on cellulose acetate and gel chromatography on Sephadex G-200.

Amino Acids↗

PubMed1979

The effect of tunicamycin on the glycosylation of lactating-rabbit mammary glycoproteins.

1. Tunicamycin inhibited the incorporation of d-[2-(3)H]mannose into dolichol-linked oligosaccharide and glycoprotein of lactating-rabbit mammary explants by approximately the same extent (approx. 30% of control value), suggesting that lipid-linked intermediates are involved in the mannosylation of mammary glycoproteins. 2. The incorporation of radioactivity from N-acetyl-d-[1-(14)C]glucosamine into dolichol-linked oligosaccharide was inhibited by tunicamycin to 32% of the control value, whereas the incorporation of the radiolabel into glycoprotein was only inhibited to 72% of the control value. 3. Considerable redistribution of label from N-acetylglucosamine to N-acetylgalactosamine was found to occur in the explants. In the presence of tunicamycin approx. 76% of the radioactivity incorporated into glycoprotein from N-acetyl-d-[1-(14)C]glucosamine was present as N-acetylgalactosamine, compared with approx. 61% in the absence of the inhibitor. Thus tunicamycin selectively inhibits the incorporation of N-acetylglucosamine into glycoprotein. 4. Radioactivity from N-acetyl-d-[1-(14)C]glucosamine was incorporated into a glycoprotein that was identified as casein by the use of a casein-specific antiserum, and also into a group of glycopolypeptides with apparent mol.wts. ranging between 40000 and 80000. N-Acetylgalactosamine was the only radioactive sugar released on strong-acid hydrolysis of the immunoprecipitated casein, whereas N-acetylglucosamine was the major radioactive residue present in the non-casein glycoproteins. Glucosamine and galactosamine were the only radiolabelled sugars detected by paper chromatography of the strong-acid hydrolysate of the protein fraction. 5. Tunicamycin inhibited the incorporation of radioactivity from N-acetyl-d-[1-(14)C]glucosamine into the glycopolypeptides with mol.wts. between 40000 and 80000 as described by polyacrylamide-gel electrophoresis, but did not affect the incorporation of label into casein. It appears that tunicamycin inhibits the incorporation of mannose and N-acetylglucosamine into a number of mammary glycoproteins by inhibiting the formation of lipid-linked intermediates, but does not inhibit the incorporation of N-acetylgalactosamine into casein.

Acetylgalactosamine↗

PubMed1977

Biochemical investigations of retinotectal adhesive specificity.

The preferential adhesion of chick neural retina cells to surfaces of intact optic tecta has been investigated biochemically. The study uses a collection assay in which single cells from either dorsal or ventral halves of neural retain adhere preferentially to ventral or dorsal halves of optic tecta respectively. The data presented support the following conclusions: (a) The adhesion of ventral retina to dorsal tecta seems to depend on proteins located on ventral retina and on terminal beta-N-acetylgalactosamine residues on dorsal tecta. (b) The adhesion of dorsal retina to ventral tecta seems to depend on proteins located on ventral tecta and on terminal beta- N-acetylgalactosamine residues on dorsal retina. (c) A double gradient model for retinotectal adhesion along the dorsoventral axis is consistent with the data presented. The model utilizes only two complementary molecules. The molecule suggested to be concentrated dorsally in both retina and tectum seems to require terminal beta-N-acetylgalactosamine residues for adhesion. Its activity is not affected by protease. A molecule fitting these qualifications, the ganglioside GM(2), could not be detected in a gradient, but lecithin vesicles containing GM(2) adhered preferentially to ventral tectal surfaces. The second molecule, concentrated ventrally in both retina and tectum, is a protein and seems capable of binding terminal beta-N- acetylgalactosamine residues. One enzyme, UDP-galactose:GM(2) galactosyltransferase, has been found to be more concentrated in ventral retina than dorsal, but only by 30 percent.

Acetylgalactosamine↗

PubMed1979

A pathway of polygalactosamine formation in Aspergillus parasiticus: enzymatic deacetylation of N-acetylated polygalactosamine.

1. An enzyme which hydrolyzes the acetamido groups of N-acetylgalactosamine residues in N-acetylated polygalactosamine was found in the supernatant fraction of Aspergillus parasiticus AHU 7165, a polygalactosamine-producing strain. 2. N-Acetylated polygalactosamine was used as a substrate in the purification and characterization of this enzyme. A 140-fold purification was obtained by means of ammonium sulfate fractionation followed by chromatography on carboxymethylcellulose and DEAE-cellulose. 3. The enzyme releases about 60-70% of the acetyl groups of N-acetylated polygalactosamine, giving a product with free amino groups. Whereas the enzyme also deacetylates oligosaccharides with 14 or more N-acetylgalactosamine units at a rate similar to that of deacetylation of the polymer, it deacetylates shorter oligosaccharides (trimer to hexamer of N-acetylgalactosamine) much more slowly and is virtually inactive toward disaccharide. Deacetylation can not be detected with bacterial cell wall peptidoglycan, N-acetylated heparin, partially O-hydroxyethylated chitin or monomeric N-acetylgalactosamine derivatives as substrates. 4. This enzyme shows double pH optima of 5.3 and 9.3. The Km value for N-acetylated poly-galactosamine is 0.15 g/l (or 0.54 mM with respect to monosaccharide residues). 5. The occurrence of this enzyme may account for the formation of polygalactosamine with free amino groups.

Acetylgalactosamine↗

PubMed1979

Production of monoclonal antibodies specific for two distinct steric portions of the glycolipid ganglio-N-triosylceramide (asialo GM2).

Two hybrid cell lines were prepared by the fusion of mouse myeloma cells with the spleen cells of BALB/c mice that had been immunized with the glycolipid ganglio-N-triosylceramide (asialo GM2). The specificity of the monoclonal antibodies produced by these hybridomas, one an IgM and the other an IgG3, has been defined by hemagglutination inhibition, complement fixation, and lysis of glycolipid liposomes by antibody and complement. A major determinant recognized by the IgM antibody is the nonreducing terminal N-acetylgalactosamine including the C6 primary hydroxyl group, but excluding the C2-acetamide group of N-acetylgalactosamine, because oxidation with galactose oxidase produced a structure showing only minimal cross-reaction with the IgM but replacement of the N-acetyl group with an N-n-butyryl group produced a glycolipid that reacts with IgM antibody to the same extent as with the unmodified glycoplipd. A major determinant recognized by the IgG3 antibody is the terminal N-acetylgalactosamine including the C2-acetamido group, but excluding the C6 primary hydroxyl group of N-acetylgalactosamine, because replacement of the N-acetyl group with an N-n-butyryl group produced a glycolipid that did not react with the IgG3 antibody; in striking contrast the IgG3 antibody reacted with the C6-oxidized glycolipid as well as with the native glycolipid. Neither antibody reacted significantly with any other natural glycolipids tested including several that are structurally related to asialo GM2 such as ganglioside GM2, ganglio-N-tetraosylceramide (asialo GM1), or ceramide dihexoside. These results indicated that in addition to the fine structure specificity described above both antibodies recognize the nonreducing terminal GalNAc beta 1 leads to 4Gal structure. The strict antigenic specificity of these monoclonal anti-glycolipid antibodies indicates their great potential as specific probes for cell surface studies.

Animals↗

PubMed1978

Composition and synthesis of three higher ganglioside homologs in bovine mammary tissue.

Three higher gangliosides were identified as constituents of bovine mammary gland. The structures of these three gangliosides were shown to be ceramide-glucose-galactose-(sialic acid)-N-acetylgalactosamine-galactose, ceramide-glucose-galactose-(sialic acid)2-N-acetylgalactosamine, and ceramide-glucose-galactose-(sialic acid)2-N-acetylgalactosamine-galactose. These gangliosides accounted for only a small fraction (less than 20%) of the lipid-bound sialic in mammary gland. White fatty acids with even carbon numbers from C14 to C26 were predominant in these gangliosides, they also contained C23 and C25 fatty acids. Mammary gland Golgi apparatus-rich fractions had all glycosyltransferases required for synthesis of these gangliosides starting with ceramide.

Animals↗

PubMed1979

Structural studies on the carbohydrate units of armadillo submandibular glycoprotein.

The structure of carbohydrate units of the major glycoprotein fraction of armadillo submandibular gland was investigated. Alkaline borohydride reductive cleavage of the glycoprotein resulted in the release of O-glycosidically linked mono- and disaccharide units. The monosaccharide was identified as N-acetylgalactosaminitol, whereas disaccharide contained of N-acetylneuraminic acid and N-acetylgalactosaminitol. Treatment of the native and desialyzed glycoprotein with alpha-N-acetylgalactosaminidase resulted in the removal of 60% and 96% of N-acetylgalactosamine, respectively. No cleavage of this sugar was affected by the action of beta-N-acetylhexosaminidase. Both N-acetylgalactosamine and N-acetylneuraminic acid were susceptible to oxidation with periodate. Analyses of the partially methylated N-acetylgalactosamine derivatives, obtained from the permethylated native glycoprotein, showed the presence of 3,4,6-tri-O-methyl-N-methylacetamidogalactose and 3,4-di-O-methyl-N-methylacetamidogalactose in a ratio of 1 : 0.4. Only 3,4,6-tri-O-methyl-N-methylacetamidogalactose was found in the hydrolysates of permethylated desialyzed glycoprotein. These results together with our previous data on chemical composition of the glycoprotein suggest that about 30% of the oligosaccharide chains consist of NeuAc alpha 2 leads to 6GalNAc alpha 1 leads to O-Thr(Ser) and 70% of GalNAc alpha leads to O-Thr(Ser).

Animals↗

PubMed1978

A sensitive procedure for the diagnosis of N-acetyl-galactosamine-6-sulfate sulfatase deficiency in classical Morquio's disease.

The trisaccharide 6-sulfo-N-acetylgalactosamine-glucuronic acid-6-sulfo-N-acetyl-[1-3H]galactosaminitol was used as a substrate for the determination of N-acetylgalactosamine-6-sulfate sulfatase activity. The amount of liberated sulfate was measured indirectly by separating monosulfated reaction products from the substrate on Dowex 1 X 2 microcolumns in a simple two step procedure. Fibroblast homogenates from patients with various genotypes, except classical Morquio's disease, released 410 +/- 90 pmol sulfate/h/mg cell protein. The enzyme exhibited a pH optimum of pH 4.8 and a KM of about 1 X 10(-4) mol/1. It was strongly inhibited by phosphate, sulfate and chloride ions. In three cell lines from patients with classical Morquio's disease a residual activity between 1 and 2% of the mean normal activity was found. All cell lines tested released sulfate from 6-sulfo-N-acetylglucosamine-glucuronic acid-[1-3H]-anhydromannitol. Cell extracts from cultured amniotic fluid cells exhibited a N-acetylgalactosamine-6-sulfate sulfatase activity between 120 and 320 pmol/h/mg protein. An enzyme activity of 370 +/- 100 pmol sulfate/h/mg protein was found in peripheral leucocytes from healthy donors. The determination of N-acetyl-galactosamine-6-sulfate sulfatase activity in one family with an affected patient indicated that the enzyme deficiency is also expressed in leucocytes.

Amniotic Fluid↗

PubMed1979

Enzymic O-glycosylation of synthetic peptides from sequences in basic myelin protein.

Nine synthetic peptides containing sequences in the region of a threonine residue at position 98 of bovine basic myelin protein were prepared by the Merrifield solid-phase method and tested for their ability to be glycosylated with [14C]uridinediphospho-N-acetylgalactosamine and a crude detergent-solubilized preparation of uridinediphospho-N-acetylgalactosamine:mucin polypeptide N-acetylgalactosaminyltransferase obtained from porcine submaxillary glands. The tetrapeptide Thr-Pro-Pro-Pro and all larger peptides containing this sequence were glycosylated. The glycosylation was greater for peptides containing residues N-terminal to the Thr-Pro-Pro-Pro. Under the conditions used, the peptide Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro was glycoslyated twice as much as bovine basic myelin protein. Thr-Pro and Thr-Pro-Pro, as well as 10 other synthetic peptides which did not contain the Thr-Pro-Pro-Pro sequence, were not glycosylated. Treatment of the glycopeptide of Phe-Lys-Asn-Leu-Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro-Ser with an alpha-N-acetylgalactosaminidase released N-acetylgalactosamine from the peptide, indicating that the hexosamine was covalently bonded to the peptide in an alpha linkage.

Amino Acid Sequence↗

PubMed1975

Immunochemical and chemical studies on streptococcal group-specific carbohydrates.

Structural studies on the carbohydrates of Groups A, C, and A-variant (AV) streptococci have utilized periodate oxidation, permethylation analysis, and immunochemical comparison of intact and periodate-oxidized polysaccharides. The data indicate that a similar 1,2- and 1,3-linked rhamnose chain is present in both the A and AV carbohydrates. The group A carbohydrate contains in addition N-acetylglucosamine residues at nonreducing terminals, whereas the AV is a homopolymer of rhamnose. There is some evidence that Group Ccarbohydrate contains the same rhamnose chain, but structural comparisons to the A and AV carbohydrates are complicated by the presence of intrachain N-acetylgalactosamine residues. Periodate oxidation and permethylation analysis show that while approximately 50% of the N-acetylgalactosamine of the Group C carbohydrate occupies terminal positions, the remainder is present as 1,3-linked units. Removal of the nonreducing terminal hexosamine units from the Group A carbohydrate by periodate treatment significantly enhanced its cross-reactivity with AV antiserum, whereas no enhancement was observed after similar treatment of the Group C carbohydrate. The data indicate the presence of an alpha-1,3-linked N-acetylgalactosamine disaccharide at the nonreducing terminal of the Group C carbohydrate.

Amino Acids↗

PubMedDate not supplied

Isolation, characterization and nature of carbohydrate-peptide linkage of an alkali-extractable non-collagenous glycoprotein from albino rat skins.

A glycoprotein was isolated from young albino rat skins by alkali extraction under mild conditions and purified by Sephadex G-200 and DEAE-Sephadex A-50 chromatography. It was found to be homogeneous by agar gel electrophoresis. It had a molecular weight of approximately 90,000 and contained galactose, mannose, fucose, N-acetylglucosamine, N-acetylgalactosamine and sialic acids as its carbohydrate constituents. The release of sialic acids from the glycoprotein by neuraminidase indicated their terminal positions in the carbohydrate chains. The glycoprotein lacked hydroxyproline which indicates its non-collagenous nature. The treatment of the glycoprotein with alkaline borohydride resulted in the decrease of threonine, serine and N-acetylgalactosamine contents. The presence of O-glycosidic linkage of N-acetylgalactosamine with serine and threonine is therefore suggested.

Amino Acids↗

PubMed1978

The isolation and partial characterization of the major bronchial glycoproteins.

Partial characterization of glycoprotein obtained from mucous secretion of the bronchi and stomach has been attempted. The isolated glycoproteins and the glycoproteins from gastric aspirates showed similar carbohydrate and amino-acid composition. They consist of a protein core to which are attached carbohydrate side chains of galactose, N-acetylglucosamine and N-acetylgalactosamine in the ratio of 4 : 3 : 1. Superimposed on this structure were additional sugar residues, the blood group determinants. The carbohydrate side chains are linked by an alkali-labile O-glycosidic linkage to the threonine and serine residues of the protein core, with N-acetylgalactosamine forming the link.

Acetylgalactosamine↗

PubMed1978

Site of synthesis, intracellular transport and secretion of glycoprotein in exocrine cells.

The site of attachment of the first sugar, N-acetylgalactosamine, to the seryl and threonyl residues of the protein chain is unknown in exocrine cells. The subsequent sugars of the carbohydrate side chains, galactose and N-acetylglucosamine alternately, and the end-group sugars, galactose, N-acetylgalactosamine and fucose, are attached in the Golgi complex. Sulphate too is attached in that structure. In the stomach, sulphate is probably transferred in the most mature cisterna of the Golgi stacks, galactose and fucose in other cisternae, suggesting a gradient in transferase activities along the stack. The possibilities of regulating the amount and relative sugar composition of the glycoproteins are discussed. The secretory product is stored in granules. Their polygonal, large and swollen appearance and complex formation by loss of bordering membranes, as observed in many kinds of glycoprotein-secreting cells ('mucous cells') might be caused by ineffective fixation techniques. Direct vascular perfusion results in a picture no different from what is found in non-mucous cells. Whether secretion is merely exocytotic, as in non-mucous cells, or whether it is accompanied by a loss of membrane and even cytoplasm needs thorough investigation, with the effects of various fixation techniques being compared.

Acetylgalactosamine↗

PubMed1979

Characterization of the sulfated glycosaminoglycan on the surface and in the storage granules of rabbit platelets.

Rabbit platelets were labeled in vivo with 35S for characterization of platelet sulfated glycosaminoglycan. When rabbit platelets were aggregated by ADP, sulfated proteoglycan was lost from the platelet surface although no release of granule contents occurred. The sulfated proteoglycan contained in the granules of platelets pretreated with ADP was subsequently released by treatment with thrombin. The 35S-labeled proteoglycan from both sources was isolated by gel filtration and the glycosaminoglycan portion of the proteoglycan was characterized as chondroitin 4-sulfate by examining the products of digestion with hyaluronidase, chondroitinase AC and ABC, and chondro-4- and 6-sulfatases; by identification of the hexosamine as N-acetylgalactosamine; by determination of a 1 : 1 : 1 molar ratio of N-acetylgalactosamine, uronic acid and inorganic sulfate; and by cetylpyridinium chloride cellulose chromatography. In these studies, the use of 35S-labeled proteoglycan made possible detection and quantification of much smaller amounts of material than would be possible with unlabeled material. Chondroitin 4-sulfate was the only sulfated glycosaminoglycan identified in the proteoglycan lost from the platelet surface during ADP-induced aggregation and in the proteoglycan released from the granules when the platelets were exposed to thrombin.

Acetylgalactosamine↗

PubMed1978

Immunochemical characterization of Lymantri dispar NPV hemagglutinin: protein-carbohydrate interaction.

The agglutination of chicken erythrocytes by Lymantria dispar nuclear polyhedrosis virus polyhedrin has been shown to provide specific virus identification. Selected mono- and oligosaccharides, present in blood group substances, were assayed by the Land-steiner hapten inhibition technique for specific inhibition of polyhedrin hemagglutination. N-acetylgalactosamine and N-acetylglucosamine inhibit to the greatest extent; galactosamine, glucosamine and fucose to a lesser extent. The hapten inhibition data suggest that a monosaccharide possessing an equatorial 2-acetamido group interacts most avidly with the polyhedrin-combining site. Bergold demonstrated that the polyhedrin dissociates into six subunits at a pH greater than 10.0. Diafiltration equilibrium and Scatchard analysis indicate that N-acetylgalactosamine binds most avidly to the polyhedrin (Kd = 1.7 X 10(-6)) which contains six available sites, suggesting that one hemagglutination site resides on each subunit. Since virions derived in vivo and polyhedrin are serologically cross-reactive, this protein-carbohydrate interaction may play a role in host infectivity by providing a receptor site for virus attachment to target cells.

Acetylgalactosamine↗

PubMed1977

[Effect of peptidoglycan preparations on phage inactivation: decrease in phage 187 binding using monosaccharides].

Monosaccharides were found to be capable to decreasing the binding of phage 187 with peptidoglycan. Galactosamine hydrochloride and glucosamine hydrochloride proved to be the most effective, followed in order of decreasing activity by N-acetylgalactosamine, N-acetylglucosamine, glucose and galactose; mannose produced a weak effect. Ca2+ ions increased the reduction of phage peptiglycan binding with N-acetylgalactosamine and N-acetylglucosamine. Both of these monosaccharides also reduced the adsorption of phage 187 by the Staphylococcus aureus cells. In the medium enriched with Ca2+ ions; in the absence of Ca2+, they were, however, incapable of releasing the phage irreversibly bound with the peptidoglycan.

Acetylgalactosamine↗