A new O-glycosidically linked tri-hexosamine core structure in sheep gastric mucin: A preliminary note

Hounsell, Elizabeth F.; Fukuda, Minoru; Powell, Mark; Feizi, Ten; Hakomori, Sen‐itiroh

doi:10.1016/0006-291x(80)90406-4

Cited by 41 publications

(5 citation statements)

References 26 publications

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“…In each of these cases the core A-acetylgalactosamine branch points consisted of a 3-linked galactose and a 6-linked TV-acetylglucosamine. Such structures have been known for some time to occur in mucins and blood group glycoproteins (Lloyd et al, 1968;Oates et al, 1974;Hounsell et al, 1980;Akiyama et al, 1984). The structures of the triand tetrasaccharides demonstrated in this study for the rat sialoglycoproteins have been described previously in a variety of secreted and cell surface glycoproteins including human glycophorin (Thomas & Winzler, 1969;Spiro & Bhoyroo, 1974).…”

Section: Discussionsupporting

confidence: 66%

Characterization of the O-glycosidically linked oligosaccharides of rat erythrocyte membrane sialoglycoproteins

Langenhove¹,

Reinhold²,

Weber³

1986

Biochemistry

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The carbohydrate units of the rat erythrocyte membrane sialoglycoprotein rSGP-4 [Edge, A. S. B., & Weber, P. (1981) Arch. Biochem. Biophys. 209, 697-705] have been characterized. All of the carbohydrate of this Mr 19,000 glycoprotein occurs in O-glycosidic linkage to the peptide; following alkaline borohydride treatment and chromatography on Bio-Gel P-2, sialic acid containing oligosaccharides terminating in N-acetylgalactosaminitol were obtained. Their structures were determined by compositional analysis, exoglycosidase digestions, alkaline sulfite degradation, and periodate oxidation. The oligosaccharides were characterized for molecular weight and linkage by direct chemical ionization and gas-liquid chromatography/mass spectrometry, respectively. The structures are proposed to be NeuAc alpha 2----3Gal beta 1----3GalNAc-ol, Gal beta 1----3(NeuAc alpha 2----6)GalNAc-ol, NeuAc alpha 2----3Gal beta 1----3(NeuAc alpha 2----6)GalNAc-ol, and NeuAc alpha 2----3Gal beta 1----3(NeuAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-ol. Two of the N-acetylglucosamine-containing hexasaccharides were present per molecule of rSGP-4 along with two trisaccharides and seven tetrasaccharides.

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Section: Discussionsupporting

confidence: 66%

Characterization of the O-glycosidically linked oligosaccharides of rat erythrocyte membrane sialoglycoproteins

Langenhove¹,

Reinhold²,

Weber³

1986

Biochemistry

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“…Eleven of these structures have previously been isolated from other mucin sources, in particular, cystic fibrosis bronchial mucins and ovarian cyst mucins [10,12,13,19]. Although oligosaccharide N2c has been identified as a core structure in many mucins (core-type 4) [10,17,22], the occurrence of this oligosaccharide as a distinct entity is novel. 'H n.m.r.…”

Section: Galnacolmentioning

confidence: 99%

Structural characterization of neutral oligosaccharides with blood-group A and H activity isolated from bovine submaxillary mucin

Savage

D'Arcy

Donoghue

1991

Biochemical Journal

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In this study we investigated the structures of 11 neutral oligosaccharides released from bovine submaxillary mucin by alkaline borohydride treatment and isolated by h.p.l.c. One hexa-, one penta-, three tetra-, four tri- and two di-saccharides containing core types 1, 2, 3 or 4 were obtained. We report their structures, determined by a combination of one- and two-dimensional 1H n.m.r. spectroscopy at 270 MHz and methylation analysis involving g.l.c.-m.s., along with their approximate molar ratios. Only three of these oligosaccharides have previously been reported in this source. Of the new oligosaccharides, one contains the blood-group-A antigenic determinant, two contain the blood-group-H type 2 determinant, while another contains the blood-group-H type 3 determinant. The oligosaccharide GlcNAc beta (1----6)[GlcNAc beta (1----3)]GalNAcol, although previously found as a core structure, has been isolated here as a novel trisaccharide.

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“…In these tissues, core 3 is converted to core 4 by core 4 ␤1,6-N-acetylglucosaminyltransferase (C4GnT), forming Gal␤134GlcNAc␤-136(GlcNAc␤133)GalNAc (23,24).…”

mentioning

confidence: 99%

Poly-N-acetyllactosamine Extension inN-Glycans and Core 2- and Core 4-branchedO-Glycans Is Differentially Controlled by i-Extension Enzyme and Different Members of the β1,4-Galactosyltransferase Gene Family

Ujita¹,

Misra

McAuliffe

et al. 2000

Journal of Biological Chemistry

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Poly-N-acetyllactosamines are attached to N-glycans, O-glycans, and glycolipids and serve as underlying glycans that provide functional oligosaccharides such as sialyl Lewis X . Poly-N-acetyllactosaminyl repeats are synthesized by the alternate addition of ␤1,3-linked GlcNAc and ␤1,4-linked Gal by i-extension enzyme (iGnT) and a member of the ␤1,4-galactosyltransferase (␤4Gal-T) gene family. In the present study, we first found that poly-N-acetyllactosamines in N-glycans are most efficiently synthesized by ␤4Gal-TI and iGnT. We also found that iGnT acts less efficiently on acceptors containing increasing numbers of N-acetyllactosamine repeats, in contrast to ␤4Gal-TI, which exhibits no significant change. In O-glycan biosynthesis, N-acetyllactosamine extension of core 4 branches was found to be synthesized most efficiently by iGnT and ␤4Gal-TI, in contrast to core 2 branch synthesis, which requires iGnT and ␤4Gal-TIV. Poly-N-acetyllactosamine extension of core 4 branches is, however, less efficient than that of N-glycans or core 2 branches. Such inefficiency is apparently due to competition between a donor substrate and acceptor in both galactosylation and N-acetylglucosaminylation, since a core 4-branched acceptor contains both Gal and GlcNAc terminals. These results, taken together, indicate that poly-N-acetyllactosamine synthesis in N-glycans and core 2-and core 4-branched Oglycans is achieved by iGnT and distinct members of the ␤4Gal-T gene family. The results also exemplify intricate interactions between acceptors and specific glycosyltransferases, which play important roles in how poly-Nacetyllactosamines are synthesized in different acceptor molecules.Poly-N-acetyllactosamines are unique glycans having N-acetyllactosamine repeats (Gal␤134GlcNAc␤133) n in one side chain (1). Poly-N-acetyllactosamines are attached to Nglycans (2-4), O-glycans (5-7), and glycolipids (8 -10). Poly-Nacetyllactosamines are often modified to express differentiation antigens and functional oligosaccharides. One of those oligosaccharides is sialyl Le X , 1 NeuNAc␣233Gal␤134(Fuc␣133)-GlcNAc3 R discovered in human granulocytes and monocytes (11,12). Sialyl Le X and its sulfated forms, such as 6-sulfo sialyl Le X , NeuNAc␣233Gal␤134[Fuc␣133(sulfo36)]GlcNAc3 R in mucin-type glycoproteins, have been shown to be ligands for E-, P-, and L-selectin (13-15).Since these O-glycans are present as clusters in mucin-type glycoproteins, mucin-type glycoproteins can present multiple ligands to a selectin. In mucin-type glycoproteins of blood cells, sialyl Le X can be found in core 2-branched oligosaccharides (5, 6, 16). Similarly, 6-sulfo sialyl Le X in L-selectin ligands found in high endothelial venules are synthesized in core 2-branched oligosaccharides such as NeuNAc␣233Gal␤134[Fuc␣133-(sulfo36)]GlcNAc␤136(Gal␤133)GalNAc␣13serine/threonine (17-19).The enzyme responsible for core 2 branching is called core 2 ␤1,6-N-acetylglucosaminyltransferase (C2GnT), and its cDNA has been cloned (20). When C2GnT was inactivated by gene targeting, leukocytes...

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A new O-glycosidically linked tri-hexosamine core structure in sheep gastric mucin: A preliminary note

Cited by 41 publications

References 26 publications

Characterization of the O-glycosidically linked oligosaccharides of rat erythrocyte membrane sialoglycoproteins

Characterization of the O-glycosidically linked oligosaccharides of rat erythrocyte membrane sialoglycoproteins

Structural characterization of neutral oligosaccharides with blood-group A and H activity isolated from bovine submaxillary mucin

Poly-N-acetyllactosamine Extension inN-Glycans and Core 2- and Core 4-branchedO-Glycans Is Differentially Controlled by i-Extension Enzyme and Different Members of the β1,4-Galactosyltransferase Gene Family

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