Control of O-Glycan Branch Formation

@article{Schwientek1999ControlOO,
  title={Control of O-Glycan Branch Formation},
  author={T. Schwientek and M. Nomoto and S. Levery and G. Merkx and A. V. van Kessel and E. Bennett and M. Hollingsworth and H. Clausen},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={4504 - 4512}
}
A novel human UDP-GlcNAc:Gal/GlcNAcβ1–3GalNAcα β1,6GlcNAc-transferase, designated C2/4GnT, was identified by BLAST analysis of expressed sequence tags. The sequence of C2/4GnT encoded a putative type II transmembrane protein with significant sequence similarity to human C2GnT and IGnT. Expression of the secreted form of C2/4GnT in insect cells showed that the gene product had UDP-N-acetyl-α-d-glucosamine:acceptor β1,6-N-acetylglucosaminyltransferase (β1,6GlcNAc-transferase) activity. Analysis… Expand
Control of O-Glycan Branch Formation
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Molecular Cloning and Characterization of a Novel UDP-GlcNAc:GalNAc-peptide β1,3-N-Acetylglucosaminyltransferase (β3Gn-T6), an Enzyme Synthesizing the Core 3 Structure of O-Glycans*
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It is concluded that β3Gn-T6 is the most logical candidate for the core 3 synthase, which plays an important role in the synthesis of mucin-type O-glycans in digestive organs. Expand
Soluble human core 2 beta6-N-acetylglucosaminyltransferase C2GnT1 requires its conserved cysteine residues for full activity.
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Core 2 β6-N-acetylglucosaminyltransferase (Core2GlcNAcT) is a glycosyltransferase that transfers GlcNAc from UDP-GlcNAc to αGalNAc residues in core 1, Galβ1- 3GalNAcα1-Ser/Thr with β1,6-linkage,Expand
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I-branching β6-N-acetylglucosaminyltransferase (IGnT) is a glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to β1,4-linked Gal residue in a linear poly-N-acetyllactosamine,Expand
Purification, Characterization, and Subunit Structure of Rat Core 1 β1,3-Galactosyltransferase*
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Several β3Gn-N-acetylglucosaminyltransferases form a family with structural similarity to the β1,3-galactosyltransferase family, which may play different roles in human gastric mucosa and neuroblastoma. Expand
Peptide-specific Transfer of N-Acetylgalactosamine to O-Linked Glycans by the Glycosyltransferases β1,4-N-Acetylgalactosaminyl Transferase 3 (β4GalNAc-T3) and β4GalNAc-T4*
TLDR
It is shown that β4GalNAc-T3 and β4 galactosaminyltransferases are able to utilize the same peptide motif to selectively add GalNAc to β1,6-linked GlcNAc in core 2 O-linked oligosaccharide structures. Expand
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TLDR
A stable partly purified recombinant human C2GnT is prepared by expression of a truncated form of the enzyme in the baculovirus/Spodoptera frugiperda 9 (Sf9) insect cell system by eliminating one or both of the two potential N-glycosylation sites. Expand
Tissue-specific Regulation of Mouse Core 2 β-1,6-N-Acetylglucosaminyltransferase*
TLDR
The cDNA sequence that encodes the kidney GNT of BALB/c mice is reported, and the deduced amino acid sequence exhibits 84% identity to that of human core 2 β-1,6-GlcNAc-transferase, which suggests that kidney G NT is a mouse homologue of humancore 2 β,1, 6-GlCNAc -transferase. Expand
Cloning of a Novel Member of the UDP-Galactose:β-N-Acetylglucosamine β1,4-Galactosyltransferase Family, β4Gal-T4, Involved in Glycosphingolipid Biosynthesis*
TLDR
A novel putative member of the human UDP-galactose:β-N-acetylglucosamine β1,4-Galactosyltransferase family, designated β4Gal-T4, was identified by BLAST analysis of expressed sequence tags and its kinetic parameters suggest unique functions in the synthesis of neolactoseries glycosphingolipids. Expand
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TLDR
A novel saccharide was synthesized by incubating globo-N-tetraose, GalNAc beta1-3Gal alpha1-4Gal beta 1-4Glc, and UDP[3H]GlcNAc with hog gastric mucosal microsomes, revealing a pathway to novel hybrid type glycans with N-acetyllactosamine chains on globotype saccharides. Expand
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TLDR
expression of soluble secreted constructs in the baculovirus system showed that these genes represented genuine UDP-galactose:β-N-acetylglucosamine β1,4-Galactosyltransferases, thus designated β4Gal-T2 and β4 Gal-T3. Expand
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TLDR
It is reported here that cIGnT6 activity is expressed in human (PA1) and murine (PC13) embryonal carcinoma (EC) cells, both of which contain branched polylactosamines in large amounts. Expand
Substrate Specificities of Three Members of the Human UDP-N-Acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase Family, GalNAc-T1, -T2, and -T3*
TLDR
It is demonstrated that individual GalNAc-transferases have distinct activities and the initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAC-transferase. Expand
A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation.
TLDR
This review will cover recent developments in the understanding of a family of GalNAc-transferases that mediate this type of protein glycosylation, an important post-translational modification of many animal proteins. Expand
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TLDR
The results strongly suggest that the common ancestral gene was first duplicated and then each duplicated gene evolved into the C2GnT or IGnT gene by intron insertion and divergence following the duplication. Expand
Control of mucin synthesis: the peptide portion of synthetic O-glycopeptide substrates influences the activity of O-glycan core 1 UDPgalactose:N-acetyl-alpha-galactosaminyl-R beta 3-galactosyltransferase.
TLDR
Variation in enzyme activity indicates that the beta 3-Gal-transferase recognizes both the peptide and carbohydrate moieties of the substrate. Expand
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