Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions

Amado, Margarida; Almeida, Raquel; Schwientek, Tilo; Clausen, Henrik

doi:10.1016/s0304-4165(99)00168-3

Cited by 273 publications

(174 citation statements)

References 107 publications

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“…A large family of ␤1,3-galactosyltransferases has been described based on expressed sequence tags exhibiting a high degree of homology and by use of PCR-based cloning strategies (13)(14)(15)(16)(17)(18)(19)(20). ␤3GalT1, -2, -3, and -5 utilize GlcNAc-terminated oligosaccharide as acceptor substrates, producing linkages characteristic of type 1 N-acetyllactosamine repeat units on N-and O-linked oligosaccharides and glycolipids, whereas ␤3GalT4 transfers galactose to the terminal GalNAc unit of the ganglioside series GM2, GD2, and GA2 acceptors (35).…”

Section: Resultsmentioning

confidence: 99%

“…Five members of this family have already been described (13)(14)(15)(16)(17)(18)(19)(20), with a possible homolog in Drosophila (Braniac) (21). None of the ␤3GalT enzymes characterized to date have activity with galactose-terminated oligosaccharide acceptors, suggesting that another member of the family must exist in order to catalyze the formation of the linkage region of glycosaminoglycans.…”

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confidence: 99%

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Biosynthesis of the Linkage Region of Glycosaminoglycans

Bai

Zhou

Brown

et al. 2001

Journal of Biological Chemistry

162

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A family of five ␤1,3-galactosyltransferases has been characterized that catalyze the formation of Gal␤1, 3GlcNAc␤ and Gal␤1,3GalNAc␤ linkages present in glycoproteins and glycolipids (␤3GalT1, -2, -3, -4, and -5). We now report a new member of the family (␤3GalT6), involved in glycosaminoglycan biosynthesis. The human and mouse genes were located on chromosomes 1p36.3 and 4E2, respectively, and homologs are found in Drosophila melanogaster and Caenorhabditis elegans. Unlike other members of the family, ␤3GalT6 showed a broad mRNA expression pattern by Northern blot analysis. Although a high degree of homology across several subdomains exists among other members of the ␤3-galactosyltransferase family, recombinant enzyme did not utilize glucosamine-or galactosamine-containing acceptors. Instead, the enzyme transferred galactose from UDP-galactose to acceptors containing a terminal ␤-linked galactose residue. This product, Gal␤1,3Gal␤ is found in the linkage region of heparan sulfate and chondroitin sulfate (GlcA␤1,3Gal␤1,3Gal␤1,4Xyl␤-O-Ser), indicating that ␤3GalT6 is the so-called galactosyltransferase II involved in glycosaminoglycan biosynthesis. Its identity was confirmed in vivo by siRNA-mediated inhibition of glycosaminoglycan synthesis in HeLa S3 cells.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Biosynthesis of the Linkage Region of Glycosaminoglycans

Bai

Zhou

Brown

et al. 2001

Journal of Biological Chemistry

162

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“…␤1,4-galactosyltransferase (GalT1) is the first glycosyltransferase being cloned and biologically characterized [12]. GalT1 acts as a type II membrane glycoprotein, and it exists abundantly in the Golgi complex, where it participates in oligosaccharide synthesis.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Ubiquitin-Conjugating Enzyme That Regulates β1,4-Galactosyltransferase-1 in Embryonic Stem Cells

Wassler¹,

Shur

Zhou³

et al. 2008

Stem Cells

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In this study we identified a novel galactosyltransferase 1-associating protein (GTAP) by cDNA cloning from a murine embryonic cDNA library using the two-hybrid yeast system. GTAP is expressed in early embryonic tissues, as well as in adult tissues with active cell turnover, and belongs to the class III ubiquitin-conjugating (E2) enzyme family. Its COOH-terminal domain contains a consensus sequence for ubiquitin binding shared by all the ubiquitin-conjugating enzymes, whereas its NH 2 -terminal domain appears critical for the binding and internalization of cell surface galactosyltransferase 1 (GalT1) in embryonic stem cells through a monensin-and MG132-dependent pathway. We have found that GTAP regulates GalT1-associated, laminin-dependent embryonic cell adhesion and the formation of embryoid bodies. Thus, GTAP functions as an evolutionarily conserved E2 enzyme, which may participate in intercellular adhesion and embryonic development. STEM CELLS 2008;

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“…In the past, we succeeded in the molecular cloning of a series of b3-GT genes. Thirteen human b3-GTs, i.e., five b3Gal-Ts, two b3GalNAc-Ts and six b3Gn-Ts, have been identified and reported [1][2][3][4][5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

A novel β1,3‐N‐acetylglucosaminyltransferase (β3Gn‐T8), which synthesizes poly‐N‐acetyllactosamine, is dramatically upregulated in colon cancer

et al. 2004

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A new member of the UDP-N-acetylglucosamine: bgalactose b1,3-N-acetylglucosaminyltransferase (b3Gn-T) family having the b3-glycosyltransferase motifs was identified using an in silico method. This novel b3Gn-T was cloned from a human colon cancer cell line and named b3Gn-T8 based on its position in a phylogenetic tree and enzymatic activity. b3Gn-T8 transfers GlcNAc to the non-reducing terminus of the Galb1-4GlcNAc of tetraantennary N-glycan in vitro. HCT15 cells transfected with b3Gn-T8 cDNA showed an increase in reactivity to both LEA and PHA-L4 in a flow cytometric analysis. These results indicated that b3Gn-T8 is involved in the biosynthesis of poly-Nacetyllactosamine chains on tetraantennary (b1,6-branched) N-glycan. In most of the colorectal cancer tissues examined, the level of b3Gn-T8 transcript was significantly higher than in normal tissue. b3Gn-T8 could be an enzyme involved in the synthesis of poly-N-acetyllactosamine on b1-6 branched N-glycans in colon cancer.

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Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions

Cited by 273 publications

References 107 publications

Biosynthesis of the Linkage Region of Glycosaminoglycans

Biosynthesis of the Linkage Region of Glycosaminoglycans

Characterization of a Novel Ubiquitin-Conjugating Enzyme That Regulates β1,4-Galactosyltransferase-1 in Embryonic Stem Cells

A novel β1,3‐N‐acetylglucosaminyltransferase (β3Gn‐T8), which synthesizes poly‐N‐acetyllactosamine, is dramatically upregulated in colon cancer

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