2. Academic Validation
  3. A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer

A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer

  • FEBS Lett. 2005 Jan 3;579(1):71-8. doi: 10.1016/j.febslet.2004.11.037.
Hiroyasu Ishida 1,  Akira Togayachi,  Tokiko Sakai,  Toshie Iwai,  Toru Hiruma,  Takashi Sato,  Reiko Okubo,  Niro Inaba,  Takashi Kudo,  Masanori Gotoh,  Junichi Shoda,  Naomi Tanaka,  Hisashi Narimatsu
Affiliations

Affiliation

  • 1 Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Central-2 OSL, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
PMID: 15620693 DOI: 10.1016/j.febslet.2004.11.037
Abstract

A new member of the UDP-N-acetylglucosamine: beta-galactose beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T) family having the beta3-glycosyltransferase motifs was identified using an in silico method. This novel beta3Gn-T was cloned from a human colon Cancer cell line and named beta3Gn-T8 based on its position in a phylogenetic tree and enzymatic activity. Beta3Gn-T8 transfers GlcNAc to the non-reducing terminus of the Galbeta1-4GlcNAc of tetraantennary N-glycan in vitro. HCT15 cells transfected with beta3Gn-T8 cDNA showed an increase in reactivity to both LEA and PHA-L4 in a flow cytometric analysis. These results indicated that beta3Gn-T8 is involved in the biosynthesis of poly-N-acetyllactosamine chains on tetraantennary (beta1,6-branched) N-glycan. In most of the colorectal Cancer tissues examined, the level of beta3Gn-T8 transcript was significantly higher than in normal tissue. Beta3Gn-T8 could be an Enzyme involved in the synthesis of poly-N-acetyllactosamine on beta1-6 branched N-glycans in colon Cancer.

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