| Literature DB >> 15620693 |
Hiroyasu Ishida1, Akira Togayachi, Tokiko Sakai, Toshie Iwai, Toru Hiruma, Takashi Sato, Reiko Okubo, Niro Inaba, Takashi Kudo, Masanori Gotoh, Junichi Shoda, Naomi Tanaka, Hisashi Narimatsu.
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.Entities:
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Year: 2005 PMID： 15620693 DOI： 10.1016/j.febslet.2004.11.037
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124