A novel β1,3-N-acetylglucosaminyltransferase (β3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer
A novel β1,3-N-acetylglucosaminyltransferase (β3Gn-T8), which synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon cancer
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DOI:
10.1016/j.febslet.2004.11.037
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发表时间:
2005-01-03
期刊:
影响因子:
3.5
通讯作者:
Narimatsu, H
中科院分区:
文献类型:
--
作者:
Ishida, H;Togayachi, A;Narimatsu, H
A new member of the UDP-N-acetvlalucosamine: beta galactose beta1,3-N-acetyliglucosaminyltransferase (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-acetyflactosamine on beta1-6 branched N-glycans in colon cancer. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.