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A novel β1,3‐ N ‐acetylglucosaminyltransferase (β3Gn‐T8), which synthesizes poly‐ N ‐acetyllactosamine, is dramatically upregulated in colon cancer
Author(s) -
Ishida Hiroyasu,
Togayachi Akira,
Sakai Tokiko,
Iwai Toshie,
Hiruma Toru,
Sato Takashi,
Okubo Reiko,
Inaba Niro,
Kudo Takashi,
Gotoh Masanori,
Shoda Junichi,
Tanaka Naomi,
Narimatsu Hisashi
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.037
Subject(s) - glycan , glycosyltransferase , colorectal cancer , in silico , complementary dna , enzyme , transfection , in vitro , biosynthesis , cell culture , microbiology and biotechnology , biochemistry , biology , chemistry , glycoprotein , gene , cancer , genetics
A new member of the UDP‐ N ‐acetylglucosamine: β‐galactose β1,3‐ N ‐acetylglucosaminyltransferase (β3Gn‐T) family having the β3‐glycosyltransferase motifs was identified using an in silico method. This novel β3Gn‐T was cloned from a human colon cancer cell line and named β3Gn‐T8 based on its position in a phylogenetic tree and enzymatic activity. β3Gn‐T8 transfers GlcNAc to the non‐reducing terminus of the Galβ1–4GlcNAc of tetraantennary N ‐glycan in vitro. HCT15 cells transfected with β3Gn‐T8 cDNA showed an increase in reactivity to both LEA and PHA‐L4 in a flow cytometric analysis. These results indicated that β3Gn‐T8 is involved in the biosynthesis of poly‐ N ‐acetyllactosamine chains on tetraantennary (β1,6‐branched) N ‐glycan. In most of the colorectal cancer tissues examined, the level of β3Gn‐T8 transcript was significantly higher than in normal tissue. β3Gn‐T8 could be an enzyme involved in the synthesis of poly‐ N ‐acetyllactosamine on β1–6 branched N ‐glycans in colon cancer.