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β1,3‐ N ‐Acetylglucosaminyltransferase‐7 (β3Gn‐T7) acts efficiently on keratan sulfate‐related glycans
Author(s) -
Seko Akira,
Yamashita Katsuko
Publication year - 2004
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/s0014-5793(03)01440-6
Subject(s) - glycan , keratan sulfate , chemistry , biochemistry , glycoprotein , chondroitin sulfate , glycosaminoglycan
β1,3‐ N ‐Acetylglucosaminyltransferase‐7 (β3Gn‐T7) has been identified as an anti‐migration factor for a lung cancer cell line but its enzymatic activity has not yet been characterized. Here we show that β3Gn‐T7 efficiently acts on keratan sulfate‐related glycans including Galβ1→4(SO 3 − →6)GlcNAcβ1→3Galβ1→4(SO 3 − →6)GlcNAc (L2L2), while lacto‐ N ‐tetraose and lacto‐ N ‐ neo ‐tetraose were poor substrates. Moreover, we found that among the other five β3Gn‐Ts and i antigen‐producing β3Gn‐T (iGn‐T), β3Gn‐T2 and iGn‐T act well on L2L2, although these specific activities were lower than those for a tetraantennary N ‐glycan. These results indicate that β3Gn‐T7 is the one that most efficiently elongates L2L2 and may be involved in the biosynthesis of keratan sulfate.