β1,3‐N‐Acetylglucosaminyltransferase‐7 (β3Gn‐T7) acts efficiently on keratan sulfate‐related glycans

FEBS Letters

Yamashita, Katsuko¹  Seko, Akira¹ 

[1] Department of Biochemistry, Sasaki Institute, 2-2, Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan

关键词: β1;    3-N-Acetylglucosaminyltransferase;    Keratan sulfate;    Sulfated glycan;    N-linked glycan;    β3Gn-T;    β1;    3-N-acetylglucosaminyltransferase;    pNP;    p-nitrophenyl;    PVL;    Psathyrella velutina lectin;    RCA-I;    Ricinus communis agglutinin-I;   

DOI  :  10.1016/S0014-5793(03)01440-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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(SO₃ ⁻→6)GlcNAcβ1→3Galβ1→4(SO₃ ⁻→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.

【 授权许可】

Unknown