Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

被引：59

作者：

Cheng, LM

Tachibana, K

Iwasaki, H

Kameyama, A

Zhang, Y

Kubota, T

Hiruma, T

Tachibana, K

Kudo, T

Guo, JM

Narimatsu, H

机构：

[1] AIST, Res Ctr Glycosci, Glycogene Funct Team, Tsukuba, Ibaraki 3058568, Japan

[2] Amerham Biosci KK, Shinjuku Ku, Tokyo 1690073, Japan

[3] Fujirebio Inc, Diagnost Res Labs, Tokyo 1920031, Japan

来源：

FEBS LETTERS | 2004年 / 566卷 / 1-3期

关键词：

UDP-GaINAc : polypeptide; N-acetylgalactosaminyltransferase (EC 2.4.1.41); O-glycosylation; O-glycan; mucin;

D O I：

10.1016/j.febslet.2004.03.108

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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页码：17 / 24

页数：8

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