Cloning and characterization of a novel UDP-GaINAc:polypeptide N-acetylgalactosaminyltransferase, pp-GaINAc-T14

被引：76

作者：

Wang, H

Tachibana, K

Zhang, Y

Iwasaki, H

Kameyama, A

Cheng, LM

Guo, JM

Hiruma, T

Togayachi, A

Kudo, T

Kikuchi, N

Narimatsu, H

机构：

[1] Natl Inst Adv Ind Sci & Technol, Res Ctr Glycosci, Glycogene Funct Team, Open Space Lab Cent 2, Tsukuba, Ibaraki 3058568, Japan

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

[3] Fujirebio Inc, Diabet Res Labs, Hachioji, Tokyo 1920031, Japan

[4] New Energy & Ind Technol Dev Org, NEDO, Toshima Ku, Tokyo 170628, Japan

[5] Mitsui Knowledge Ind Co Ltd, Nakano Ku, Tokyo 1648721, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 300卷 / 03期

关键词：

glycosyltransferase; polypeptide N-acetylgalactosaminyltransferase; O-glycosylation; O-glycan; mucin;

D O I：

10.1016/S0006-291X(02)02908-X

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：

A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family was cloned and designated pp-GalNAc-T14. This type II membrane protein contains all motif's that are conserved in the pp-GalNAc-T family proteins and forms a subfamily with pp-GalNAc-T2 on the phylogenetic tree. Quantitative real time PCR analysis revealed significantly high expression of the pp-GalNAc-T14 transcript in kidney, although the transcripts were ubiquitously expressed in all tissues examined. Furthermore, the recombinant pp-GalNAc-T14 transferred GalNAc to a panel of mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). Our results provide evidence that pp-GalNAc-T14 is a new member of the pp-GalNAc-T family and suggest that pp-GalNAc-T14 may be involved in the O-glycosylation in kidney. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：738 / 744

页数：7

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