Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12

被引：74

作者：

Guo, JM

Zhang, Y

Cheng, LM

Iwasaki, H

Wang, H

Kubota, T

Tachibana, K

Narimatsu, H

机构：

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

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

来源：

FEBS LETTERS | 2002年 / 524卷 / 1-3期

关键词：

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

D O I：

10.1016/S0014-5793(02)03007-7

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 cloned in silico a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T), pp-GalNAc-T12. The deduced amino acid sequence of pp-GalNAc-T12 contains all conserved motifs in pp-GalNAc-T family proteins. Quantitative real time polymerase chain reaction analysis revealed that the pp-GalNAc-T12 transcript was expressed mainly in digestive organs such as stomach, small intestine and colon. The recombinant pp-GalNAc-T12 transferred GalNAc to the mucin-derived peptides such as the Muc1a, Muc5AC, EA2 peptides and the GalNAc-Muc5AC glycopeptide. Since mucins are glycoproteins mainly produced in the digestive organs, our results suggest that pp-GalNAc-T12 plays an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：211 / 218

页数：8

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