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
收藏
页码：211 / 218
页数：8
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