Molecular cloning and characterization of a novel member of the UDP‐GalNAc:polypeptide N‐acetylgalactosaminyltransferase family, pp‐GalNAc‐T12 1

FEBS Letters

Cheng, Lamei¹  Narimatsu, Hisashi¹  Iwasaki, Hiroko¹  Tachibana, Kouichi¹  Zhang, Yan¹  Kubota, Tomomi¹  Guo, Jian-Ming¹  Wang, Han¹ 

[1]Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan

关键词: Glycosyltransferase;    N-Acetylgalactosaminyltransferase;    Mucin;    O-Glycosylation;    O-Glycan;    pp-GalNAc-T;    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase;    EST;    expressed sequence tag;    ORF;    open reading frame;    PCR;    polymerase chain reaction;    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;    HPLC;    high performance liquid chromatography;    FAM;    5-carboxyfluorescein succinimidyl ester;   

DOI  :  10.1016/S0014-5793(02)03007-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown