Guo Jian-Ming, Zhang Yan, Cheng Lamei, Iwasaki Hiroko, Wang Han, Kubota Tomomi, Tachibana Kouichi, Narimatsu Hisashi
Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory C-2, Tsukuba, Ibaraki, Japan.
FEBS Lett. 2002 Jul 31;524(1-3):211-8. doi: 10.1016/s0014-5793(02)03007-7.
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.
我们通过电子克隆技术获得了一种新型人类UDP-N-乙酰半乳糖胺:多肽N-乙酰半乳糖胺基转移酶(pp-GalNAc-T),即pp-GalNAc-T12。pp-GalNAc-T12推导的氨基酸序列包含pp-GalNAc-T家族蛋白中的所有保守基序。定量实时聚合酶链反应分析表明,pp-GalNAc-T12转录本主要在胃、小肠和结肠等消化器官中表达。重组pp-GalNAc-T12将N-乙酰半乳糖胺转移至黏蛋白衍生肽,如Muc1a、Muc5AC、EA2肽以及GalNAc-Muc5AC糖肽。由于黏蛋白是主要在消化器官中产生的糖蛋白,我们的研究结果表明pp-GalNAc-T12在消化器官黏蛋白型寡糖生物合成的起始步骤中发挥重要作用。