Wang Han, Tachibana Kouichi, Zhang Yan, Iwasaki Hiroko, Kameyama Akihiko, Cheng Lamei, Guo Jian ming, Hiruma Toru, Togayachi Akira, Kudo Takashi, Kikuchi Norihiro, Narimatsu Hisashi
Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), Open Space Laboratory Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki-ken 305-8568, Japan.
Biochem Biophys Res Commun. 2003 Jan 17;300(3):738-44. doi: 10.1016/s0006-291x(02)02908-x.
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 motifs 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.
人类UDP-N-乙酰-D-半乳糖胺:多肽N-乙酰半乳糖胺基转移酶(pp-GalNAc-T)基因家族的一个新成员被克隆并命名为pp-GalNAc-T14。这种II型膜蛋白包含在pp-GalNAc-T家族蛋白中保守的所有基序,并在系统发育树上与pp-GalNAc-T2形成一个亚家族。定量实时PCR分析显示,pp-GalNAc-T14转录本在肾脏中表达显著高,尽管转录本在所检测的所有组织中均有普遍表达。此外,重组的pp-GalNAc-T14将GalNAc转移到一组粘蛋白衍生的肽底物上,如Muc2、Muc5AC、Muc7和Muc13(-58)。我们的结果提供了证据表明pp-GalNAc-T14是pp-GalNAc-T家族的一个新成员,并表明pp-GalNAc-T14可能参与肾脏中的O-糖基化。