| Literature DB >> 12507512 |
Han Wang1, Kouichi Tachibana, Yan Zhang, Hiroko Iwasaki, Akihiko Kameyama, Lamei Cheng, Jian ming Guo, Toru Hiruma, Akira Togayachi, Takashi Kudo, Norihiro Kikuchi, Hisashi Narimatsu.
Abstract
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.Entities:
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Year: 2003 PMID： 12507512 DOI： 10.1016/s0006-291x(02)02908-x
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575