9
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile.

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          A novel member of the human ppGalNAc-T family, ppGalNAc-T20, was identified and characterized. Amino acid alignment revealed a high sequence identity between ppGalNAc-T20 and -T10. In the GalNAc transfer assay towards mucin-derived peptide substrates, the recombinant ppGalNAc-T20 demonstrated to be a typical glycopeptide GalNAc-transferase that exhibits activity towards mono-GalNAc-glycosylated peptide EA2 derived from rat submandibular gland mucin but no activity towards non-modified EA2. The in vitro catalytic property of ppGalNAc-T20 was compared with that of ppGalNAc-T10 to show different acceptor substrate specificities and kinetic constants. The ppGalNAc-T20 transcript was found exclusively in testis and brain. In situ hybridization further reveals that ppGalNAc-T20 was specifically localized in primary and secondary spermatocytes of the two meiotic periods, suggesting that it may involve in O-glycosylation during mouse spermatogenesis.

          Related collections

          Author and article information

          Journal
          Biochem Biophys Res Commun
          Biochemical and biophysical research communications
          Elsevier BV
          1090-2104
          0006-291X
          Nov 26 2010
          : 402
          : 4
          Affiliations
          [1 ] Ministry of Education Key Laboratory of Systems Biomedicine, Shanghai Center for Systems Biomedicine (SCSB), Shanghai Jiao Tong University, Shanghai, China.
          Article
          S0006-291X(10)01962-5
          10.1016/j.bbrc.2010.10.084
          20977886
          32f3c45b-4c0f-4864-8ad1-f54b5042e777
          Copyright © 2010 Elsevier Inc. All rights reserved.
          History

          Comments

          Comment on this article