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UDP-N-Acetyl-Alpha-D-Galactosamine: Polypeptide N-Acetylgalactosaminyltransferases (ppGalNAc-Ts)

  • Liping Zhang
  • E. Tian
  • Kelly G. Ten Hagen
Reference work entry

Abstract

Mucin-type O-linked glycosylation is initiated by the UDP-N-acetyl-α-d-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts), which catalyze the addition of N-acetylgalactosamine (GalNAc) in an alpha-anomeric linkage to the hydroxyl groups of serines or threonines (Fig. 46.1). The ppGalNAc-Ts belong to family 27 of the retaining nucleotide-diphospho-sugar transferases, based on amino acid sequence similarities. The initial transfer of GalNAc from the nucleotide sugar UDP-GalNAc onto protein substrates occurs in the Golgi apparatus and can then be followed by the subsequent addition of other saccharides to form extended and branched mucin-type O-glycans.

Keywords

Bovine Colostrum Lectin Domain Radioisotopic Method Lymphocyte Homing Ascites Hepatoma 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2014

Authors and Affiliations

  • Liping Zhang
    • 1
  • E. Tian
    • 1
  • Kelly G. Ten Hagen
    • 1
  1. 1.NIDCR/National Institutes of HealthBethesdaUSA

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