Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

FEBS Lett. 2004 May 21;566(1-3):17-24. doi: 10.1016/j.febslet.2004.03.108.

Abstract

We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Catalysis
  • Glycosylation
  • Humans
  • Isoenzymes
  • Molecular Sequence Data
  • N-Acetylgalactosaminyltransferases / genetics*
  • N-Acetylgalactosaminyltransferases / metabolism*
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Polypeptide N-acetylgalactosaminyltransferase
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Substrate Specificity
  • Tissue Distribution
  • Transcription, Genetic
  • Uridine Diphosphate N-Acetylgalactosamine / metabolism

Substances

  • Isoenzymes
  • Oligopeptides
  • Recombinant Proteins
  • Uridine Diphosphate N-Acetylgalactosamine
  • N-Acetylgalactosaminyltransferases

Associated data

  • GENBANK/AB078149
  • GENBANK/BG699346
  • GENBANK/BG714178
  • GENBANK/BG715977