N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin

FEBS Lett. 2004 Oct 8;576(1-2):51-6. doi: 10.1016/j.febslet.2004.08.061.

Abstract

Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS). Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif. The latter has been reported to be a minor N-glycosylation site in several glycoproteins. The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Asparagine / chemistry*
  • Glycopeptides / analysis
  • Glycopeptides / metabolism
  • Glycosylation
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / analysis
  • Peptide Fragments / metabolism
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Transferrin / chemistry*

Substances

  • Glycopeptides
  • Peptide Fragments
  • Transferrin
  • Asparagine