A quantitative investigation of fucosylated serum glycoproteins with application to esophageal adenocarcinoma

Electrophoresis. 2010 Jun;31(11):1833-41. doi: 10.1002/elps.201000046.


Although glycoproteomic studies provide unique opportunities for cancer research, it has been necessary to develop specific methods for analysis of oncologically interesting glycoproteins. We describe a general, multimethodological approach for quantitative glycoproteomic analysis of fucosylated glycoproteins in human blood serum. A total of 136 putative fucosylated glycoproteins were identified with very high confidence in three clinically relevant sample pools (N=5 for each), with a mean CV of 3.1% observed for replicate analyses. Two samples were collected from subjects diagnosed with esophagus disease states, high-grade dysplasia plus esophageal adenocarcinoma, while the third sample was representative of a disease-free condition. Some glycoproteins, observed to be significantly upregulated in esophageal adenocarcinoma, i.e. more than twofold higher than in the disease-free condition, are briefly discussed. Further investigation will be necessary to validate these findings; however, the method itself is demonstrated to be an effective tool for quantitative glycoproteomics of clinical samples.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenocarcinoma / blood*
  • Collagen Type I / analysis
  • Collagen Type I / blood
  • Esophageal Neoplasms / blood*
  • Fetuin-B
  • Fucose / blood*
  • Glycoproteins / analysis
  • Glycoproteins / blood*
  • Humans
  • Lectins / chemistry
  • Peptide Fragments / analysis
  • Peptide Fragments / metabolism
  • Proteome / analysis*
  • Trypsin / metabolism
  • alpha-Fetoproteins / analysis
  • alpha-Fetoproteins / metabolism


  • Collagen Type I
  • EMILIN2 protein, human
  • FETUB protein, human
  • Fetuin-B
  • Glycoproteins
  • Lectins
  • Peptide Fragments
  • Proteome
  • alpha-Fetoproteins
  • collagen type I, alpha 1 chain
  • fucose-binding lectin
  • lectin, Aleuria aurantia
  • Fucose
  • Trypsin