Changes in plasma and IgG N-glycome during childhood and adolescence

Glycobiology. 2012 Jul;22(7):975-82. doi: 10.1093/glycob/cws062. Epub 2012 Mar 16.


Despite the importance of protein glycosylation in all physiological and pathological processes and their potential as diagnostic markers and drug targets, the glycome of children is still unexplored. We analyzed N-linked plasma and IgG glycomes in 170 children and adolescents between 6 and 18 years of age. The results showed large biological variability at the population level as well as a large number of associations between different glycans and age. The plasma N-glycome of younger children was found to contain a larger proportion of large complex glycan structures (r = -0.71 for tetrasialylated glycans; r = -0.41 for trisialylated glycans) as well as an increase in disialylated biantennary structures (r = 0.55) with age. Core fucosylation and the level of agalactosylated plasma and IgG glycans decreased while digalactosylated glycans increased with age. This pattern of age-dependent changes in children differs from changes reported in adult population in both, direction and the intensity of changes. Also, sex differences are much smaller in children than in adults and are present mainly during puberty. These important observations should be accounted for when glycan-based diagnostic tests or therapeutics are being developed or evaluated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Child
  • Female
  • Galactans / blood
  • Glycoproteins / blood*
  • Glycosylation
  • Hexosamines / blood
  • Humans
  • Immunoglobulin G / blood*
  • Male
  • Mannans / blood
  • Molecular Sequence Data
  • Protein Processing, Post-Translational*
  • Sialic Acids / blood


  • Galactans
  • Glycoproteins
  • Hexosamines
  • Immunoglobulin G
  • Mannans
  • Sialic Acids