Protein glycosylation in development and disease

Bioessays. 1999 May;21(5):412-21. doi: 10.1002/(SICI)1521-1878(199905)21:5<412::AID-BIES8>3.0.CO;2-5.


N- and O-linked glycan structures of cell surface and secreted glycoproteins serve a variety of functions related to cell-cell communication in systems affecting development and disease. The more sophisticated N-glycan biosynthesis pathway of metazoans diverges from that of yeast with the appearance of the medial-Golgi beta-N-acetylglucosaminyltransferases (GlcNAc-Ts). Tissue-specific regulation of medial- and trans-Golgi glycosyltransferases contribute structural diversity to glycoproteins in metazoans, and this can affect their molecular properties including localization, half-life, and biological activity. Null mutations in glycosyltransferase genes positioned later in the biosynthetic pathway disrupt expression of smaller subsets of glycan structures and are progressively milder in phenotype. In this review, we examine data on targeted mutations affecting glycosylation in mice and congenital mutations in man, with a view to understanding the molecular functions of glycan structures as modulators of glycoprotein activity. Finally, pathology associated with the expression of GlcNAc-Ts in cancer and diabetes-induced cardiac hypertrophy suggest that inhibitors of these enzymes may have therapeutic value.

Publication types

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

MeSH terms

  • Animals
  • Carbohydrate Sequence
  • Glycoproteins / metabolism*
  • Glycosylation
  • Glycosyltransferases / metabolism*
  • Humans
  • Mice
  • Molecular Sequence Data
  • Polysaccharides / biosynthesis
  • Polysaccharides / chemistry
  • Protein Processing, Post-Translational*


  • Glycoproteins
  • Polysaccharides
  • Glycosyltransferases