Clinical aspects of altered glycosylation of glycoproteins in cancer

Electrophoresis. 1999 Feb;20(2):362-71. doi: 10.1002/(SICI)1522-2683(19990201)20:2<362::AID-ELPS362>3.0.CO;2-V.

Abstract

Alteration of the expression of carbohydrate structures is frequently observed in tumor cells. This review summarizes the different changes of O- and N-linked glycoproteins observed in cancer cells, the impact of the tumor-related carbohydrate phenotypes on the clinical outcome of the cancer disease, and the various ways in which carbohydrate structures can interact with different carbohydrate-detecting adhesion molecules, selectins, and sialoadhesins. Various ways of inhibiting the formation of cell adhesion-engaged carbohydrates on the cell surface, or inhibiting the binding are discussed. Carbohydrate structures which are in clinical use as circulating tumor markers and the effect of genotypes on tumor marker concentrations are reviewed.

Publication types

  • Review

MeSH terms

  • Antigens, Neoplasm / metabolism
  • Biomarkers, Tumor
  • Carbohydrate Metabolism
  • Carbohydrates / chemistry
  • Glycoproteins / metabolism*
  • Glycosylation
  • Humans
  • Neoplasm Proteins / metabolism*
  • Neoplasms / metabolism*

Substances

  • Antigens, Neoplasm
  • Biomarkers, Tumor
  • Carbohydrates
  • Glycoproteins
  • Neoplasm Proteins