Sialylation is involved in cell fate decision during development, reprogramming and cancer progression

Protein Cell. 2019 Aug;10(8):550-565. doi: 10.1007/s13238-018-0597-5. Epub 2018 Nov 26.

Abstract

Sialylation, or the covalent addition of sialic acid to the terminal end of glycoproteins, is a biologically important modification that is involved in embryonic development, neurodevelopment, reprogramming, oncogenesis and immune responses. In this review, we have given a comprehensive overview of the current literature on the involvement of sialylation in cell fate decision during development, reprogramming and cancer progression. Sialylation is essential for early embryonic development and the deletion of UDP-GlcNAc 2-epimerase, a rate-limiting enzyme in sialic acid biosynthesis, is embryonically lethal. Furthermore, the sialyltransferase ST6GAL1 is required for somatic cell reprogramming, and its downregulation is associated with decreased reprogramming efficiency. In addition, sialylation levels and patterns are altered during cancer progression, indicating the potential of sialylated molecules as cancer biomarkers. Taken together, the current evidences demonstrate that sialylation is involved in crucial cell fate decision.

Keywords: cancer; cell fate; development; reprogramming; sialylation.

Publication types

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

MeSH terms

  • Animals
  • Biomarkers, Tumor / metabolism*
  • Carbohydrate Epimerases / metabolism
  • Carcinogenesis / metabolism*
  • Cell Transformation, Neoplastic / metabolism*
  • Cellular Reprogramming / physiology*
  • Humans
  • Mice
  • N-Acetylneuraminic Acid / metabolism*
  • Sialyltransferases / metabolism

Substances

  • Biomarkers, Tumor
  • Sialyltransferases
  • Carbohydrate Epimerases
  • UDP acetylglucosamine-2-epimerase
  • N-Acetylneuraminic Acid