Modulation of O-GlcNAc glycosylation during Xenopus oocyte maturation

J Cell Biochem. 2004 Nov 15;93(5):999-1010. doi: 10.1002/jcb.20242.


O-linked N-acetylglucosamine (O-GlcNAc) glycosylation is a post-translational modification, which is believed antagonises phosphorylation. We have studied the O-GlcNAc level during Xenopus oocyte meiotic resumption, taking advantage of the high synchrony of this model which is dependent upon a burst of phosphorylation. Stimulation of immature stage VI oocytes using progesterone was followed by a 4.51 +/- 0.32 fold increase in the GlcNAc content, concomitantly to an increase in phosphorylation, notably on two cytoplasmic proteins of 66 and 97 kDa. The increase of O-GlcNAc for the 97 kDa protein, which we identified as beta-catenin was partly related to its accumulation during maturation, as was demonstrated by the use of the protein synthesis inhibitor--cycloheximide. Microinjection of free GlcNAc, which inhibits O-glycosylated proteins-lectins interactions, delayed the progesterone-induced maturation without affecting the O-GlcNAc content. Our results suggest that O-GlcNAc glycosylation could regulate protein-protein interactions required for the cell cycle kinetic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Acetylglucosamine / pharmacology
  • Animals
  • Cycloheximide / metabolism
  • Glycosylation
  • Meiosis / physiology*
  • Microinjections
  • Oocytes / cytology
  • Oocytes / drug effects
  • Oocytes / physiology*
  • Progesterone / metabolism
  • Protein Processing, Post-Translational*
  • Protein Synthesis Inhibitors / metabolism
  • Xenopus laevis


  • Protein Synthesis Inhibitors
  • Progesterone
  • Cycloheximide
  • Acetylglucosamine