Gain of glycosylation: a new pathomechanism of myelin protein zero mutations

Ann Neurol. 2012 Mar;71(3):427-31. doi: 10.1002/ana.22695.

Abstract

We report the first case of a missense mutation in MPZ causing a gain of glycosylation in myelin protein zero, the main protein of peripheral nervous system myelin. The patient was affected by a severe demyelinating neuropathy caused by a missense mutation, D32N, that created a new glycosylation sequence. We confirmed that the mutant protein is hyperglycosylated, is partially retained into the Golgi apparatus in vitro, and disrupts intercellular adhesion. By sequential experiments, we demonstrated that hyperglycosylation is the main mechanism of this mutation. Gain of glycosylation is a new mechanism in Charcot-Marie-Tooth type 1B.

Publication types

  • Case Reports
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Charcot-Marie-Tooth Disease / genetics*
  • Charcot-Marie-Tooth Disease / metabolism
  • Charcot-Marie-Tooth Disease / pathology*
  • Female
  • Glycosylation
  • Humans
  • Middle Aged
  • Mutation, Missense / genetics*
  • Myelin P0 Protein / genetics*
  • Myelin P0 Protein / metabolism

Substances

  • Myelin P0 Protein