Identification of the first COG-CDG patient of Indian origin

Mol Genet Metab. 2011 Mar;102(3):364-7. doi: 10.1016/j.ymgme.2010.11.161. Epub 2010 Nov 24.

Abstract

Mutations in the Conserved Oligomeric Golgi (COG) complex give rise to type II congenital disorders of glycosylation (CDG). Thus far, mutations have been identified in 6 of the 8 COG subunits. Here we present data identifying a previously reported CDG-IIx case from Singapore as a new COG4 patient with 2 novel mutations leading to p.E233X and p.L773R; with p.E233X being a de novo mutation. As a result, COG4 protein expression was dramatically reduced, while expression of the other subunits remained unaffected. Analysis of serum N-glycans revealed deficiencies in both sialylation and galactosylation. Furthermore, patient fibroblasts have impaired O-glycosylation. Importantly, patient fibroblasts exhibited a delay in Brefeldin A (BFA) induced retrograde transport, a common characteristic seen in COG deficiencies.

Publication types

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

MeSH terms

  • Adaptor Proteins, Vesicular Transport / genetics*
  • Adaptor Proteins, Vesicular Transport / metabolism*
  • Brefeldin A / pharmacology
  • Congenital Disorders of Glycosylation / genetics*
  • Congenital Disorders of Glycosylation / metabolism*
  • Congenital Disorders of Glycosylation / physiopathology
  • Fibroblasts / drug effects
  • Fibroblasts / metabolism
  • Genetic Complementation Test
  • Golgi Apparatus / metabolism
  • Golgi Apparatus / pathology
  • Humans
  • Lentivirus / genetics
  • Mutation
  • Polysaccharides / analysis
  • Protein Synthesis Inhibitors / pharmacology
  • Protein Transport / drug effects
  • Singapore

Substances

  • Adaptor Proteins, Vesicular Transport
  • Polysaccharides
  • Protein Synthesis Inhibitors
  • Brefeldin A