The lecticans of mammalian brain perineural net are O-mannosylated.

Abstract

O-Mannosylation is an important protein modification in brain. During the last years, a few mammalian proteins have been identified as targets of the protein-O-mannosyltransferases 1 and 2. However, these still cannot explain the high content of O-mannosyl glycans in brain and the strong brain involvement of congenital muscular dystrophies caused by POMT mutations (Walker-Warburg syndrome, dystroglycanopathies). By fractionating and analyzing the glycoproteome of mouse and calf brain lysates, we could show that proteins of the perineural net, the lecticans, are O-mannosylated, indicating that major components of neuronal extracellular matrix are O-mannosylated in mammalian brain. This finding corresponds with the high content of O-mannosyl glycans in brain as well as with the brain involvement of dystroglycanopathies. In contrast, the lectican neurocan is not O-mannosylated when recombinantly expressed in EBNA-293 cells, revealing the possibility of different control mechanisms for the initiation of O-mannosylation in different cell types.

• Authors: Sandra Pacharra, Franz-Georg Hanisch, Martina Mühlenhoff, Andreas Faissner, Uwe Rauch, Isabelle Breloy
• Journal: Journal of proteome research (J Proteome Res) Vol. 12 Issue 4 Pg. 1764-71 (Apr 05 2013) ISSN: 1535-3907 [Electronic] United States
• PMID: 23428289 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Chondroitin Sulfate Proteoglycans
• Glycoproteins
• Ncan protein, rat
• Neurocan
• Polysaccharides
• Recombinant Proteins

Topics

• Animals
• Brain (metabolism)
• Carbohydrate Sequence
• Cattle
• Chondroitin Sulfate Proteoglycans (genetics, metabolism)
• Glycoproteins (analysis, metabolism)
• Humans
• Mammals
• Mice
• Molecular Sequence Data
• Nerve Net (metabolism)
• Neurocan
• Polysaccharides (analysis, chemistry, metabolism)
• Protein Processing, Post-Translational
• Rats
• Recombinant Proteins (genetics, metabolism)