Myelin proteomics: the past, the unexpected and the future.

Abstract

Myelin proteomics has been the subject of intense research over the last decade, and its profiling has achieved good results by both in-gel and mass spectrometry-based techniques. 1280 proteins have been identified, a number expected to increase. Some of the identified proteins are as yet not established as true components of myelin. There appears to be a limit in our ability to discover markers of myelin biogenesis, function and disease. Myelin can be easily isolated free of contaminants, thanks to its lipidic nature, which however necessitates pretreatment with detergents before mass spectrometry analysis. Here, the key issue of solubilization of myelin proteins for mass spectrometry measurements is addressed. An in-depth characterization of the myelin proteome would have a profound impact on our knowledge of its pathology and physiology. Future quantitative proteomic studies of the low-abundance myelin protein complement, likely representing key regulatory components, may in future provide molecular description of the dysmyelinating/demyelinating diseases.

• Authors: Isabella Panfoli, Maurizio Bruschi, Laura Santucci, Daniela Calzia, Silvia Ravera, Andrea Petretto, Giovanni Candiano
• Journal: Expert review of proteomics (Expert Rev Proteomics) Vol. 11 Issue 3 Pg. 345-54 (Jun 2014) ISSN: 1744-8387 [Electronic] England
• PMID: 24702188 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Myelin Proteins
• Proteome

Topics

• Humans
• Mass Spectrometry
• Myelin Proteins (analysis)
• Myelin Sheath (chemistry)
• Proteome (analysis)