Myelin proteomics: The past, the unexpected and the future

Isabella Panfoli, Maurizio Bruschi, Laura Santucci, Daniela Calzia, Silvia Ravera, Andrea Petretto, Giovanni Candiano

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)345-354
Number of pages10
JournalExpert Review of Proteomics
Volume11
Issue number3
DOIs
Publication statusPublished - 2014

Keywords

  • mass spectrometry
  • myelin sheath
  • proteomic analysis
  • targeted-proteomics
  • two dimensional gel electrophoresis

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Medicine(all)

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