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  The CNS Myelin Proteome: Deep Profile and Persistence After Post-mortem Delay

Jahn, O., Siems, S. B., Kusch, K., Hesse, D., Jung, R. B., Liepold, T., et al. (2020). The CNS Myelin Proteome: Deep Profile and Persistence After Post-mortem Delay. Frontiers in Cellular Neuroscience, 14: 249. doi:10.3389/fncel.2020.00239.

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 Creators:
Jahn, O.1, Author              
Siems, S. B.2, Author              
Kusch, Kathrin2, Author              
Hesse, D.1, Author              
Jung, R. B.2, Author              
Liepold, T.1, Author              
Uecker, M.1, Author              
Sun, T.2, Author              
Werner, H. B.2, Author              
Affiliations:
1Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173673              
2Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173664              

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Free keywords: oligodendrocyte, myelin proteome, central nervous system (CNS), demyelination, post-mortem delay, autopsy, label-free proteomics, transcriptome
 Abstract: Myelin membranes are dominated by lipids while the complexity of their protein composition has long been considered to be low. However, numerous additional myelin proteins have been identified since. Here we revisit the proteome of myelin biochemically purified from the brains of healthy c56Bl/6N-mice utilizing complementary proteomic approaches for deep qualitative and quantitative coverage. By gel-free, label-free mass spectrometry, the most abundant myelin proteins PLP, MBP, CNP, and MOG constitute 38, 30, 5, and 1% of the total myelin protein, respectively. The relative abundance of myelin proteins displays a dynamic range of over four orders of magnitude, implying that PLP and MBP have overshadowed less abundant myelin constituents in initial gel-based approaches. By comparisons with published datasets we evaluate to which degree the CNS myelin proteome correlates with the mRNA and protein abundance profiles of myelin and oligodendrocytes. Notably, the myelin proteome displays only minor changes if assessed after a post-mortem delay of 6 h. These data provide the most comprehensive proteome resource of CNS myelin so far and a basis for addressing proteomic heterogeneity of myelin in mouse models and human patients with white matter disorders.

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 Dates: 2020-08-19
 Publication Status: Published online
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3389/fncel.2020.00239
 Degree: -

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Project name : MyeliNANO
Grant ID : 647168
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Frontiers in Cellular Neuroscience
  Other : Front. Cell. Neurosci.
  Abbreviation : FNCEL
Source Genre: Journal
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Pages: 15 Volume / Issue: 14 Sequence Number: 249 Start / End Page: - Identifier: ISSN: 1664-8714
ISSN: 1662-5102
CoNE: https://pure.mpg.de/cone/journals/resource/1662-5102