Proteomics

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The CNS myelin proteome: Deep profile and persistence after post-mortem delay


ABSTRACT: We revisited the proteome of myelin biochemically purified from the brains of healthy c56Bl/6N-mice utilizing complementary proteomic approaches for deep qualitative and quantitative coverage. A data-independent acquisition (DIA) workflow with alternating low and elevated energy (MSE) provided the high dynamic range required for correct quantification of highest-abundance proteins. According to this analysis, the most abundant myelin proteins PLP, MBP, CNP and MOG constitute 38%, 30%, 5% and 1% of the total myelin protein, respectively. Combined with data from an ion mobility-enhanced version of the MSE mode (referred to as UDMSE) and from 1D-gel-based proteomic approaches, we provide the most comprehensive proteome resource of CNS myelin so far and correlate it with published datasets on mRNA and protein abundance profiles of myelin and oligodendrocytes. Using dynamic range enhancement (DRE)-UDMSE as a dedicated data acquisition mode for routine differential myelin proteome profiling, we also establish that the myelin proteome displays only minor changes if assessed after a post mortem-delay of six hours. Together, these data provide a basis for addressing proteomic heterogeneity of myelin in mouse models and human patients with white matter disorders.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain, Oligodendrocyte

SUBMITTER: Olaf Jahn  

LAB HEAD: PD Dr. Olaf Jahn

PROVIDER: PXD020007 | Pride | 2020-07-16

REPOSITORIES: Pride

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Publications

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

Jahn Olaf O   Siems Sophie B SB   Kusch Kathrin K   Hesse Dörte D   Jung Ramona B RB   Liepold Thomas T   Uecker Marina M   Sun Ting T   Werner Hauke B HB  

Frontiers in cellular neuroscience 20200819


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 cons  ...[more]

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