Dataset Information

Conservation and divergence of myelin proteome profiles between humans and mice

ABSTRACT: While myelin is commonly assessed in mice as a model for humans, it remained unclear to which extent their myelin protein composition is similar. We analyzed the proteome of myelin biochemically purified from human white matter by two steps of discontinuous sucrose density gradient centrifugation intermitted by osmotic shocks. We utilized a data-independent acquisition (DIA) workflow with alternating low and elevated energy (MSE) and an ion mobility-enhanced version thereof (referred to as UDMSE) to achieve both, a correct quantification of exceptionally abundant myelin proteins and a comprehensive coverage of the myelin proteome. Label-free protein quantification revealed that the relative abundance of the structural myelin proteins PLP, MBP, CNP and SEPTIN8 correlates well with that in c57Bl/6N-mice. Conversely, multiple other proteins were identified exclusively or predominantly in human or mouse myelin. Species-dependent diversity of myelin protein composition can be instructive when translating from mouse models to humans.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain, Cerebral White Matter, Oligodendrocyte

SUBMITTER: Olaf Jahn

LAB HEAD: Prof. Dr. Olaf Jahn

PROVIDER: PXD029727 | Pride | 2022-05-16

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	191206_FASP_191204_Myelin_human_Verdau1_1628_HDMSe_2ul.raw.zip	Raw
	191206_FASP_191204_Myelin_human_Verdau1_1628_HDMSe_2ul_IA_final_peptide.csv	Csv
	191206_FASP_191204_Myelin_human_Verdau1_1628_HDMSe_2ul_IA_final_protein.csv	Csv
	191206_FASP_191204_Myelin_human_Verdau1_1628_MSe_2ul.raw.zip	Raw
	191206_FASP_191204_Myelin_human_Verdau1_1628_MSe_2ul_IA_final_peptide.csv	Csv

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Publications

Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice.

Gargareta Vasiliki-Ilya VI Reuschenbach Josefine J Siems Sophie B SB Sun Ting T Piepkorn Lars L Mangana Carolina C Späte Erik E Goebbels Sandra S Huitinga Inge I Möbius Wiebke W Nave Klaus-Armin KA Jahn Olaf O Werner Hauke B HB

eLife 20220511

Human myelin disorders are commonly studied in mouse models. Since both clades evolutionarily diverged approximately 85 million years ago, it is critical to know to what extent the myelin protein composition has remained similar. Here, we use quantitative proteomics to analyze myelin purified from human white matter and find that the relative abundance of the structural myelin proteins PLP, MBP, CNP, and SEPTIN8 correlates well with that in C57Bl/6N mice. Conversely, multiple other proteins were ...[more]

PMID: 35543322

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