Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice
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 h...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2022-05-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/77019 |
| _version_ | 1811252309151186944 |
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| author | Vasiliki-Ilya Gargareta Josefine Reuschenbach Sophie B Siems Ting Sun Lars Piepkorn Carolina Mangana Erik Späte Sandra Goebbels Inge Huitinga Wiebke Möbius Klaus-Armin Nave Olaf Jahn Hauke B Werner |
| author_facet | Vasiliki-Ilya Gargareta Josefine Reuschenbach Sophie B Siems Ting Sun Lars Piepkorn Carolina Mangana Erik Späte Sandra Goebbels Inge Huitinga Wiebke Möbius Klaus-Armin Nave Olaf Jahn Hauke B Werner |
| author_sort | Vasiliki-Ilya Gargareta |
| collection | DOAJ |
| description | 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 identified exclusively or predominantly in human or mouse myelin. This is exemplified by peripheral myelin protein 2 (PMP2), which was specific to human central nervous system myelin, while tetraspanin-2 (TSPAN2) and connexin-29 (CX29/GJC3) were confined to mouse myelin. Assessing published scRNA-seq-datasets, human and mouse oligodendrocytes display well-correlating transcriptome profiles but divergent expression of distinct genes, including Pmp2, Tspan2, and Gjc3. A searchable web interface is accessible via www.mpinat.mpg.de/myelin. Species-dependent diversity of oligodendroglial mRNA expression and myelin protein composition can be informative when translating from mouse models to humans. |
| first_indexed | 2024-04-12T16:32:48Z |
| format | Article |
| id | doaj.art-4e5b92e78c254760b002c60c7dec1836 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:32:48Z |
| publishDate | 2022-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-4e5b92e78c254760b002c60c7dec18362022-12-22T03:25:05ZengeLife Sciences Publications LtdeLife2050-084X2022-05-011110.7554/eLife.77019Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and miceVasiliki-Ilya Gargareta0Josefine Reuschenbach1Sophie B Siems2https://orcid.org/0000-0002-7760-2507Ting Sun3https://orcid.org/0000-0002-7104-7215Lars Piepkorn4Carolina Mangana5Erik Späte6Sandra Goebbels7Inge Huitinga8Wiebke Möbius9https://orcid.org/0000-0002-2902-7165Klaus-Armin Nave10https://orcid.org/0000-0001-8724-9666Olaf Jahn11https://orcid.org/0000-0002-3397-8924Hauke B Werner12https://orcid.org/0000-0002-7710-5738Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyNeuroproteomics Group, Department of Molecular Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany; Translational Neuroproteomics Group, Department of Psychiatry and Psychotherapy, University Medical Center Göttingen, Georg-August-University, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyUniversity of Amsterdam, Swammerdam Institute for Life Sciences, Brain Plasticity Group, Amsterdam, Netherlands; Neuroimmunology Group, Netherlands Institute for Neuroscience, Amsterdam, NetherlandsDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany; Electron Microscopy Unit, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyNeuroproteomics Group, Department of Molecular Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany; Translational Neuroproteomics Group, Department of Psychiatry and Psychotherapy, University Medical Center Göttingen, Georg-August-University, Göttingen, GermanyDepartment of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, GermanyHuman 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 identified exclusively or predominantly in human or mouse myelin. This is exemplified by peripheral myelin protein 2 (PMP2), which was specific to human central nervous system myelin, while tetraspanin-2 (TSPAN2) and connexin-29 (CX29/GJC3) were confined to mouse myelin. Assessing published scRNA-seq-datasets, human and mouse oligodendrocytes display well-correlating transcriptome profiles but divergent expression of distinct genes, including Pmp2, Tspan2, and Gjc3. A searchable web interface is accessible via www.mpinat.mpg.de/myelin. Species-dependent diversity of oligodendroglial mRNA expression and myelin protein composition can be informative when translating from mouse models to humans.https://elifesciences.org/articles/77019Oligodendrocytemyelin sheathaxon-glia interactionlabel-free proteomicsscRNA-seqcross-species comparison |
| spellingShingle | Vasiliki-Ilya Gargareta Josefine Reuschenbach Sophie B Siems Ting Sun Lars Piepkorn Carolina Mangana Erik Späte Sandra Goebbels Inge Huitinga Wiebke Möbius Klaus-Armin Nave Olaf Jahn Hauke B Werner Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice eLife Oligodendrocyte myelin sheath axon-glia interaction label-free proteomics scRNA-seq cross-species comparison |
| title | Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| title_full | Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| title_fullStr | Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| title_full_unstemmed | Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| title_short | Conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| title_sort | conservation and divergence of myelin proteome and oligodendrocyte transcriptome profiles between humans and mice |
| topic | Oligodendrocyte myelin sheath axon-glia interaction label-free proteomics scRNA-seq cross-species comparison |
| url | https://elifesciences.org/articles/77019 |
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