Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
Lars Piepkorn
Neuroproteomics 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, Germany
Carolina Mangana
Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
Erik Späte
Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
Sandra Goebbels
Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
Inge Huitinga
University of Amsterdam, Swammerdam Institute for Life Sciences, Brain Plasticity Group, Amsterdam, Netherlands; Neuroimmunology Group, Netherlands Institute for Neuroscience, Amsterdam, Netherlands
Department of Neurogenetics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany; Electron Microscopy Unit, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
Neuroproteomics 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, Germany
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.