Human myelin proteome and comparative analysis with mouse myelin
Open accessAbstract
Myelin, formed by oligodendrocytes (OLs) in the CNS, is critical for axonal functions, and its damage leads to debilitating neurological disorders such as multiple sclerosis. Understanding the molecular mechanisms of myelination and the pathogenesis of human myelin disease has been limited partly by the relative lack of identification and functional characterization of the repertoire of human myelin proteins. Here, we present a large-scale analysis of the myelin proteome, using the shotgun approach of 1-dimensional PAGE and liquid chromatography/tandem MS. Three hundred eight proteins were commonly identified from human and mouse myelin fractions. Comparative microarray analysis of human white and gray matter showed that transcripts of several of these were elevated in OL-rich white matter compared with gray matter, providing confidence in their detection in myelin. Comparison with other databases showed that 111 of the identified proteins/transcripts also were expressed in OLs, rather than in astrocytes or neurons. Comparison with 4 previous myelin proteomes further confirmed more than 50% of the identified proteins and revealed the presence of 163 additional proteins. A select group of identified proteins also were verified by immunoblotting. We classified the identified proteins into biological subgroups and discussed their relevance in myelin biogenesis and maintenance. Taken together, the study provides insights into the complexity of this metabolically active membrane and creates a valuable resource for future in-depth study of specific proteins in myelin with relevance to human demyelinating diseases.
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BIN1 was one of the 308 proteins identified in both human and mouse brain myelin preparations by mass spectrometry.
“Entirely consistent with our findings, BIN1 was one of the 308 proteins identified in both human and mouse brain myelin preparations by mass spectrometry [50].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [50]
BIN1 transcript levels are higher in human white matter than gray matter according to independent microarray analyses.
“This finding is in agreement with the comparison of BIN1 transcript levels between the human white matter and the gray matter reported from independent microarray analyses [50, 52, 53].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [50]
BIN1 was identified in human and mouse brain myelin preparations by proteomic analysis.
“proteomic identification of BIN1 in human and mouse brain myelin preparations [50].”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [50]
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White Matter Changes in Schizophrenia: Evidence for Myelin-Related Dysfunction
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“RAC1 signaling is important for myelin sheath formation (19) and growth of astrocytic processes (20).”
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- [23]Trapp BD, Pfeiffer SE, Anitei M, Kidd GJ (2004) Cell biology of myelin assembly. Myelin Biology and Disorders , ed Lazzarini RA (Elsevier, New York), pp 29-55.
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Dynamics and Mechanisms of CNS Myelination
Bercury, K. K., & Macklin, W. B. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.016 · Cited by 320 · see citing works
Central nervous system myelin: structure, synthesis and assembly
Aggarwal, S., Yurlova, L., & Simons, M. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.004 · Cited by 301 · see citing works
De Rossi, P., Buggia-Prévot, V., Clayton, B. L. L., Vasquez, J. B., van Sanford, C., Andrew, R. J., Lesnick, R., Botté, A., Deyts, C., Salem, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0124-1 · Cited by 151 · see citing works
“This finding is in agreement with the comparison of BIN1 transcript levels between the human white matter and the gray matter reported from independent microarray analyses [50, 52, 53].”
Stys, P. K. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.06.004 · Cited by 51 · see citing works
- Authors
- Ishii, A., Dutta, R., Wark, G. M., Hwang, S.-I., Han, D. K., Trapp, B. D., Pfeiffer, S. E., & Bansal, R.
- Affiliations
- University of Connecticut (US)
- Cleveland Clinic (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-08-25
- Volume
- 106
- Issue
- 34
- Pages
- 14605-14610
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2732873
- OpenAlex
- W2095208158
- Cited by
- 119
- References
- 3
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 3 · 2023: 5 · 2022: 6 · 2021: 8 · 2020: 7 · 2019: 4 · 2018: 5 · 2017: 10 · 2016: 7 · 2015: 12 · 2014: 4 · 2013: 7 · 2012: 10
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL067569)
- National Institute of Neurological Disorders and Stroke (R01NS041078, P01NS038667)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- oligodendrocytes, myelination, white matter, gray matter, demyelinating disease, multiple sclerosis, myelin biogenesis, myelin maintenance, comparative proteomics
- MeSH terms
- Aged, Animals, Brain, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Female, Humans, Male, Mice, Inbred C57BL, Middle Aged, Myelin Sheath, Immunoblotting, Cluster Analysis, Oligonucleotide Array Sequence Analysis, Proteome, Gene Expression Profiling, Proteomics, Mice, Tandem Mass Spectrometry
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