ArticleScientific reports2025
Amyloid fibrils of the myelin basic protein are an integral component of myelin in the vertebrate brain.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Article
- Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences.International journal of molecular sciences · 2025Review
- Review
- [Association of Myelin Basic Protein and S100 Calcium-Binding Protein B With the Risk of Early Neurological Deterioration After Interventional Therapy for Cerebral Infarction].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025Article
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Authors and funding
6 authors.
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Abstract
The myelin basic protein (MBP) is the most abundant intracellular protein of the myelin, which forms the electrically insulating sheath of axons of many actively functioning neurons. This protein binds the opposite membranes of the flattened processes of oligodendrocytes and plays a crucial role in myelin compaction. Here we show that MBP is present in amyloid form in the oligodendrocytes in the brain of vertebrates. It forms SDS-resistant insoluble aggregates and clearly colocalizes with Congo Red and Thioflavin S in vivo, ex vivo, and in vitro. The fibrils of MBP extracted from the brain are detected by electron microscopy and exhibit apple-green birefringence after Congo Red staining. We showed that the central region of MBP, spanning amino acid residues 60-119, is responsible for the formation of amyloid fibrils. Based on these data, we present a model in which MBP not only connects the opposite membranes of oligodendrocyte processes but also provides longitudinal amyloid stitching of myelin sheaths. Amyloid fibrils appear to be an ideal natural material for myelin compaction and axon insulation.
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