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Aggregation of MBP in chronic demyelination
Kati Frid1, Ofira Einstein1, Yael Friedman-Levi1
1Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital Jerusalem, 91120, Israel.
Annals of Clinical and Translational Neurology
|August 15, 2015
Summary
Myelin basic protein (MBP) aggregates in neurodegenerative phases of multiple sclerosis (MS). This prion-like misfolding, linked to altered brain lipids, may drive neuronal damage in progressive MS.
Area of Science:
- Neuroscience
- Neuroimmunology
- Protein Misfolding Diseases
Background:
- Neurodegenerative diseases involve protein misfolding into insoluble aggregates.
- Multiple Sclerosis (MS) is a demyelinating disease affecting the central nervous system.
Purpose of the Study:
- Investigate if myelin basic protein (MBP) exhibits prion-like aggregation in animal models of MS.
- Determine MBP's role in the neurodegenerative phases of demyelinating diseases.
Main Methods:
- Studied animal models of multiple sclerosis (MS), including Cuprizone-induced demyelination and Experimental Autoimmune Encephalomyelitis (EAE).
- Assessed MBP aggregation and its co-precipitation with Tau.
- Analyzed brain membrane lipid composition using Triton X-100 floatation gradients.
Main Results:
- MBP did not decrease in total levels but formed aggregates within oligodendrocytes and around neurons in demyelinated areas.
- MBP co-precipitated with Tau in chronic EAE, a marker for neurodegeneration.
- Significant alterations in brain membrane lipid composition were observed in chronic EAE, potentially due to oxidative stress.
Conclusions:
- Prion-like aggregation of MBP in chronic demyelination may stem from aberrant lipid composition.
- MBP aggregation could contribute to neuronal damage in the progressive stages of MS.
