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β2-Microglobulin boosts β-amyloid aggregation and neurotoxicity in an Alzheimer’s disease model

β2-Microglobulin (β2M) is an amyloidogenic protein. β2M coaggregates with β-amyloid (Aβ) in the brains of patients with Alzheimer’s disease and enhances Aβ deposition. β2M is essential for Aβ neurotoxicity in vivo, and neutralization of pathogenetic β2M–Aβ aggregates ameliorates the amyloid pathology and cognitive deficits associated with disease in a mouse model.

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Fig. 1: β2M coaggregates with Aβ and constitutes the core of amyloid plaques.

References

  1. Long, J. M. & Holtzman, D. M. Alzheimer disease: an update on pathobiology and treatment strategies. Cell 179, 312–339 (2019). This article reviews AD pathobiology and treatment strategies, highlighting clinical trials and opportunities for developing disease-modifying therapies.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  2. Yu, Y. J. & Watts, R. J. Developing therapeutic antibodies for neurodegenerative disease. Neurotherapeutics 10, 459–472 (2013). This review article discusses traditional antibody drug development for neurodegenerative diseases and new technologies for improved delivery of antibodies to the brain.

    Article  PubMed  PubMed Central  Google Scholar 

  3. Fuller, J. P., Stavenhagen, J. B. & Teeling, J. L. New roles for Fc receptors in neurodegeneration—the impact on immunotherapy for Alzheimer’s Disease. Front. Neurosci. 8, 235 (2014). This review article discusses Fcγ receptor expression, function and proposed roles in multiple age-related neurological diseases.

    Article  PubMed  PubMed Central  Google Scholar 

  4. Eichner, T. et al. Conformational conversion during amyloid formation at atomic resolution. Mol. Cell 41, 161–172 (2011). This paper describes the structure of an amyloidogenic state of β2-microglobulin and how it forms amyloid.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

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This is a summary of: Zhao, Y. et al. β2-Microglobulin coaggregates with Aβ and contributes to amyloid pathology and cognitive deficits in Alzheimer’s disease model mice. Nat. Neurosci. https://doi.org/10.1038/s41593-023-01352-1 (2023).

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β2-Microglobulin boosts β-amyloid aggregation and neurotoxicity in an Alzheimer’s disease model. Nat Neurosci 26, 1143–1144 (2023). https://doi.org/10.1038/s41593-023-01354-z

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