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Basic Science and Pathogenesis.

Yifei Cai1, Iguaracy Pinheiro-de-Sousa2, Mykhaylo Slobodyanyuk3

  • 1Yale University, New Haven, CT, USA.

Alzheimer'S & Dementia : the Journal of the Alzheimer'S Association
|December 23, 2025
PubMed
Summary
This summary is machine-generated.

Alzheimer's disease disrupts the myelin-axon interface, leading to protein aggregation and altered neuro-glial communication. This study reveals molecular changes at this critical junction, offering insights into disease mechanisms.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Proteomics

Background:

  • Myelin ensheathment is crucial for neuronal function, supporting rapid electrical conduction and plasticity.
  • Alzheimer's disease (AD) is characterized by myelin and axonal disruptions, but the underlying molecular mechanisms are unclear.

Purpose of the Study:

  • To investigate the molecular and cellular mechanisms driving myelin-axon disruption in Alzheimer's disease.
  • To uncover novel signaling pathways and cellular interactions at the myelin-axon interface in AD.

Main Methods:

  • Utilized proximity labeling subcellular proteomics on postmortem human brains and AD-model mice.
  • Developed computational algorithms to analyze cell-cell communication and disruption.
  • Employed super-resolution expansion and confocal microscopy to visualize myelin-axon pathology.

Main Results:

  • Discovered dysregulated signaling pathways, including those in beta-amyloid processing, axonal outgrowth, and lipid metabolism.
  • Identified beta-amyloid aggregation within the myelin-axon interface.
  • Observed reduced paranode density and aberrant myelination around dystrophic axons in AD.

Conclusions:

  • The myelin-axon interface is a key site for protein aggregation and disrupted neuro-glial communication in Alzheimer's disease.
  • Uncovered molecular architecture of the myelin-axon interface provides a basis for future AD research.