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Basic Science and Pathogenesis.

Huong T Phuong1, Rodrigo Francisco Tomas1, Cemal Akamese1

  • 1University of Florida, Gainesville, FL, USA.

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Summary
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New findings reveal poly-Glycine-Arginine (polyGR+) aggregates in Alzheimer's disease (AD) brains correlate with amyloid plaques and tau tangles. These aggregates also disrupt the autophagy-lysosomal pathway, a key cellular process.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Alzheimer's disease (AD) is a prevalent neurodegenerative disorder affecting individuals over 65, characterized by cognitive decline, beta-amyloid (Aβ) plaques, and hyperphosphorylated tau (pTau) tangles.
  • The precise molecular mechanisms underlying AD pathogenesis remain incompletely understood.
  • Recent research identified poly-Glycine-Arginine containing (polyGR+) aggregates in AD autopsy brains, with specific CASP8 gene variants linked to increased AD risk.

Purpose of the Study:

  • To investigate the association between polyGR+ aggregates and established AD pathological hallmarks, namely Aβ plaques and pTau tangles.
  • To determine if polyGR+ aggregates are linked to the disruption of the autophagy-lysosomal pathway, crucial for cellular protein homeostasis.

Main Methods:

  • Immunohistochemical staining was performed on hippocampal sections from 133 AD cases, 30 controls, and 15 primary age-related tauopathy (PART) cases to assess polyGR+, Aβ, and pTau levels.
  • Double immunofluorescence staining was used to examine the co-localization of polyGR+ aggregates with autophagy-lysosomal markers (p62 and LC3B).

Main Results:

  • PolyGR+ aggregates were frequently observed in approximately 50% of AD brains but were absent in control and PART cases (p < 0.0001).
  • Significant positive correlations were found between polyGR+ staining levels and both Aβ (R²=0.2544, p=0.0007) and pTau (R²=0.2822, p=0.0003) deposition in the hippocampus.
  • PolyGR+ aggregates demonstrated co-localization with p62 and LC3B, indicating an association with the autophagy-lysosomal pathway.

Conclusions:

  • PolyGR+ aggregates represent a significant protein-pathological feature in Alzheimer's disease brains.
  • The co-localization of polyGR+ aggregates with autophagy and proteasome markers suggests dysregulation of the autophagy-lysosomal pathway, contributing to AD pathogenesis.