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Basic Science and Pathogenesis.

Rodrigo Francisco Tomas1, Huong T Phuong2, Logan R Bell2

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

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|December 24, 2025
PubMed
Summary
This summary is machine-generated.

A specific gene variant (CASP8-GGGAGA-AD-R1) linked to Alzheimer's disease (AD) increases toxic polyGR protein aggregation. Oxidative stress exacerbates this, contributing to AD's tau pathology and caspase-8 activation.

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Area of Science:

  • Neuroscience
  • Genetics
  • Cell Biology

Background:

  • Alzheimer's disease (AD) affects millions, with unclear causes for most sporadic cases.
  • Pathological hallmarks include tau tangles and amyloid plaques.
  • A CASP8 gene repeat expansion (RE) variant, CASP8-GGGAGA-AD-R1, is linked to increased AD risk.

Purpose of the Study:

  • Investigate disease mechanisms of the CASP8-GGGAGA-AD-R1 variant.
  • Determine the role of CASP8 polyGR-containing proteins in AD pathogenesis.

Main Methods:

  • Transfected SH-SY5Y cells with CASP8 variants to express polyGR proteins.
  • Induced oxidative stress using hydrogen peroxide (H2O2).
  • Analyzed protein levels of polyGR, phosphorylated tau (p-tau), and caspases via immunofluorescence.

Main Results:

  • PolyGR-positive cells showed increased caspase-8 (1.9-fold) and p-tau (2.4-fold).
  • Oxidative stress significantly increased CASP8 polyGR protein (16-fold) and p-tau (1.5-fold) levels.
  • Caspase-3 levels did not increase similarly.

Conclusions:

  • PolyGR aggregates contribute to tau pathology and caspase-8 activation in AD.
  • Oxidative stress promotes polyGR accumulation, worsening AD pathological hallmarks.