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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Reduced Autophagy in Aged Trigeminal Neurons Causes Amyloid β Diffusion.

R Sonoda1,2, E Kuramoto2, S Minami1,2

  • 1Department of Periodontology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima, Japan.

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|March 15, 2023
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Summary

Impaired autophagy in aging trigeminal neurons may drive Alzheimer's disease (AD) by allowing amyloid-beta (Aβ) oligomers to spread. This study investigates how Vmes neuron degeneration affects Aβ diffusion and AD pathogenesis.

Keywords:
Alzheimer’s diseaseagingautophagosomebeta amyloidhomeostasistrigeminal nuclei

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Gerontology

Background:

  • The link between oral health and Alzheimer's disease (AD) in the elderly remains unclear.
  • The role of trigeminal nervous system aging and neurodegeneration in AD pathogenesis, specifically amyloid-beta (Aβ) oligomer accumulation, is unknown.
  • Selective autophagy's function in the trigeminal mesencephalic nucleus (Vmes) concerning Aβ oligomer diffusion requires investigation.

Purpose of the Study:

  • To examine selective autophagy and Aβ oligomer processing in aging Vmes neurons.
  • To determine if Vmes neuron degeneration influences Aβ oligomer diffusion.
  • To elucidate the role of autophagy in maintaining Vmes neuron homeostasis and its relation to AD development.

Main Methods:

  • Utilized female transgenic 3xTg-AD and App knock-in mice (2-8 months old).
  • Conducted immunohistochemical analysis of aging-related changes in selective autophagy and Aβ processing within the Vmes.
  • Induced Vmes neuron degeneration via maxillary molar extraction to assess Aβ oligomer kinetics.

Main Results:

  • Autophagosome-like membranes positive for Aβ, HO-1, and LC3B were found in Vmes neurons of 3xTg-AD mice.
  • Extracellular Aβ42 oligomers and clusters were prominent in App mice, with increased diffusion linked to Rubicon expression (indicating autophagy deterioration) and Vmes neuron aging.
  • Tooth extraction elevated extracellular Aβ42 oligomer levels in App mice.

Conclusions:

  • Autophagy is crucial for maintaining homeostasis in Vmes neurons.
  • Aging or neurodegeneration-induced autophagy impairment promotes Aβ42 oligomer diffusion into the extracellular space.
  • This diffusion may contribute to the pathogenesis of Alzheimer's disease.