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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. 
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Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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Prion-like Spreading in Tauopathies.

Jacob I Ayers1, Benoit I Giasson1, David R Borchelt1

  • 1Department of Neuroscience, University of Florida, Gainesville, Florida; Center for Translational Research in Neurodegenerative Disease, University of Florida, Gainesville, Florida; McKnight Brain Institute, University of Florida, Gainesville, Florida.

Biological Psychiatry
|May 17, 2017
PubMed
Summary

Misfolded tau proteins in neurodegenerative diseases may act like prions, spreading and causing distinct pathologies. Different tau strains explain the varied characteristics seen in tauopathies like Alzheimer's disease.

Keywords:
Alzheimer’s diseaseAnimal modelsPrionStrainsTauTransmission

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Tau is a microtubule-associated protein crucial for neuronal cytoskeleton dynamics.
  • Misfolded and aggregated tau forms pathological structures in neurodegenerative diseases, including Alzheimer's disease (AD) and tauopathies.
  • Tauopathies exhibit diverse clinical and pathological features, with sporadic (e.g., AD) and familial etiologies.

Purpose of the Study:

  • To review the clinical, pathological, and genetic diversity of tauopathies.
  • To explore the emerging understanding of tauopathies based on prion-like tau propagation.
  • To discuss how distinct tau strains may explain the unique characteristics of different tauopathies.

Main Methods:

  • Review of existing clinical, pathological, and genetic data on tauopathies.
  • Analysis of evidence supporting prion-like features of misfolded tau.
  • Examination of cell and animal model studies demonstrating tau propagation and strain diversity.

Main Results:

  • Evidence suggests misfolded tau possesses prion-like properties, explaining tauopathy progression.
  • Misfolded tau propagates cell-to-cell and region-to-region via neuroanatomical connections.
  • Experimentally propagated tau forms distinct strains with unique biochemical, morphological, and neuropathological profiles.

Conclusions:

  • The diversity in tauopathies may be attributed to the specific strain of misfolded tau propagating within the brain.
  • Understanding tau strains offers insights into the distinct pathological features of various tauopathies.
  • Prion-like tau propagation provides a framework for explaining the heterogeneity of tau-related neurodegenerative diseases.