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Transthyretin amyloidosis and two other aging-related amyloidoses in an aged vervet monkey

S Nakamura1, S Okabayashi, N Ageyama

  • 1The Corporation for Production and Research of Laboratory Primates, Tsukuba, Ibaraki, Japan. snakamur@belle.shiga-med.ac.jp

Veterinary Pathology
|January 15, 2008
PubMed

Insights

This study reports the first known case of spontaneous transthyretin amyloidosis in an aged vervet monkey, alongside other aging-related amyloids. This finding offers insights into comparative aging and amyloid disease mechanisms.

Area of Science:

  • Veterinary Pathology
  • Comparative Pathology
  • Aging Research

Background:

  • Amyloidosis is a group of diseases characterized by the deposition of misfolded proteins (amyloids) in various organs.
  • Senile systemic amyloidosis, typically involving transthyretin amyloid, is a common age-related condition in humans.
  • Understanding amyloidosis in non-human primates can provide valuable insights into human aging and disease processes.

Observation:

  • An aged male vervet monkey presented with chronic cardiac arrhythmia.
  • Post-mortem examination revealed multifocal transthyretin amyloid deposition throughout the heart and systemic organs, excluding the liver and spleen.
  • Additional amyloid deposits of amyloid beta protein and islet amyloid polypeptide were identified in the brain and pancreas, respectively.

Findings:

  • The study identified three distinct aging-related amyloids in the vervet monkey: transthyretin, amyloid beta protein, and islet amyloid polypeptide.
  • Transthyretin amyloidosis was widespread in the heart and systemic organs, mimicking human senile systemic amyloidosis.
  • This marks the first reported instance of spontaneous transthyretin amyloidosis in an animal model.

Implications:

  • This case highlights the potential for spontaneous amyloidosis in non-human primates, serving as a model for human aging diseases.
  • The co-occurrence of multiple amyloid types provides a unique opportunity to study their interactions and pathological pathways.
  • Further research in this area could lead to novel therapeutic strategies for age-related amyloidosis in both animals and humans.

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