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Published on: September 29, 2019
Systemic AA amyloidosis in the common marmoset
E Ludlage1, C L Murphy, S M Davern
1New England Primate Research Center, Harvard Medical School, Southborough, MA 01772-9012, USA. elisabeth_ludlage@hms.harvard.edu
Veterinary Pathology
|March 9, 2005
Summary
A study found that 17% of common marmosets in a research setting developed amyloid deposits, likely due to serum amyloid A (SAA) protein. This suggests a potential inherited condition, making marmosets a model for studying amyloidosis.
Area of Science:
- Veterinary Pathology
- Primate Research
- Biomedical Science
Background:
- The common marmoset (Callithrix jacchus) is a widely used model organism in biomedical research.
- Amyloidosis, characterized by protein deposits in organs, can affect various species.
Observation:
- A retrospective analysis examined 86 marmosets over 1 year of age euthanized due to morbidity.
- Amyloid deposits, identified as serum amyloid A (SAA)-related protein, were found in 17% of the analyzed marmosets.
- Affected organs included the liver, adrenal glands, kidneys, and intestine.
Findings:
- The amyloidosis was identified as AA or secondary amyloidosis, typically linked to inflammation and elevated SAA levels.
- No significant pathological differences were observed between marmosets with and without amyloid deposits.
- Comparable SAA concentrations in limited serum samples suggested a possible inheritable basis for the disorder.
Implications:
- The common marmoset serves as a unique experimental model for investigating the pathogenesis of AA amyloidosis.
- This model may facilitate research into novel therapeutic strategies for systemic amyloidosis in both animals and humans.
- Understanding the potential genetic predisposition is crucial for marmoset colony health and research integrity.
Related Concept Videos
03:03Amyloid Fibrils
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, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
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, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...