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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus
Published on: June 17, 2015
Diffusible amyloid oligomers trigger systemic amyloidosis in mice
Sivanesan Senthilkumar1, Edwin Chang, Rajadas Jayakumar
1Bioorganic and Neurochemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India.
The Biochemical Journal
|June 20, 2008
Summary
Amyloid A (AA) amyloidosis is accelerated by injecting AA-laden tissue extracts. These extracts contain toxic globular oligomers that seed amyloid deposition and alter cytokine expression, worsening AA amyloidosis.
Area of Science:
- Biochemistry
- Immunology
- Pathology
Background:
- AA amyloidosis is a systemic inflammatory disease.
- Amyloid fibrils are known to enhance amyloid deposition via nucleation seeding.
- Globular aggregates, not fibrils, are suspected toxic entities in amyloidosis.
Purpose of the Study:
- To investigate the structural and morphological features of amyloid-enhancing factor (AEF).
- To identify the primary amyloidogenic material within active AEF.
- To explore the relationship between altered cytokine expression and AA accumulation.
Main Methods:
- Extraction and partial purification of AEF from amyloid-laden mouse spleen.
- Intravenous injection of partially purified AEF into mice to assess amyloid deposition.
- Analysis of structural and morphological features of amyloidogenic material in AEF.
- Assessment of cytokine expression in systemically inflamed tissues.
Main Results:
- The primary amyloidogenic material in active AEF consists of diffusible globular oligomers.
- Injection of active AEF triggered amyloid deposition in vital organs.
- An association was observed between altered cytokine expression and AA accumulation.
- Serum AA monomers and proteolytic oligomers in spleen AEF suggest extrahepatic processing.
Conclusions:
- Toxic globular oligomers in AEF can seed amyloid deposition and potentially induce altered cytokine expression.
- Extrahepatic processing of serum AA may lead to local amyloidogenic protein accumulation.
- AEF's globular oligomers play a crucial role in accelerating AA amyloidosis.
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...