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Reduced SOD2 expression does not influence prion disease course or pathology in mice
Simote T Foliaki1, Brent Race2, Katie Williams1
1Prion Cell Biology Unit, Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, United States of America.
Plos One
|November 4, 2021
Summary
Reduced levels of the antioxidant enzyme superoxide dismutase 2 (SOD2) do not accelerate prion disease progression or cause spongiform changes in mice. SOD2 changes are likely secondary to prion disease toxicity.
Area of Science:
- Neuroscience
- Biochemistry
- Pathology
Background:
- Prion diseases, or transmissible spongiform encephalopathies, are progressive neurodegenerative disorders.
- These diseases are characterized by spongiform changes in the brain and increased oxidative damage.
- Superoxide dismutase 2 (SOD2) is a critical antioxidant enzyme; its absence causes spongiform encephalopathy in mice.
Purpose of the Study:
- To investigate if reduced SOD2 levels accelerate prion disease progression.
- To determine if reduced SOD2 levels contribute to spongiform change formation in prion disease.
Main Methods:
- Used SOD2 heterozygous knock-out mice and wild-type littermate controls.
- Infected mice with three strains of mouse-adapted scrapie.
- Assessed neuronal long-term potentiation, disease duration, pathology, and spongiform change severity.
Main Results:
- Reduced SOD2 expression did not influence disease duration or pathology.
- No effect of reduced SOD2 was observed on neuronal long-term potentiation.
- The degree of spongiform change was not affected by SOD2 levels.
Conclusions:
- Changes in SOD2 during prion disease are likely a consequence of disease-induced toxicity, not a cause.
- Reduced SOD2 levels do not play a critical role in the development of spongiform pathology in prion diseases.
