The relationship between oxidative SOD1 and Abeta production and aggregation

Abstract

To determine the relationship between SOD1 oxidation and amyloid beta production and aggregation, we used ELISA to analysis soluble and insoluble Aβ40 and Aβ42 in the cortex and spinal cord and used immunofluorescence to test the co‐localization of the oxidative SOD1 aggregation and Aβ aggregation. We found that the insoluble Aβ40 in cortex was significant higher in 6 month old G37R mice than in non‐transgenic mice. The soluble and insoluble Aβ42 in cortex and spinal cord were significantly higher in 6 month old G37R mice and G93A mice than in non‐transgenic mice. The mutant SOD1 could influence the production of the soluble or insoluble Aβ40 and Aβ42 in the brain and in the spinal cord. The oxidative SOD1 aggregations and Aβ40 were co‐localized in the G93A and G37R transgenic mice, but not non‐transgenic mice. Meanwhile, the oxidative SOD1 aggregations localized in the senile plaques in the APP/PS1 mice. We speculated that mutant SOD1 was easy to be oxidated, and the oxidative SOD1 could interact with APP. SOD1 oxidation may be the earliest event that triggers SOD1 aggregation and induces Aβ aggregation. We will cross APP transgenic mice with G93A and G37R mice to further prove our conclusions.