Premium
The relationship between oxidative SOD1 and Abeta production and aggregation
Author(s) -
Li Chen,
Chen Xueping,
Li Xin-min,
Kong Jiming
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.521.12
Subject(s) - sod1 , genetically modified mouse , chemistry , oxidative stress , transgene , spinal cord , cortex (anatomy) , oxidative phosphorylation , mutant , superoxide dismutase , biochemistry , microbiology and biotechnology , biology , neuroscience , gene
To determine the relationship between SOD1 oxidation and amyloid beta production and aggregation, we used ELISA to analysis soluble and insoluble Aβ 40 and Aβ 42 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 Aβ 40 in cortex was significant higher in 6 month old G37R mice than in non‐transgenic mice. The soluble and insoluble Aβ 42 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 Aβ 40 and Aβ 42 in the brain and in the spinal cord. The oxidative SOD1 aggregations and Aβ 40 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.