Parkinson’s disease is a neurodegenerative disease thatis caused by the death of dopaminergic neurons in the substantia nigra. α-Synuclein aggregation and oxidative stress have each been linked to the incidence of this neuronal loss, but the mechanisms linking these events together remain unclear. This study focused on the effects of α-synuclein expression in yeast strains lacking Cu,Zn-SOD (sod1Δ) and Mn-SOD (sod2Δ),enzymes that metabolize oxygen radicals. The sod2Δ strain expressing α-synuclein was less viable than the parent strain, while sod1Δ showed minor toxicity compared to parent strain. To examine sod2Δ toxicity further, we used live cell fluorescent microscopy to detect GFP-tagged α-synuclein localization in sod2Δ; we found no change in α-synuclein distribution compared to the parent strain. Treatments of the parent strain with 2mM H2O2 showed no change in viability or α-synuclein localization. Sod2Δ strains expressing α-synuclein were less viable when treated with H2O2 compared to untreated cells. The increased toxicity in untreated sod2Δ may be caused by increased levels of damaging oxygen radicals due to lack of Mn-SOD activity; increased toxicity due to H2O2 treatment may be caused by even higher levels of oxygen radicals.
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