Abstract
Alpha-synuclein and Cu, Zn superoxide dismutase (SOD1) are both aggregation-prone proteins that are associated with Parkinson´s disease (PD) and amyotrophic lateral sclerosis (ALS), respectively. Recently, we showed that alpha-synuclein interacts with SOD1 in various cell types and tissues. Using a cell culture model, we also found that alpha-synuclein nucleates the polymerization of SOD1. Here, we discuss the current literature regarding their interaction and their co-localization in aggregates of human post-mortem tissue. Furthermore we comment on the reported alpha-synuclein-induced SOD1 polymerization in terms of cross-seeding effects in neurodegeneration.
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CITATION STYLE
Danzer, K. (2016). Commentary: alpha-synuclein interacts with SOD1 and promotes its oligomerization. Journal of Neurology and Neuromedicine, 1(7), 28–30. https://doi.org/10.29245/2572.942x/2016/7.1065
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