Commentary: Alpha-synuclein interacts with SOD1 and promotes its oligomerization
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...
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| Main Authors: | , , , |
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| Format: | Article (Journal) Editorial |
| Language: | English |
| Published: |
2016 Nov 14
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| In: |
Journal of neurology & neuromedicine
Year: 2016, Volume: 1, Issue: 7, Pages: 28-30 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5108581/
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| Author Notes: | Anika M. Helferich, Pamela J. McLean, Jochen H. Weishaupt, and Karin M. Danzer |
| Summary: | 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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| Item Description: | Gesehen am 15.07.2021 |
| Physical Description: | Online Resource |