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Assay Development for High Content Quantification of Sod1 Mutant Protein Aggregate Formation in Living Cells
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Commentary: alpha-synuclein interacts with SOD1 and promotes its oligomerization.
Anika M Helferich1, Pamela J McLean2, Jochen H Weishaupt1
1Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany.
Journal of Neurology & Neuromedicine
|November 18, 2016
Summary
Alpha-synuclein protein interacts with copper, zinc superoxide dismutase (SOD1) and promotes its polymerization. This interaction is relevant to neurodegenerative diseases like Parkinson's disease and amyotrophic lateral sclerosis.
Area of Science:
- Neuroscience
- Biochemistry
- Protein Misfolding Diseases
Background:
- Alpha-synuclein aggregation is linked to Parkinson's disease (PD).
- Copper, zinc superoxide dismutase (SOD1) mutations are associated with amyotrophic lateral sclerosis (ALS).
- Both proteins are prone to aggregation.
Purpose of the Study:
- To investigate the interaction between alpha-synuclein and SOD1.
- To explore the role of alpha-synuclein in SOD1 polymerization.
- To discuss the implications of this interaction in neurodegeneration.
Main Methods:
- Cell culture models were used to study protein interactions.
- Analysis of human post-mortem tissue for protein co-localization.
- Literature review on alpha-synuclein and SOD1 interactions.
Main Results:
- Alpha-synuclein interacts with SOD1 in various cell types and tissues.
- Alpha-synuclein was found to nucleate SOD1 polymerization in cell culture.
- Co-localization of alpha-synuclein and SOD1 in aggregates within human post-mortem tissue.
Conclusions:
- Alpha-synuclein and SOD1 interact and co-aggregate in neurodegenerative diseases.
- Alpha-synuclein can induce SOD1 polymerization, suggesting cross-seeding mechanisms.
- This interaction may contribute to the pathogenesis of PD and ALS.
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