Commentary: Alpha-synuclein interacts with SOD1 and promotes its oligomerization

• Verfasst von: Helferich, Anika Marie [VerfasserIn]
• Verfasst von: McLean, Pamela J. [VerfasserIn]
• Verfasst von: Weishaupt, Jochen H. [VerfasserIn]
• Verfasst von: Danzer, Karin M. [VerfasserIn]
• Titel: Commentary: Alpha-synuclein interacts with SOD1 and promotes its oligomerization
• Verf.angabe: Anika M. Helferich, Pamela J. McLean, Jochen H. Weishaupt, and Karin M. Danzer
• E-Jahr: 2016
• Jahr: 2016 Nov 14
• Umfang: 3 S.
• Teil: volume:1
• Teil: year:2016
• Teil: number:7
• Teil: pages:28-30
• Teil: extent:3
• Fussnoten: Gesehen am 15.07.2021
• Titel Quelle: Enthalten in: Journal of neurology & neuromedicine
• Ort Quelle: Grand Rapids, MI : Sciaccess Publishers, LLC, 2016
• Jahr Quelle: 2016
• Band/Heft Quelle: 1(2016), 7, Seite 28-30
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1762994984

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.