Mutations in cooper-zinc superoxide dismutase (SOD1) underlie 20% of familial ALS cases, and are thought to cause ALS through an acquired toxic function of the mutant SOD1 protein, which misfolds and aggregates in the cell. At the annual International Congress of Parkinson’s Disease and Movement Disorders, held June 17-23 in Berlin, Germany, researchers presented data suggesting that neurotoxic SOD1 aggregates may contribute to Parkinson’s disease (PD). The investigators were studying mechanisms of selective vulnerability of dopaminergic neurons in the substantia nigra in PD, and detected decreased copper levels in PD-patient post postmortem samples in the most vulnerable brain regions to denegeration. This prompted an analysis of SOD1 expression, a protein, whose structure and function are impacted by copper levels. Strikingly, a five-fold increase in abundance of SOD1 aggregates was observed in the substantia nigra compared to control brain regions. These findings revisit the question of whether SOD1 aggregation is a driver of neuronal death, or rather a consequence of the degenerative process.
Click here to read the report in Neurology Today.
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