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Credit: Zach Sheldon

A recent Penn Medicine study has shown that a certain misfolded protein implicates a different type of neurodegenerative disorder depending on the type of cell the protein is in.

According to Penn Medicine News, this breakthrough lead by Penn Pathology and Laboratory professor Virginia Lee's group, is speculated to allow for targeted therapies to help those with these disorders. No study has ever shown that cell type leads to a different variety of malformed protein in any other type of neurodegenerative disorder.

This study, which was published in Nature earlier this month, showed a direct correlation between a strain of α-synuclein proteins and Multiple System Atrophy, according to Penn Medicine News. MSA is a rare, neurodegenerative disease that shares many symptoms with Parkinson’s disease, according to Mayo Clinic. Treatment exists, but there is currently no cure. 

Lee's lab showed how the different sorts of aggregation of α-synuclein proteins was found in MSA and Parkinson’s disease, according to Penn Medicine. The study showed how α-synuclein proteins affected glial cytoplasmic inclusions, which are found in MSA, differently than Lewy Bodies in Parkinson's disease. 

In a past study by Lee's group in 2011, the researchers had shown how α-synuclein fibrils acted as "seeds" inducing the aggregation leading to these disorders, according to Penn Medicine News. The study found that healthy neurons took up α-synuclein fibrils, leading to the formation of bodies which impacted neuron function and leading to nerve cell death. 

The next steps for this project is looking to uncover the underlying molecular mechanism for the difference between the α-synuclein protein strains, according to Penn Medicine News. 

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