Neurodegenerative diseases like Alzheimer’s and Parkinson’s are a growing health concern in the United States. The Parkinson’s Foundation currently estimates that around 1.1 million Americans are diagnosed with Parkinson’s disease, and nearly 90,000 more people join their ranks every year.
People with Parkinson’s disease often experience motor issues, such as tremors, trouble with balance, and slowed movement. These symptoms are caused by the accumulation of misfolded α-synuclein in motor cells in the brain. As α-synuclein spreads between neurons, symptoms worsen.
One way α-synuclein could enter new cells is by binding to surface proteins. To determine whether this was the case, Strittmatter and his colleagues created 4,400 batches of cells, each expressing different cell surface proteins, and observed whether they bound to misfolded α-synuclein.
Most cell surface proteins did not. But 16 did, including two found in the human dopamine neurons of the substantia nigra, a region of the brain that degenerates in Parkinson’s disease. The researchers found that these two, called mGluR4 and NPDC1, transported misfolded α-synuclein into the cell.
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