Examining the spread of toxic proteins

Researchers think a cascade reaction is responsible: Mutations in the gene produce misshapen huntingtin, which causes its normal counterparts to change shape and form clumps. Over time, the brain becomes less able to rid itself of these aggregates, which accumulate and damage neurons, cells that transmit and receive messages.  

Research by Maggie Panning Pearce, PhD, an associate professor in the Department of Biological and Biomedical Sciences in the College of Science & Mathematics, implicates other brain cells called glia. As a postdoc, she demonstrated that glia remove huntingtin aggregates, but that, over time, these cells lose this ability and instead contribute to spreading the clumps.

“I want to determine, how this is happening?” Pearce says. “If we can figure out how glia control not only the burden of aggregates in the brain, but also their ability to spread, maybe we could identify targets for new therapies that could slow disease progression.” 

Her research has implications beyond Huntington’s. Researchers have documented a similar process, in which malformed proteins seed the formation of toxic aggregates, in other neurodegenerative diseases, including Alzheimer’s, Parkinson’s and amyotrophic lateral sclerosis.

She also studies frontotemporal dementia, degenerative disorders with similarities to Alzheimer’s but that tend to affect younger people. 

“We’d like to understand if glia are involved in other disorders as we think they are in Huntington’s,” she said. “That would open up potential for new therapies that target not just neurons, the focus of the field for decades, but also other cell types.”

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