WEST LAFAYETTE, Ind. - Purdue University researchers revealed how a mutation in a protein shuts down a protective function needed to prevent the death of neurons in Parkinson's disease, possibly opening the door to new drug strategies to treat the disorder.
Fred Regnier, the J.H. Law Distinguished Professor of Chemistry, and Jean-Christophe Rochet, an associate professor of medicinal chemistry and molecular pharmacology, led the team that discovered how the protein DJ-1, which plays a significant role in protecting neurons from damage, is shut down by a subtle mutation.
A substitution in one link of the chain of amino acids that makes up the protein renders it unable to be activated to protect neurons from the build up of protein "aggregates," or "clumps," that lead to cell death in those with Parkinson's disease.
"The saying that you are only as strong as your weakest link appears to hold true in the case of the chain of amino acids that make up a protein," Regnier said. "The magnitude of the effect of this subtle change is surprising. It can make the difference between having a disease and being healthy."
According to the Parkinson's Disease Foundation, an estimated 7 million to 10 million people worldwide are living with the disease, which is a neurodegenerative disorder that causes muscular rigidity, slowness of movement, poor balance and tremors. The death of neurons in a region of the brain called the substantia nigra cause the symptoms.
The findings of the Purdue-led study could potentially lead to new Parkinson's treatments, Rochet said.
"The current methods of treatment are to add back what the lost cells used to produce, similar to hormone replacement therapies," he said. "Understanding this error in a key protein could help researchers find a way to prevent cell death in the first place. Perhaps a compound could be found that could correct the problem and resurrect the protective function of the
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