Researchers Describe Brain Plaques Involved In Huntington's Disease

Researchers at the University of Pittsburgh School of Medicine have found that a core of protein clumps in the brains of those with Huntington's disease show distinctive structure--shedding light on molecular mechanisms that underline the neurodegernative disorder. The findings are published in the Proceedings of the National Academy of Sciences.

"Despite decades of research, the nature of the protein deposition has been unclear, which makes it difficult to design drugs that affect the process," said senior investigator Patrick C.A. van der Wel, Ph.D., assistant professor of structural biology, Pitt School of Medicine, in a news release. "Using advanced nuclear magnetic resonance spectroscopy, we were able to provide an unprecedented view of the internal structure of the protein clumps that form in the disease, which we hope will one day lead to new therapies.

"This is exciting because it may suggest new ways to intervene with these disease-causing events," Dr. van der Wel said. "For the first time, we were able to really look at the protein structure in the core of the deposits formed by the mutant protein that causes Huntington's. This is an important breakthrough that provides crucial new insights into the process of how the protein undergoes misfolding and aggregation."

Huntington's disease, as well as several other progressive brain diseases, are the result of certain proteins that aggregate to form plaques or deposits in the brain, researchers stay. Statistics suggest that the inherited condition, in which nerve cells brain down over time, affects a little under 200,000 in the United States every year.

Learning more about the neurodegenerative illness could help in understanding how these diseases like Huntington's develop and how this protein influences the illness.

The gene associated with Huntington's makes a protein that has a repetitive sequence called polyglutamine. In the 1990s, it was discovered that the patients have mutated proteins in which this sequence is too long, yet it has remained unclear how exactly this unusual mutation causes the protein to misbehave, clump together and cause the disease.

For more great science stories and general news, please visit our sister site, Headlines and Global News (HNGN).