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HarvardScience is a publication of the Harvard Office of News and Public Affairs devoted to all matters related to science at the various schools, departments, institutes, and hospitals of Harvard University.
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From left to right, Peter Lansbury, Yichin Liu, Hilal Lashuel, and Zhihua Liu uncovered a dual role for UCH-L1 that explains why a genetic variant of the enzyme may be protective against Parkinson's disease.

Photo by Graham Ramsay

Enzyme linked to pathology of Parkinson's disease appears two-faced

Protein's reckless side may lead to deadly pileups in cell

November 8, 2002

A finding by Harvard Medical School researchers adds a new wrinkle to the story of Parkinson's disease and insight into how failure to dispose of proteins can wreak havoc on a cell. Much research has focused on how the aggregated proteins found in neurodegenerative diseases like Parkinson's are produced, overproduced, folded, and eventually clumped together. But a defect in protein degradation could also lead to a pathogenic traffic jam in the cell. "The idea is that the concentration of these proteins needs to be kept below some threshold in order to avoid aggregation," said Peter Lansbury, Harvard Medical School associate professor of neurology at Brigham and Women's Hospital. The findings by Lansbury's research team were published in the Oct. 18, 2002 issue of the journal Cell.

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