Yeast Protein Reverses Plaque Formation in Parkinson's Disease Model

A team of researchers studying Parkinson's disease has found that a protein produced by yeast is able to partially dissolve the alpha-synuclein plaques that are a toxic characteristic of the syndrome.

Investigators at the University of Pennsylvania School of Medicine (Philadelphia, USA) worked with the yeast protein Hsp104, which was known to reverse protein aggregation. Hsp104 does not have an analogue in mammals. The investigators reported in the August 14, 2008, online edition of the Journal of Clinical Investigation (JCI) that Hsp104 in vitro could partially dissolve alpha-synuclein aggregates. In experiments conducted in a rat model of Parkinson's disease, Hsp104 reduced formation of phosphorylated alpha-synuclein inclusions and prevented nigrostriatal dopaminergic neurodegeneration induced by alpha-synuclein.

"Yeast expresses a protein called Hsp104, which is able to reverse protein aggregation,” explained contributing author Dr. James Shorter, assistant professor of biochemistry and biophysics at the University of Pennsylvania School of Medicine. "However, for reasons that are unclear, Hsp104 is not found in mammals. We wondered if introducing Hsp104 into mammals could help with diseases connected with protein aggregation. This study represents an important preliminary step. One thing we would like to do next is to treat an animal model which already has considerable quantities of alpha-synuclein aggregates to see if Hsp104 can actually reverse the process in the rat brain.”

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