December 18, 2012
New Research Advances Understanding Of Parkinson’s Disease
[ Watch the Video: Rice University Opens New Window on Parkinson´s Disease ]
Lee Rannals for redOrbit.com - Your Universe OnlineScientists at Rice University have found a new way to look inside living cells to see the insoluble fibrillar deposits associated with Parkinson's disease.
Two laboratories at the university helped lead to the spectroscopic technique that could be a valuable tool for fighting the disease.
By testing live neuroglioma cells in the lab, the team found the probe binds with the misfiled alpha-synuclein proteins that clump together and form fibrils and disrupt the cell's function.
Researchers trying to understand molecular mechanisms of protein misfiling have had limited alternatives to monitor protein aggregation in cells. A probe that is capable of monitoring the formation of aggregates should be of great value in the search for drugs that break up fibrils or prevent them from forming.
A couple of years ago, researchers from the team revealed their metallic compounds that switch on like a light bulb when they attach to misfiled proteins. This study involved the beta amyloids that form plaques in the brains of Alzheimer's patients.
“There are a few compounds you can use to detect the presence of these types of protein aggregates, but none of them have been reported to work in cells,” wrote Laura Segatori, an author of the paper in the journal. “When you´re thinking about developing a therapeutic strategy, you want to be able to detect the presence of fibril aggregates in living cells, or even in animals. It´s been very nice to collaborate with someone with the expertise to do this.”
Angel MartÃ, another researcher on the project, said the connection between Parkinson's and Alzheimer's is natural.
Segatori said that although ruthenium complex has no therapeutic benefit for Parkinson's sufferers, it is a step towards understanding the chemistry.
The team said they see the possibility that metallic complexes can be tailored to tag aggregates implicated in other degenerative diseases.
“Metal complexes are like Legos, in the sense that you can attach whatever you want to them,” Cook said.
The researchers created an in vitro cell model of Parkinson's disease and found their ruthenium complexes are clearly labeled fibrillar alpha-synuclein proteins in cells.
“We can use it to test our strategies to prevent misfolding of proteins or to increase their degradation, so they will be eliminated,” Segatori concluded. “It will be an easy tool to use for a lot of experiments.”