Cells, which employ a process called autophagy to clean up and reuse protein debris leftover from biological processes, were the original recyclers. A team of scientists from Paul Greengard's Rockefeller University laboratory have linked a molecule that stimulates autophagy with the reduction of one of Alzheimer's disease's major hallmarks, amyloid peptide. Their finding suggests a mechanism that could be used to eliminate built-up proteins in diseases such as Alzheimer's, Down syndrome, Huntingdon's and Parkinson's.
The molecule, called SMER28, spurs autophagy, which in turn eliminates unwanted materials such as amyloid-beta, the protein aggregates that cause Alzheimer's plaques. Increasing autophagy, either through a drug or a natural process such as diet, could improve the outcome for people with neurodegenerative diseases, the researchers report in the FASEB Journal.
"Much effort has been carried out to prevent the formation of amyloid-beta without much success," says Greengard, who is Vincent Astor Professor and head of the Laboratory of Molecular and Cellular Neuroscience. "In order to develop better-suited therapies, alternative approaches are clearly needed. One approach would be the identification of potential therapeutic targets that enhance the removal of amyloid-beta, for example, by increasing autophagy."
Most prior strategies to develop Alzheimer's disease drugs were designed to inhibit the formation of the toxic amyloid-beta. Greengard, who directs the Fisher Center for Research on Alzheimer's Disease at Rockefeller, and his colleagues propose a radically different approach: boosting a cellular mechanism to enhance their clearance. This approach, says Marc Flajolet, a research assistant professor in Greengard's lab, may also be beneficial for targeting a hallmark of advanced Alzheimer's disease, twisted fibers of tau protein that build up inside nerve cells and cause tangles.
The researchers, led by
|Contact: Joseph Bonner|