Researchers discover potential new way to slow neurodegenerative disease

The likely targets are oxidized proteins, and researchers at OSU's College of Science are looking for the best way to attack them

The findings were published in the journal Redox Biology

Neurodegenerative diseases occur when nerve cells lose function over time and eventually die

According to the Parkinson's Foundation, the Alzheimer's Disease Association estimates that more than 6 million Americans have the disease and another 1 million have Parkinson's

The National Institutes of Health said that everyone's risk of developing neurological disorders increases with age, meaning that as people live longer, more and more cases are likely to appear in the coming decades

Franco, assistant professor of biochemistry and biophysics, explained that in inflammatory diseases, including neurogenesis disorders, diseased cells produce peroxynitrite -- the strongest oxidant a cell can produce

An oxidant, also known as an oxidant or oxidant, is any substance that is capable of oxidizing other substances—for example, by taking electrons from those substances in a chemical reaction

Franco and collaborators at Oregon, University of Central Florida and Rollins University found that when peroxynitrate is oxidized in half—the short heat shock protein 90 inside triggers a signal that activates cells, causing them to die in a "suicide" that The process is called apoptosis, Franco said

"We discovered earlier that the oxidation of specific molecules by peroxynitrite leads to the death of motor neurons, the cells that transmit signals from the brain to the muscles to coordinate muscle movement," said Maria A.

The normal function of heat shock protein 90 is to support healthy cellular processes, but oxidation can have profound effects on the three-dimensional structure of proteins, such as heat shock protein 90, changing their function, Franco said

"By understanding how oxidation alters the structure of Hsp90, and how oxidized proteins work in cells, we can search for drugs that bind to Hsp90-modified structures and stop its toxicity without affecting normal Hsp90 activity in healthy tissue," she said.

Oregon State University undergraduate Asra Noor helped Franco lead the study along with University of Central Florida researchers Megan Jandy and Pascal Nelson

The National Institutes of Health supported this research

Journal Reference :

1. Megan Jandy, Asra Noor, Pascal Nelson, Cassandra N.