Thaindian News

London, March 21 (ANI): It is believed that when vital proteins are misfolded in your body, neurodegenerative disorders such as Alzheimer’s, Parkinson, and Creutzfeld-Jakob disease occur.

While there are currently no cures for these conditions, biologists at Brown University researchers have reported that cells can fix the problems themselves with only a little bit of help.

The insight suggested that there are more opportunities to develop a therapy for protein misfolding than scientists had thought.

“There are multiple steps that you could target,” said lead author Susanne DiSalvo.

Until now most scientists guessed that the only way to stop the runaway misfolding was right at the beginning and assumed the mutants must be blocking that first step to keep the protein in a harmless form.

“That’s one of the biggest outcomes of Susanne’s work: that if you just even slightly interfere with this process, the cell can deal with it and get rid of it,” said Tricia Serio, associate professor of medical science, who led the research team.

“The dogma in the field is that these conformations were so abnormal the cell couldn’t resolve them. But what we’ve found is that this process of misfolding is so efficient the cells can’t keep up with it. If you make it even just a little bit less efficient the cell can get rid of the pathological state.”

One mutant prion, Q24R, hinders the ability of misfolded proteins to aggregate into harmful clumps. It’s like a dryer sheet that cuts down on static cling and makes it easier to fold laundry. Another helpful mutant prion known as G58D, assists the cell by speeding up its ability to unfold and refold misfolded proteins. That’s more like a friend who helps untangle strings of holiday lights when they come out of storage.

DiSalvo’s experiments showed how the mutants and cells work together. Cells would only be cured when she both added a mutant and allowed the cells’ own quality assurance system to work. Adding the mutant G58D, for example, could cure a cell of infection by the Sup35 prion, but if she perturbed the cell’s quality assurance system then G58D would not work.

The study has been published in Nature Structural and Molecular Biology. (ANI)