The study, appearing in the October 3 issue of the Journal of Biological Chemistry, highlights research conducted on the gene rhodopsin, a protein located in the back of the eye that is credited with helping sight in dim or low-light conditions. It is one of several proteins in the retina that controls how light is detected. The mutation linked to RP can be traced to the photoreceptor, rhodopsin. A single mutation, state the researchers, can cause a cascade of retinal events that leads to retinitis pigmentosa and eventual blindness.
"We wanted to concentrate on the reasons why rhodopsin is prone to misfold; that way we have the best chance of correcting that distortion before the disease can worsen," said lead author, John Hwa, MD, PhD, an assistant professor of pharmacology and toxicology at Dartmouth Medical School.
Retinitis pigmentosa is a degenerative disease that affects the photoreceptors in the retina. It begins with a single mutation within the rhodopsin protein that triggers a domino effect and, over a period of years, the mutation is responsible for aggregation of the protein, death of the individual retinal cells, destruction of the retina and eventually blindness.
"Basically, if we can stabilize the second domino after the first has fallen, we will be on our way for a cure to this disease that makes 1 million people go blind around the world," said Hwa. "We needed to understand the problem at the level of the protein then we can design a ligand or drug to stabilize the abnormal protein to make sure it is destroyed p
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Dartmouth Medical School