File:Prion Protein and Mouse Nerve Cells (48440889002).jpg

Prion protein, shown in red, can become infectious and cause neurodegenerative disease. Here four nerve cells in a mouse illustrate how infectious prion protein moves within cells along neurites – wire-like connections the nerve cells use for communicating with adjacent cells. Scientists using an experimental treatment have slowed the progression of scrapie, a degenerative central nervous disease caused by prions, in laboratory mice and greatly extended the rodents’ lives, according to a new report in JCI Insight. The scientists used antisense oligonucleotides (ASOs), synthetic compounds that inhibit the formation of specific proteins.

Prion diseases occur when normally harmless prion protein molecules become abnormal and gather in clusters and filaments in the body, including the brain. The diseases are thought to be always fatal. Scrapie, which affects sheep and goats and can be adapted to rodents, is closely related to human prion diseases such as Creutzfeldt-Jakob disease, which is currently untreatable. Thus, scrapie is a valuable experimental model for the development of human prion disease therapies.

Read more: <a href="https://www.nih.gov/news-events/news-releases/experimental-treatment-slows-prion-disease-extends-life-mice" rel="noreferrer nofollow">www.nih.gov/news-events/news-releases/experimental-treatm...</a>