Prion protein and prion disease at a glance

Prion diseases are neurodegenerative disorders caused by conformational conversion of the cellular prion protein (PrPC) into scrapie prion protein (PrPSc). As the main component of prion, PrPSc acts as an infectious template that recruits and converts normal cellular PrPC into its pathogenic, misfolded isoform. Intriguingly, the phenomenon of prionoid, or prion-like, spread has also been observed in many other disease-associated proteins, such as amyloid beta (A beta), tau and a-synuclein. This Cell Science at a Glance and the accompanying poster highlight recently described physiological roles of prion protein and the advanced understanding of pathogenesis of prion disease they have afforded. Importantly, prion protein may also be involved in the pathogenesis of other neurodegenerative disorders such as Alzheimer's and Parkinson's disease. Therapeutic studies of prion disease have also exploited novel strategies to combat these devastating diseases. Future studies on prion protein and prion disease will deepen our understanding of the pathogenesis of a broad spectrum of neurodegenerative conditions.

Automated summary

Prion diseases are neurodegenerative disorders caused by the abnormal conformational conversion of cellular prion protein. The phenomenon of prion-like spread has also been observed in other disease-associated proteins, such as Aβ, tau, and α-synuclein. Prion protein may play a role in the pathogenesis of a broad spectrum of neurodegenerative conditions, including Alzheimer's and Parkinson's disease.