New research has proven the existence of an important interaction between the molecules involved in the two types of pathologies.
Parkinson’s disease and prion diseases are very different from each other in regards to both origins and course. A group of researchers has discovered an unexpected and important link between the two pathologies.
According to the study recently published Scientific Reports, the link is a result the complex interaction between two different proteins present in our nerve cells: α-synuclein, in its aggregated form, and the prion protein PrPC, the molecule which is responsible for Creuzfeldt Jacob disease.
The presence of α-synuclein deposits in brain cells is typical of diseases technically called synucleinopathies, including Parkinson’s disease, dementia with Lewy bodies and multiple system atrophy. However, the modalities according to which these aggregates form and spread were unknown. The study reports α-synuclein actually makes use of the action of the prion protein to spread and deposit in the brain. This seems to favour the formation of these deposits and their spreading among brain cells.
But that’s not all. While the activity of the prion protein seems to support the development of synucleopathies, α-synuclein deposits seem to slacken the course of prion diseases. The research has proven that α-synuclein fibrils block the deposit of prions in nerve cells, thus preventing their replication. This surprising effect is corroborated by further evidence already found in the pathology: the course of the disease progression is slower in patients affected by prion diseases presenting α-synuclein deposits in nerve cells.
Paper: “α-Synuclein Amyloids Hijack Prion Protein to Gain Cell Entry, Facilitate Cell-to-Cell Spreading and Block Prion Replication”
Reprinted from materials provided by SISSA.