Linking brain pathology to ion imbalances
Another key characteristic of all TSEs is the causative agent of the disease, a protein-like molecule termed Prion (PrP). Accumulation of PrP leads to neuronal cell death and disease onset. However, the molecular mechanism behind PrP-induced pathology is still largely unknown and is further complicated given that PrP is also naturally produced by nerve cells but its function is unknown. The EU-funded PRP AND NEURODEGENER project set out to shed light on the links between pathology and ion metabolism in cells infected with the pathogenic form of PrP. PrP has been implicated in ion imbalances in affected neurones in spite of limited information on the topic. Project partners set out to examine the role of PrP and the differences between the pathogenic and natural forms of PrP. Studies indicated that in its natural state, PrP binds to copper ions as part of fulfilling its physiological role. Following infection, structurally-faulty PrP molecules appear to lose their ability to bind copper, and thus failing to carry out their cellular tasks. Linking copper binding to prion infection is an important finding of this research, given that the coppers have already been implicated in neuropathology and neurodegenerative disorders. Providing further support to this line of research is likely to yield important insights in the pathology of TSEs, bringing the discovery of an innovative therapy even closer.
