Gaining knowledge on prion pathology
In order to avoid similar outbreaks in the future it is crucial to develop novel protective and therapeutic approaches against such brain pathologies. Therapeutic modalities, however, have to be founded in the firm understanding of TSEs at the molecular level. The causative agent of all TSEs, the prion (PrP), is a protein-like infective agent, which is poorly understood. Healthy neuronal cells produce PrP molecules but their function is largely unknown. EU-funded project PRP AND NEURODEGENER focused on the molecular pathways of the disease, linking PrP infection to neurodegeneration. One of the main areas of the project was the elucidation of the physiological function of PrP in healthy cells. PrP involvement in ion transport and balance had been implied in the past, however, it has been clarified what its exact role might be. Project partner, University of Grenoble explored the possibility of PrP acting as a metallochaperone in cells. Metallochaperones comprise a special protein group dealing solely with the transport/delivery of specific metal ions to target proteins or cellular compartments. Research showed an increase in metalloprotein expression, when PrP is overexpressed. The implications could be that PrP itself is involved in the signalling cascade that precedes metallochaperone expression, however further data is required. The University of Grenoble is now seeking further development support to continue these studies and further explore the possibility of novel TSE therapeutics.
