Prion Protein (PRNP)
Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases characterized by neuron loss, glial reactions, and tissue spongiosis, which course with motor and/or cognitive symptoms (Knight and Will 2004). The TSEs are associated with conformational conversion of the prion protein (PrPC, the product of the Prnp gene), wherein the predominantly α-helical secondary structure of PrPC changes into an aggregation-prone, β-sheet richer structure known as PrPSc. The latter is believed to coerce PrPC molecules into conformational conversion, thus behaving as a proteinaceous infectious particle, or prion (Prusiner 1998), which gave TSEs the epithet prion diseases.
The much needed development of effective treatment for these still incurable diseases depends on the understanding of functional properties of the prion protein (Soto and Satani 2010). Most studies of...
The authors’ research groups have been supported by the Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ), Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP), Programa Institutos Nacionais de Ciência e Tecnologia (CNPq/MCT), Ludwig Institute for Cancer Research, and PrioNet-Canada. V.R.M. is an International Scholar of the Howard Hughes Medical Institute.
- Soto C, Satani N. The intricate mechanisms of neurodegeneration in prion diseases. Trends Mol Med. 2010;17(1):14–24.Google Scholar