Prion disease, also known as transmissible spongiform encephalopathy (TES), is a fatal neurodegenerative disease caused by prion protein. The most important pathogenesis is related to changes in the conformation of cellular prion proteins (PrPC). The histopathological features of prion disease are spongiform degeneration, neuronal deficiency, glial activation and the deposition of amyloid-like PrPSc. Cellular prion protein, ubiquitously expressed in the brain and other tissues, is transformed into the PrP (PrPSc) isoform in the prion disease. In this chapter, we summarize the research progresses of prion disease, the structural organization and normal function of PrPC in the central nervous system. Moreover, the formation and transmissibility of prion aggregations (PrPSc) were also included. But we mainly focused on the function of PrPSc in autophagy. Several autophagic-related markers, such as p62 and LC3, are significantly upregulated in models of prion disease. Recent advances in the autophagic invention in prion disease and several pharmaceutical targets of autophagy were reviewed in this chapter. It is necessary to understand how the prion protein spread, transport and recycle, and what is the relationship between the clearance and autophagy.
Keywords: Autophagy; Cellular prion protein; PrPSc; Prion disease.