Taking advantage of physiological proteolytic processing of the prion protein for a therapeutic perspective in prion and Alzheimer diseases
2013; Landes Bioscience; Volume: 8; Issue: 1 Linguagem: Inglês
10.4161/pri.27438
ISSN1933-690X
Autores Tópico(s)Neurological diseases and metabolism
ResumoPrion and Alzheimer diseases are fatal neurodegenerative diseases caused by misfolding and aggregation of the cellular prion protein (PrP(C)) and the β-amyloid peptide, respectively. Soluble oligomeric species rather than large aggregates are now believed to be neurotoxic. PrP(C) undergoes three proteolytic cleavages as part of its natural life cycle, α-cleavage, β-cleavage, and ectodomain shedding. Recent evidences demonstrate that the resulting secreted PrP(C) molecules might represent natural inhibitors against soluble toxic species. In this mini-review, we summarize recent observations suggesting the potential benefit of using PrP(C)-derived molecules as therapeutic agents in prion and Alzheimer diseases.
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