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Prion propagation in vitro: Are we there yet?
- Authors
- Ryou, C.; Mays, C.E.
- Issue Date
- Nov-2008
- Publisher
- Ivyspring International Publisher
- Keywords
- Cellular prion protein; Disease-associated scrapie prion protein; In vitro conversion; In vitro prion amplification; Prion; Prion disease; Prion infectivity
- Citation
- International Journal of Medical Sciences, v.5, no.6, pp 347 - 353
- Pages
- 7
- Indexed
- SCOPUS
- Journal Title
- International Journal of Medical Sciences
- Volume
- 5
- Number
- 6
- Start Page
- 347
- End Page
- 353
- ISSN
- 1449-1907
- Abstract
- Prion diseases are caused by proteinaceous pathogens termed prions. Although the details of the mechanism of prion propagation are not fully understood, conformational conversion of cellular prion protein (PrP C) to misfolded, disease-associated scrapie prion protein (PrP Sc) is considered the essential biochemical event for prion replication. Currently, studying prion replication in vitro is difficult due to the lack of a system which fully recapitulates the in vivo phenomenon. Over the last 15 years, a number of in vitro systems supporting PrPC conversion, PrPSc amplification, or amyloid fibril formation have been established. In this review, we describe the evolving methodology of in vitro prion propagation assays and discuss their ability in reflecting prion propagation in vivo. © Ivyspring International Publisher. All rights reserved.
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Related Researcher
- Ryou, Chong suk
- COLLEGE OF PHARMACY (DEPARTMENT OF PHARMACY)