tailieunhanh - Báo cáo y học: "Prion propagation in vitro: are we there yet"

Tuyển tập các báo cáo nghiên cứu khoa học ngành y học tạp chí Medical Sciences dành cho các bạn sinh viên ngành y tham khảo đề tài: Prion propagation in vitro: are we there yet? | Int. J. Med. Sci. 2008 5 347 International Journal of Medical Sciences ISSN 1449-1907 2008 5 6 347-353 Ivyspring International Publisher. All rights reserved Review Prion propagation in vitro are we there yet Chongsuk Ryou H and Charles E. Mays Sanders Brown Center on Aging and Department of Microbiology Immunology Molecular Genetics University of Kentucky College of Medicine Lexington KY . H Correspondence to Dr. Chongsuk Ryou 800 Rose St. HSRB-326 Lexington KY 40536. Phone 859 257 4016 Fax 859 257 8382 E-mail cryou2@ Received Accepted Published 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 PrPC to misfolded disease-associated scrapie prion protein PrPSc 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. Key words prion disease prion cellular prion protein disease-associated scrapie prion protein in vitro conversion in vitro prion amplification prion infectivity Introduction Prion diseases also known as transmissible spongiform encephalopathies are fatal neurodegen-erative disorders including Creutzfeldt-Jakob disease in humans scrapie in sheep chronic wasting disease in cervids and bovine spongiform encephalopathy in cattle. The only known component of the infectious prion particle is the disease-associated isoform of the prion protein designated PrPSc replication is facilitated in a