NR ASOJ
AU Chakraborty,C.; Nandi,S.; Jana,S.
TI Prion disease: a deadly disease for protein misfolding.
QU Current Pharmaceutical Biotechnology 2005 Apr; 6(2): 167-77
PT journal article; review; review, tutorial
AB An infectious particle, termed prion, composed largely and perhaps solely of a single protein, is the likely causative agent of prion disease. It produces lethal decline of cognitive and motor function. The responsible protein arrives at a pathogenic state by misfolding from a normal form that has ubiquitous tissue distribution. Prion diseases are often called spongiform encephalopathies. Probably most mammalian species develop these diseases. Specific examples in various animals are Scrapie, Transmissible Mink Encephalopathy (TME), Chronic Wasting Disease(CWD) and bovine spongiform encephalopathy (BSE). Humans are also susceptible to several prion diseases: Creutzfeld-Jacob Disease (CJD), Gerstmann-Sträussler-Scheinker Syndrome (GSS), Fatal Familial Insomnia (FFI), Kuru and Alpers Syndrome. This paper reviews transmission of this diseases, protein involvement, nature of protein, the conversion process from PrPc to PrPsc, conversion of prion protein in vitro, the different proposed models for the conversion of PrPc to PrPsc, prion and other amyloid diseases, prion strains, structure of PrPc the particular process that may induce prion disease, and immunization against these diseases.
ZR 111
MH Animals; Brain/*metabolism; Humans; Prion Diseases/*metabolism/*transmission; Prions/*chemistry/*metabolism; Protein Folding; Structure-Activity Relationship
AD Glenmark Lab, C-33 Nizamuddin East, New Delhi-110013, India. drchiranjib@yahoo.com
SP englisch
PO Niederlande