Current Pharmaceutical Biotechnology

Zeno Foldes-Papp
Visiting Professor of Medical Biochemistry
HELIOS Clinical Center of Emergency Medicine
Department for Internal Medicine
Alte-Koelner-Strasse 9
D-51688 Koeln-Wipperfuerth
Germany

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Prion Disease: A Deadly Disease for Protein Misfolding

Author(s): Chiranjib Chakraborty, Shyam Nandi, Snehasis Jana.

Abstract:

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-Straussler-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.

Keywords: spongiform encephalopathies, gertsmann-sträussler-scheinker (gss), dementia, creutzfeldt-jakob disease (cjd), infectious, irradiation, prp protein, transgenic mouse, polymerization, amyloid diseases

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Article Details

VOLUME: 6
ISSUE: 2
Year: 2005
Page: [167 - 177]
Pages: 11
DOI: 10.2174/1389201053642321
Price: $58