Fibrillization of recombinant bovine prion protein (rec-PrP) in vitro

• Published in: Doklady. Biochemistry and biophysics Vol. 420; no. 1; pp. 112 - 114
• Main Authors: Grigoriev, V. B., Kalnov, S. L., Pokidyshev, A. N., Tsibezov, V. V., Balandina, M. V., Gibadulin, R. A., Verkhovsky, O. A., Klimenko, S. M.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 01.06.2008; Springer Nature B.V
• Subjects: Amyloid - chemistry; Amyloid - metabolism; Animals; Biochemistry; Biological and Medical Physics; Biomedical and Life Sciences; Biophysics; Bovine spongiform encephalopathy; Cattle; Disease; Electrophoresis, Polyacrylamide Gel; Humans; Hydrogen-Ion Concentration; Life Sciences; Molecular Biology; Prions; Prions - chemistry; Prions - metabolism; Protein Structure, Secondary; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Studies; Time Factors; DOKLADY Biochemistry; Prion Disease; Bovine Spongiform Encephalopathy; Scrapie; Transmissible Spongiform Encephalopathy
• ISSN: 1607-6729; 1608-3091
• DOI: 10.1134/S1607672908030046

Conversion of normal prion protein (PrPc) from the conformation with predominantly -helical structure into the conformation rich in-structures (PrPsc, -PrP, and PrPres) underlies the pathogenesis of prion diseases, a special class of degenerative diseases of the nervous system of humans and animals. Prion diseases, or transmissible spongiform encephalopathies (TSEs) of humans, include the Creutzfeldt-Jakob disease (CJD), the GerstmannStrusslerScheinker syndrome, new variant of CJD, kuru, as well as the fatal familial insomnia. The most well-known transmissible spongiform encephalopathies of animals are scrapie of sheep, chronic wasting disease of deer and moose, and bovine spongiform encephalopathy (mad cow disease). In the course of development of transmissible spongiform encephalopathies, amyloid brils (the so-called scrapie-associated brils) are formed in brain tissue of both animals and humans.