Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity.
Science
; 274(5295): 2079-82, 1996 Dec 20.
Article
em En
| MEDLINE
| ID: mdl-8953038
ABSTRACT
The fundamental event in prion diseases seems to be a conformational change in cellular prion protein (PrPC) whereby it is converted into the pathologic isoform PrPSc. In fatal familial insomnia (FFI), the protease-resistant fragment of PrPSc after deglycosylation has a size of 19 kilodaltons, whereas that from other inherited and sporadic prion diseases is 21 kilodaltons. Extracts from the brains of FFI patients transmitted disease to transgenic mice expressing a chimeric human-mouse PrP gene about 200 days after inoculation and induced formation of the 19-kilodalton PrPSc fragment, whereas extracts from the brains of familial and sporadic Creutzfeldt-Jakob disease patients produced the 21-kilodalton PrPSc fragment in these mice. The results presented indicate that the conformation of PrPSc functions as a template in directing the formation of nascent PrPSc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformation of PrPSc.
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Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Encéfalo
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Química Encefálica
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Príons
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Doenças Priônicas
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Proteínas PrPSc
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
1996
Tipo de documento:
Article