Aggregation and amyloid fibril formation of the prion protein is accelerated in the presence of glycogen
| Autor: | Tatsuo Terashima, Detlev Riesner, Eva Birkmann, Giannantonio Panza, Otto Baba, Dieter Willbold, Christian Dumpitak, Jan Stöhr |
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| Rok vydání: | 2008 |
| Předmět: |
Aging
Amyloid Prions animal diseases Scrapie Protein aggregation Biology Polysaccharide law.invention chemistry.chemical_compound Protein structure law Cricetinae Animals Protein Structure Quaternary chemistry.chemical_classification Glycogen Mesocricetus Circular Dichroism In vitro Recombinant Proteins nervous system diseases chemistry Biochemistry Recombinant DNA Geriatrics and Gerontology |
| Zdroj: | Rejuvenation research. 11(2) |
| ISSN: | 1549-1684 |
| Popis: | Prion diseases like Creutzfeldt-Jakob disease in humans or scrapie in sheep and goats are infectious neurodegenerative diseases. Their infectious agent, called prion, is composed mainly of aggregated and misfolded prion protein and non-proteinaceous components. An example of such a common non-proteinaceous secondary component of natural prions is the polysaccharide scaffold. We studied the influence of such a polysaccharide on the conformational transition of PrP applying an in vitro conversion system. Here we report that glycogen supports and accelerates PrP amorphous aggregation similar to seeded aggregation and leads to co-aggregates. Furthermore, PrP fibril formation was highly accelerated in the presence of glycogen. |
| Databáze: | OpenAIRE |
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