Influence of the Maillard Reaction to Prion Protein Aggregation
| Autor: | Christian Dumpitak, Giannantonio Panza, Eva Birkmann |
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| Rok vydání: | 2010 |
| Předmět: |
Glycation End Products
Advanced Gene isoform Aging Prions animal diseases CHO Cells Protein aggregation Antibodies symbols.namesake Cricetulus Glycation Cricetinae Age related Animals Chemical Precipitation Prion protein Chemistry Recombinant Proteins In vitro Maillard Reaction nervous system diseases Maillard reaction Biochemistry symbols Protein folding Protein Multimerization Geriatrics and Gerontology Protein Processing Post-Translational |
| Zdroj: | Rejuvenation Research. 13:220-223 |
| ISSN: | 1557-8577 1549-1684 |
| DOI: | 10.1089/rej.2009.0954 |
| Popis: | Prion diseases are fatal neurodegenerative diseases that occur either spontaneously or genetically or are caused by infection. Spontaneously occuring prion diseases are age related. The infectious agents, called prions, are proteinaceous infectious particles, composed mainly of the host-encoded prion protein (PrP) in a misfolded, insoluble, and aggregated isoform. Advanced glycation end products (AGEs) are well known to contribute to protein misfolding, insolubility, and aggregation. Thus, we studied if AGE-modification could influence PrP aggregation. We analyzed PrP preparations immunochemically to determine if they contain AGE-modified PrP. We also studied the influence of AGE modifications on the PrP aggregation process in vitro. |
| Databáze: | OpenAIRE |
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