Journal Article

PreJuSER-9743

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Influence of the Maillard Reaction to Prion Protein Aggregation

Panza, G. ; Dumpitak, C. ; Birkmann, E.FZJ*

2010
Liebert Larchmont, NY

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Please use a persistent id in citations: doi:10.1089/rej.2009.0954

Abstract: Prion diseases are fatal neurodegenerative diseases that occur either spontaneously or genetically or are caused by infection. Spontaneously occurring 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.

Keyword(s): Animals (MeSH) ; Antibodies: pharmacology (MeSH) ; CHO Cells (MeSH) ; Chemical Precipitation (MeSH) ; Cricetinae (MeSH) ; Cricetulus (MeSH) ; Glycosylation End Products, Advanced: chemistry (MeSH) ; Glycosylation End Products, Advanced: immunology (MeSH) ; Glycosylation End Products, Advanced: metabolism (MeSH) ; Maillard Reaction (MeSH) ; Prions: chemistry (MeSH) ; Prions: metabolism (MeSH) ; Protein Multimerization: physiology (MeSH) ; Protein Processing, Post-Translational (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: metabolism (MeSH) ; Antibodies ; Glycosylation End Products, Advanced ; Prions ; Recombinant Proteins ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Strukturbiochemie (ISB-3)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2010

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