Influence of the maillard reaction to prion protein aggregation.
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.
Panza
Giannantonio
G
Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Dumpitak
Christian
C
Birkmann
Eva
E
D000818:Animals; D000906:Antibodies / Q000494:pharmacology; D016466:CHO Cells; D011232:Chemical Precipitation; D006224:Cricetinae; D003412:Cricetulus; D017127:Glycation End Products, Advanced / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D015416:Maillard Reaction; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization / Q000502:physiology; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D000906:Antibodies; D017127:Glycation End Products, Advanced; D011328:Prions; D011994:Recombinant Proteins