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• W1992380863 endingPage "4770" @default.
• W1992380863 startingPage "4766" @default.
• W1992380863 abstract "Alzheimer disease (AD) is characterized by deposits of an aggregated 42-amino-acid beta-amyloid peptide (beta AP) in the brain and cerebrovasculature. After a concentration-dependent lag period during in vitro incubations, soluble preparations of synthetic beta AP slowly form fibrillar aggregates that resemble natural amyloid and are measurable by sedimentation and thioflavin T-based fluorescence. Aggregation of soluble beta AP in these in vitro assays is enhanced by addition of small amounts of pre-aggregated beta-amyloid seed material. We also have prepared these seeds by using a naturally occurring reaction between glucose and protein amino groups resulting in the formation of advanced glycosylation end products (AGEs) which chemically crosslink proteins. AGE-modified beta AP-nucleation seeds further accelerated aggregation of soluble beta AP compared to non-modified seed material. Over time, nonenzymatic advanced glycation also results in the gradual accumulation of a set of posttranslational covalent adducts on long-lived proteins in vivo. In a standardized competitive ELISA, plaque fractions of AD brains were found to contain about 3-fold more AGE adducts per mg of protein than preparations from healthy, age-matched controls. These results suggest that the in vivo half-life of beta-amyloid is prolonged in AD, resulting in greater accumulation of AGE modifications which in turn may act to promote accumulation of additional amyloid." @default.
• W1992380863 created "2016-06-24" @default.
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• W1992380863 date "1994-05-24" @default.
• W1992380863 modified "2023-10-16" @default.
• W1992380863 title "Advanced glycation end products contribute to amyloidosis in Alzheimer disease." @default.
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• W1992380863 doi "https://doi.org/10.1073/pnas.91.11.4766" @default.
• W1992380863 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/43869" @default.
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