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- W2080220120 abstract "Alzheimer's disease (AD) is a progressive disorder and the main cause of dementia in the aging population. The major characteristic of AD is extracellular plaques composed of β-amyloid (Aβ) peptides, which is a product from the much larger precursor protein APP. It is generally accepted that there are two major APP processing pathways, one resulting in Aβ formation (by the combined action of β-secretase and γ-secretase), and one precluding Aβ production (by α-secretase and γ-secretase). While much is known about the production of Aβ, many questions remain concerning how APP and Aβ are degraded. APP/Aβ peptides were immunoprecipitated from CSF using the antibody 6E10. A KingFisher magnetic particle processor was used for automatic IP and washing. The extracted APP/Aβ peptides were analyzed using MALDI-TOFMS and the identities were confirmed using nanoflow liquid chromatography and tandem mass spectrometry (nano-LC-FTICR-MS/MS). 12 truncated APP/Aβ peptides in CSF, all of which ended at amino acid 15 in the Aβ sequence were identified. Of these 12 peptides, 11 were novel peptides, 10 of which start N-terminally of the β-secretase site. Using nano-LC-FTICR-MS/MS, 5 peptides had fragments providing unique sequence information whereas the remainder 7 peptides had observed masses very close to the corresponding theoretical masses. The most intense peak starting prior to the β-secretase site was APP/Aβ(-25–15) and quantification of all of these APP/Aβ peptides suggests that they constitute a significant proportion of the today known APP/Aβ isoforms. The in vivo results presented here, suggest that the APP/Aβ isoforms represent a previously unknown non-amyloidogenic APP processing pathway that may prevent from AD. The detection of several APP/Aβ isoforms ending at amino acid Q15 in the Aβ sequence suggests that there may be a specific enzymatic activity cleaving at this site, while the demonstration of Aβ peptides spanning the β-secretase site suggest a previously unknown pathway for APP processing. Future studies will be aimed at identifying the enzymatic activity responsible for the generation of these APP fragments." @default.
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- W2080220120 date "2008-07-01" @default.
- W2080220120 modified "2023-10-02" @default.
- W2080220120 title "P1-401: Identification of novel APP/Aβ isoforms in human cerebrospinal fluid" @default.
- W2080220120 doi "https://doi.org/10.1016/j.jalz.2008.05.983" @default.
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