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- W2010489018 abstract "A transgenic mouse expressing the human β-amyloid precursor protein with the “Swedish” mutation, Tg2576, was used to investigate the mechanism of amyloid-β peptide (Aβ) deposition. We characterized Aβ deposits in the cerebral cortex biochemically and pathologically. A surface-enhanced laser desorption/ionization affinity mass spectrometric study using the 6E10 monoclonal antibody demonstrated that the major species of Aβ in a formic acid-extracted fraction of the cortex were Aβ1–38, Aβ1–40 and Aβ1–42. Immunohistochemistry using antibodies to the carboxy-terminal epitopes of Aβ1–40 and Aβ1–42, as well as 6E10, showed that plaques containing Aβ1–42 were more numerous than those containing Aβ1–40 throughout the cortex. Laser confocal analysis of the immunoreactivities in the plaques demonstrated that Aβ1–40 was preferentially located in the central part of the Aβ1–42 positive plaques. Enzyme-linked immunosorbent assay measurements of Aβ1–40 and Aβ1–42 showed that Aβ1–40 was several-fold more abundant than Aβ1–42. From these data we suggest that Aβ1–42 deposition may precede Aβ1–40 deposition, while Aβ1–40 begins to deposit in the central part of the plaques and accumulates there. Furthermore, localization of Aβ1–40 corresponded almost exactly to congophilic structures, which were associated with aberrant swollen synapses detected with antibodies to synaptophysin and α-synuclein. Thus, Aβ deposits in Tg2576 mice have similar characteristics to those in Alzheimer's disease." @default.
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- W2010489018 date "2001-05-01" @default.
- W2010489018 modified "2023-09-27" @default.
- W2010489018 title "β-amyloid deposits in transgenic mice expressing human β-amyloid precursor protein have the same characteristics as those in Alzheimer's disease" @default.
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- W2010489018 doi "https://doi.org/10.1016/s0306-4522(01)00095-1" @default.
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