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. 2015 Feb 23;9:24. doi: 10.3389/fncel.2015.00024

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Copyright © 2015 Jadhav, Katina, Kovac, Kazmerova, Novak and Zilka.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Amyloid-β 40 was reduced in the synapses of transgenic animals but not amyloid-β 42. (A) Immunoblot using N- terminal antibody of APP showed no change in the levels of APP in transgenic rats (tg) with respect to wild-type (wt) rats. Actin was used as loading control. (B) Levels of amyloid precursor protein did not change. (C) Graphs show data points and means of individual groups for the Aβ42 and Aβ40 peptides. Levels of amyloid-β alloforms in total synaptosomes showed no change in Aβ42 and a significant decrease in Aβ40 (*p ∈ 〈0.01, 0.05)).