Amyloid β-peptide (1-40) (rat) is the prone-to-aggregation product of amyloid precursor protein proteolytic cleavage, and is the major constituent of senile plaques observed in the brain of Alzheimer's disease. The Amyloid β-peptide (1-40) (rat)-treated rats require longer to find the platform hidden under the water. In the visible platform test, the latency for each group is similar (20.56±11.31 s in control and 14.68±9.97 s in Amyloid β-peptide (1-40) (rat) group, p=0.304). Among these tested proteins, 6 ones are significantly up-regulated and 7 ones significantly down-regulated in Amyloid β-peptide (1-40) (rat) group comparing with the control. Tubulin β chain is significantly down-regulated in Amyloid β-peptide (1-40) (rat) group (p=0.014) when compare with control. Similar changes are also observed for ATP synthase β subunit (p=0.010) and synapsin Ib between Amyloid β-peptide (1-40) (rat) and control groups, but not significantly for synapsin Ib (p=0.295)[1].
[1]. Shi X, et al. Rat hippocampal proteomic alterations following intrahippocampal injection of amyloid betapeptide (1-40). Neurosci Lett. 2011 Aug 15;500(2):87-91.