Abstract
Amyloid beta peptide 1–40 (Aβ 1–40) is closely associated with the progressive neuronal loss and cognitive decline observed in Alzheimer's disease (AD). This study aimed to establish a proteomic strategy for the profiling of AD tissues for disease-specific changes in protein abundance. Intrahippocampal injection of Aβ 1–40 induced spatial memory and learning decline in rats. Proteomic analysis revealed the changes in protein expression in the rat hippocampus treated with Aβ 1–40. Four proteins of interest which was in abundance was significantly altered in Aβ 1–40-treated rats were identified by peptide mass fingerprint (PMF). These proteins corresponded to synapsin Ib, protein disulfide-isomerase A3 precursor, tubulin β chain and ATP synthase β subunit. Our results provide new insights into the relationship between Aβ and the pathogenesis of AD, and suggest potential targets for the therapy of AD.
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