Profiling proteins related to amyloid deposited brain of Tg2576 mice

Publisher Website
Google Scholar
Abstract
Alzheimer's disease (AD) is an age‐related neurodegenerative disorder that is characterized by the extracellular deposition of β‐amyloid and intracellular hyperphosphorylation of tau in the cortex and hippocampus of the brain. These characterizations are caused by abnormal expression, modification and deposition of certain proteins. Post‐translational modifications of proteins including oxidation and nitration might be involved in the pathogenesis of AD. In this study, AD‐related proteins were identified in the cortex of Tg2576 mice used as a model for studying AD. Tg2576 mice express high levels of the Swedish mutated form of human β‐amyloid precursor protein (APP) and generated high levels of β‐amyloid in the brains. Using Western blotting and two‐dimensional electrophoresis, proteins with differences in expression, oxidation and nitration in the cortex of Tg2576 mice brains were compared to littermate mice brains used as a control. The proteins with different expression levels were identified using matrix‐assisted laser desorption/ionization‐time of flight and liquid chromatography‐tandem mass spectrometry analyses. As a result, 12 proteins were identified among 37 different proteins using the PDQuest program. Furthermore, two proteins, laminin receptor and α‐enolase, were more susceptible to oxidative modification in the brains of Tg2576 mice compared to those of littermates. Similarly, α‐enolase, calpain 12, and Atp5b were more modified by nitration in brains of Tg2576 mice than those of littermates. Taken together, these proteins and their modifications may play an important role in the plaque deposition of Tg2576 mice brains.