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Blue native/SDS‐PAGE combined with iTRAQ analysis reveals advanced glycation end‐product‐induced changes of synaptosome proteins in C57 BL/6 mice
Author(s) -
Xie Chunliang,
Liu Nvying,
Long Jia,
Tang Cheng,
Li Jianglin,
Huo Linju,
Wang Xianchun,
Chen Ping,
Liang Songping
Publication year - 2011
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100125
Subject(s) - glycation , synaptosome , synapse , neurotransmission , advanced glycation end product , reactive oxygen species , microbiology and biotechnology , signal transduction , biochemistry , biology , chemistry , neuroscience , receptor , in vitro
Evidence shows that administration of high‐level D ‐galactose induces the production of advanced glycation end‐products (AGEs) that have been implicated in the development of diabetic complications such as neuropathy. The deterioration of learning and memory during neuropathy might be associated with the altered expression of proteins in synapse. To evaluate AGE‐induced protein network alterations in synapse, blue native/SDS‐PAGE and iTRAQ proteomic methods were used to screen for differentially expressed synaptic proteins of cerebral cortex in D ‐galactose‐induced C57 BL/6 mice. In total, the expression level of 84 proteins is changed during AGE accumulation. The significantly differentially expressed proteins mainly participate in neurotransmission, energy metabolism and signal transduction pathway, suggesting that energy metabolism is damaged and neurotransmission is attenuated in synapse. The results of in vivo activities of malondialdehyde and superoxide dismutase suggested that AGE accumulation in the brain leads to the generation of reactive oxygen species. Therefore, elucidating the differentially expressed proteins underlying the AGE accumulation will open a new window to the mechanism of learning and memory impairments in neuropathy.