Quantitative proteomics reveals distinct composition of amyloid plaques in Alzheimer's disease

被引：76
作者：
Xiong, Feng [1 ,2 ]
Ge, Wei [1 ,2 ]
Ma, Chao [3 ]
机构：
[1] Chinese Acad Med Sci, Peking Union Med Coll, State Key Lab Med Mol Biol, Inst Basic Med Sci, Beijing, Peoples R China
[2] Chinese Acad Med Sci, Peking Union Med Coll, Dept Immunol, Inst Basic Med Sci, Beijing, Peoples R China
[3] Chinese Acad Med Sci, Peking Union Med Coll, Dept Human Anat Histol & Embryol, Neurosci Ctr,Inst Basic Med Sci, Beijing, Peoples R China
来源：
ALZHEIMERS & DEMENTIA | 2019年 / 15卷 / 03期
基金：
中国国家自然科学基金;
关键词：
Alzheimer's disease; Proteomics; Amyloid plaque; Laser dissection; COGNITIVE IMPAIRMENT; PRECURSOR PROTEIN; BETA; LESSONS; NEURODEGENERATION; QUANTIFICATION; NEUROLIGIN-1; ASSOCIATION; HYPOTHESIS; DEPOSITION;
D O I：
10.1016/j.jalz.2018.10.006
中图分类号：
R74 [神经病学与精神病学];
学科分类号：
摘要：
Introduction: We investigated the proteomic profiles of amyloid plaques (APs) from Alzheimer's disease (AD) and age-matched non-AD brains and APP/PS1 transgenic model mice. Methods: APs and adjacent control regions were collected from fresh-frozen brain sections using laser capture dissection. Proteins were quantitated using tag-labeling coupled high-throughput mass spectra. Results: Over 4000 proteins were accurately quantified, and more than 40 were identified as highly enriched in both AD and non-AD APs, including apoE, midkine, VGFR1, and complement C4. Intriguingly, proteins including synaptic structural proteins and complement C1r, C5, and C9 were found to be upregulated in AD APs but not non-AD APs. Moreover, the proteomic pattern of AD APs was distinct from APP/PS1 APs and exhibited correlation with aging hippocampus. Discussion: Our results provide new insight into AP composition. We demonstrate unexpected differences between AD, non-AD, and APP/PS1 mouse APs, which may relate to different pathological processes. (C) 2018 Published by Elsevier Inc. on behalf of the Alzheimer's Association.
引用
收藏
页码：429 / 440
页数：12
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