Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers
Zhang, JM; Lei, HZ; Chen, YB; Ma, YT; Jiang, F; Tan, JQ; Zhang, Y; Li, JD
2017
发表期刊NEUROSCIENCE LETTERS
ISSN0304-3940
卷号655期号:-页码:90-94
文章类型期刊论文
摘要Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of alpha-synuclein, which is influenced by several post-translational modifications (PTM5). O-GlcNAcylation is one PTM that has an important role in many fundamental processes. The O-GlcNAcylation of endogenous a-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis. The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic a-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively. O-GlcNAcylation at Thr72 or Ser87 suppresses the aggregation of alpha-synuclein. However, the effect of enzymatic O-GlcNAcylation of otsynuclein at multiple residues is not clear. Here, we successfully generated O-GlcNAcylated alpha-synuclein by co-expressing a shorter form of OGT (sOGT) with a-synuclein. The O-GlcNAcylation inhibited asynuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers. Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models. (C) 2017 Elsevier B.V. All rights reserved.
关键词Linked N-acetylglucosamine Parkinsons-disease Membrane Interactions Mass-spectrometry Toxicity Brain Phosphorylation Ubiquitination Proteins Form
DOI10.1016/j.neulet.2017.06.034
关键词[WOS]LINKED N-ACETYLGLUCOSAMINE ; PARKINSONS-DISEASE ; MEMBRANE INTERACTIONS ; MASS-SPECTROMETRY ; TOXICITY ; BRAIN ; PHOSPHORYLATION ; UBIQUITINATION ; PROTEINS ; FORM
收录类别SCI
语种英语
WOS记录号WOS:000407663200014
引用统计
文献类型期刊论文
条目标识符http://ir.sinap.ac.cn/handle/331007/28643
专题中科院上海应用物理研究所2011-2018年
推荐引用方式
GB/T 7714
Zhang, JM,Lei, HZ,Chen, YB,et al. Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers[J]. NEUROSCIENCE LETTERS,2017,655(-):90-94.
APA Zhang, JM.,Lei, HZ.,Chen, YB.,Ma, YT.,Jiang, F.,...&Li, JD.(2017).Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.NEUROSCIENCE LETTERS,655(-),90-94.
MLA Zhang, JM,et al."Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers".NEUROSCIENCE LETTERS 655.-(2017):90-94.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
Enzymatic O-GlcNAcyl(890KB)期刊论文作者接受稿开放获取CC BY-NC-SA浏览 下载
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Zhang, JM]的文章
[Lei, HZ]的文章
[Chen, YB]的文章
百度学术
百度学术中相似的文章
[Zhang, JM]的文章
[Lei, HZ]的文章
[Chen, YB]的文章
必应学术
必应学术中相似的文章
[Zhang, JM]的文章
[Lei, HZ]的文章
[Chen, YB]的文章
相关权益政策
暂无数据
收藏/分享
文件名: Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.pdf
格式: Adobe PDF
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。