Enzymatic O-GlcNAcylation of alpha-synuclein reduces aggregation and increases SDS-resistant soluble oligomers
文献类型：期刊论文
| 作者 | Zhang, JM; Lei, HZ; Chen, YB; Ma, YT; Jiang, F; Tan, JQ; Zhang, Y; Li, JD |
| 刊名 | NEUROSCIENCE LETTERS
 |
| 出版日期 | 2017 |
| 卷号 | 655期号:-页码:90-94 |
| ISSN号 | 0304-3940 |
| 关键词 | Linked N-acetylglucosamine Parkinsons-disease Membrane Interactions Mass-spectrometry Toxicity Brain Phosphorylation Ubiquitination Proteins Form |
| DOI | 10.1016/j.neulet.2017.06.034 |
| 文献子类 | 期刊论文 |
| 英文摘要 | 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. |
| WOS关键词 | LINKED N-ACETYLGLUCOSAMINE ; PARKINSONS-DISEASE ; MEMBRANE INTERACTIONS ; MASS-SPECTROMETRY ; TOXICITY ; BRAIN ; PHOSPHORYLATION ; UBIQUITINATION ; PROTEINS ; FORM |
| 语种 | 英语 |
| WOS记录号 | WOS:000407663200014 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/28643]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017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. |
入库方式： OAI收割
来源：上海应用物理研究所
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