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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
Source PublicationNEUROSCIENCE LETTERS
ISSN0304-3940
Volume655Issue:-Pages:90-94
Subtype期刊论文
AbstractNeurodegenerative 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.
KeywordLinked N-acetylglucosamine Parkinsons-disease Membrane Interactions Mass-spectrometry Toxicity Brain Phosphorylation Ubiquitination Proteins Form
DOI10.1016/j.neulet.2017.06.034
Indexed BySCI
WOS KeywordLINKED N-ACETYLGLUCOSAMINE ; PARKINSONS-DISEASE ; MEMBRANE INTERACTIONS ; MASS-SPECTROMETRY ; TOXICITY ; BRAIN ; PHOSPHORYLATION ; UBIQUITINATION ; PROTEINS ; FORM
Language英语
WOS IDWOS:000407663200014
Citation statistics
Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/28643
Collection中科院上海应用物理研究所2011-2019年
Recommended Citation
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.
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