NDLI: Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition

Content Provider	Springer Nature Link
Author	Xu, Miranda L. Luk, Wilson K. W. Lau, Kei M. Bi, Cathy W. C. Cheng, Anthony W. M. Gong, Amy G. W. Lin, Huangquan Tsim, Karl W. K.
Copyright Year	2015
Abstract	Acetylcholinesterase (AChE; EC 3.1.1.7) is a glycoprotein possessing three conserved N-linked glycosylation sites in mammalian species, locating at 296, 381, and 495 residues of the human sequence. Several lines of evidence demonstrated that N-glycosylation of AChE affected the enzymatic activity, as well as its biosynthesis. In order to determine the role of three N-glycosylation sites in AChE activity and glycan composition, the site-directed mutagenesis of N-glycosylation sites in wild-type human AChE$_{T}$ sequence was employed to generate the single-site mutants (i.e., AChE$_{T}$ $^{N296Q}$, AChE$_{T}$ $^{N381Q}$, and AChE$_{T}$ $^{N495Q}$) and all site mutant (i.e., AChE$_{T}$ $^{3N→3Q}$). The mutation did not affect AChE protein expression in the transfected cells. The mutants, AChE$_{T}$ $^{3N→3Q}$ and AChE$_{T}$ $^{N381Q}$, showed very minimal enzymatic activity, while the other mutants showed reduced activity. By binding to lectins, Con A, and SNA, the glycosylation profile was revealed in those mutated AChE. The binding affinity with lectins showed no significant difference between various N-glycosylation mutants, which suggested that similar glycan composition should be resulted from different N-glycosylation sites. Although the three glycosylation sites within AChE sequence have different extent in affecting the enzymatic activity, their glycan compositions are very similar.
Starting Page	486
Ending Page	491
Page Count	6
File Format	PDF
ISSN	08958696
Journal	Journal of Molecular Neuroscience
Volume Number	57
Issue Number	4
e-ISSN	15591166
Language	English
Publisher	Springer US
Publisher Date	2015-08-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	AChE PRiMA N-glycosylation sites Lectin Molecular form Neurosciences Neurochemistry Cell Biology Proteomics Neurology
Content Type	Text
Resource Type	Article
Subject	Medicine Cellular and Molecular Neuroscience

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