ArticleJournal of molecular neuroscience : MN2015
Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition.
Article in Journal of molecular neuroscience : MN, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Model acetylcholinesterase-Fc fusion glycoprotein biotechnology system for the manufacture of an organophosphorus toxicant bioscavenging countermeasure.Bioengineering & translational medicine · 2024Article
- Presenilin 1 Modulates Acetylcholinesterase Trafficking and Maturation.International journal of molecular sciences · 2023Article
- Proceedings of workshop: "Neuroglycoproteins in health and disease", INNOGLY cost action.Glycoconjugate journal · 2022Article
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Wnt3a induces the expression of acetylcholinesterase during osteoblast differentiation via the Runx2 transcription factor.The Journal of biological chemistry · 2017Article
- Glycoengineering of Esterase Activity through Metabolic Flux-Based Modulation of Sialic Acid.Chembiochem : a European journal of chemical biology · 2017Article
- LW-AFC Effects onAging and disease · 2017Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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), AChET (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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.