Evidence map›Paper›PMID 8280063›Full record

ArticleThe Biochemical journal1993

N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis.

B Velan, C Kronman, A Ordentlich, Y Flashner, M Leitner, S Cohen, A Shafferman

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  5. Construction of Recombinant Cell Lines for GPCR Expression.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  6. Article
  7. Erythrocyte acetylcholinesterase as biomarker of pesticide exposure: new and forgotten insights.Environmental science and pollution research international · 2018
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

B VelanDepartment of Biochemistry, Israel Institute for Biological Research, Ness-Ziona.
C Kronman
A Ordentlich
Y Flashner
M Leitner
S Cohen
A Shafferman
Israel Institute for Biological Research · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of N-glycosylation in the function of human acetylcholinesterase (HuAChE) was examined by site-directed mutagenesis (Asn to Gln substitution) of the three potential N-glycosylation sites Asn-265, Asn-350 and Asn-464. Analysis of HuAChE mutants, defective in a single or multiple N-glycosylation sites, by expression in transiently or stably transfected human embryonal 293 kidney cells suggests the following. (a) All three AChE glycosylation signals are utilized, but not all the secreted molecules are fully glycosylated. (b) Glycosylation at all sites is important for effective biosynthesis and secretion; extracellular AChE levels in mutants defective in one, two or all three sites amounted to 20-30%, 2-4% and about 0.5% of wild-type level respectively. (c) Some glycosylation mutants display impaired stability, as reflected by increased susceptibility to heat inactivation; substitution of Asn-464 has the most pronounced effect on thermostability. (d) Abrogation of N-glycosylation has no detectable effect on the enzyme activity of HuAChE; all glycosylation mutants, including the triple mutant, hydrolyse acetylthiocholine efficiently, displaying Km, kcat. and kcat./Km values similar to those of the wild-type enzyme. (e) In most mutants, inhibition profiles with edrophonium and bisquaternary ammonium ligands are identical with those of wild-type enzyme; the Asn-350 mutants, however, exhibit a slight decrease in their affinity towards these ligands. (f) Elimination of oligosaccharide side chains has no detectable effect on the surface-related 'peripheral-site' functions; like the wild-type enzyme, all mutants were inhibited by propidium and by increased concentrations of acetylthiocholine.

Indexed as

AcetylcholinesteraseAmino Acid SequenceCatalysisCells, CulturedCholinesterase InhibitorsEdrophoniumEnzyme StabilityGlycosylationHumansMolecular Sequence DataMutationOligosaccharidesQuaternary Ammonium CompoundsRecombinant ProteinsTransfectionAcetylcholinesteraseCholinesterase InhibitorsEdrophoniumOligosaccharidesQuaternary Ammonium CompoundsRecombinant Proteins

Identifiers

PMID8280063
PMCPMC1137746
OpenAlexW2337781405

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.