Disease relevance of acetylcholinesterase

• In summary, in chronic trichostrongylosis even relatively low nematode burdens were associated with marked pathological and biochemical damage in the intestine with both lesion severity and mucosal acetylcholinesterase activity being directly related to worm numbers [1].

Psychiatry related information on acetylcholinesterase

• Acetylcholine is the major excitatory neurotransmitter controlling motor activities in nematodes, and the enzyme which hydrolyses and inactivates acetylcholine, acetylcholinesterase, is thus essential for regulation of cholinergic transmission [2].

High impact information on acetylcholinesterase

• The single ace-1+ gene in these animals is responsible for coordinated animal movement and acetylcholinesterase activity in the regions of the nerve ring and ventral and dorsal nerve cords, as judged by histochemical assay [3].
• Release of acetylcholine from motor neurons was assayed by measuring the sensitivity of intact animals to the acetylcholinesterase inhibitor aldicarb [4].
• The acetylcholinesterase genes of C. elegans: identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype [5].
• The viable mutants are resistant to the acetylcholinesterase inhibitor aldicarb, indicating that cholinergic transmission is impaired [6].
• Furthermore, rab-3 animals were resistant to the acetylcholinesterase inhibitor aldicarb, suggesting that cholinergic transmission was generally depressed [7].

Biological context of acetylcholinesterase

• Mammalian cholinergic tissues mostly express the T splice variant of acetylcholinesterase, in which the catalytic domain is associated with a C-terminal peptide of 40 residues, called the t peptide (Massouli??, 2002) [8].
• Gene dosage experiments suggest that it may be a structural gene for a component of class A acetylcholinesterase forms [9].
• Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis [10].
• The latter proteins exist as soluble monomers released by the parasite during infection and these AChE are distinct from those enzymes which the nematodes use for synaptic transmission in their neuromuscular system [11].
• Structure and promoter activity of the 5' flanking region of ace-1, the gene encoding acetylcholinesterase of class A in Caenorhabditis elegans [12].

Anatomical context of acetylcholinesterase

• The analysis of these mosaics has led us to conclude that the synthesis of acetylcholinesterase by muscle cells is primarily responsible for the coordinated movement conferred by the ace-1+ gene [3].
• Here we show that the increased contraction rate of the pharynx in feh-1 mutant worms is associated to decreased acetylcholinesterase activity [13].
• The antibodies were further characterized by enzyme-linked immunosorbent assays specific for worm or larvae homogenates and secretions or for acetylcholinesterase from electric eel and bovine erythrocytes [14].
• Root exudates from transgenic potato plants expressing a chemoreception-disruptive peptide inhibit acetylcholinesterase by up to 63 +/- 3% [15].
• Examination of acetylcholinesterase in the rat jejunum showed decreased histochemical staining intensity in the muscle wall, and quantitative evaluation showed significantly decreased (>50%) acetylcholinesterase activity in SM/MP preparations [16].

Associations of acetylcholinesterase with chemical compounds

• Acetylcholine (ACh) is one of an array of neurotransmitters used by invertebrates and, analogous to vertebrate nervous systems, acetylcholinesterase (AChE) regulates synaptic levels of this transmitter [11].
• A tryptophan amphiphilic tetramerization domain-containing acetylcholinesterase from the bovine lungworm, Dictyocaulus viviparus [11].
• The purified preparation has a measured specific activity of 3.74 mumol/min/mg protein, and is free of acetylcholinesterase and acetyl-CoA hydrolase activities [17].
• An unusual class of acetylcholinesterase has been isolated from Meloidogyne which has very high affinity for acetylcholine, but is highly resistant to carbamate and organophosphate inhibitors [18].
• It is suggested that the increases in acetylcholinesterase activity may be due to an inhibition by the benzimidazole carbamates of the secretion of enzyme to the exterior of the worms which, in turn, leads to expulsion through failure of the so-called "chemical holdfast" [19].

Regulatory relationships of acetylcholinesterase

• A null mutation in ace-1 (allele p1000) suppresses all acetylcholinesterase activity of class A. We have identified an opal mutation TGG (W99)-->TGA (Stop) as the only alteration in the mutated gene [20].

Other interactions of acetylcholinesterase

• Derivatives homozygous only for the ace-1 mutation also lacked class A acetylcholinesterase forms, but were behaviorally and developmentally indistinguishable from wild type [9].
• Although originally isolated because of its uncoordinated behavior, this strain was subsequently shown to harbor mutations in two genes; one in the previously identified gene unc-3, accounting for its behavior, and one in a newly identified gene, ace-1, accounting for its selective acetylcholinesterase deficiency [9].
• Total extracts from three different dys-1 alleles showed significantly less acetylcholinesterase-specific activity than wild-type controls [21].
• Mutations in the dystrophin-like dys-1 gene of Caenorhabditis elegans result in reduced acetylcholinesterase activity [21].
• Although a snf-11 null mutation has no obvious effects on GABAergic behaviors, it leads to resistance to inhibitors of acetylcholinesterase [22].

Analytical, diagnostic and therapeutic context of acetylcholinesterase

• Molecular cloning of an acetylcholinesterase gene from the plant parasitic nematodes, Meloidogyne incognita and Meloidogyne javanica [23].
• Vaccination against the nematode Trichostrongylus colubriformis. II. Attempts to protect guinea-pigs with worm acetylcholinesterase [24].

References