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Gene Review

ache  -  acetylcholinesterase

Danio rerio

Synonyms: AChE, Acetylcholinesterase, SO:0000704
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Disease relevance of ache


High impact information on ache


Chemical compound and disease context of ache


Biological context of ache

  • Remarkably, the ratio of AAA/AChE activity decreased 210-fold from 4 to 144 h development, indicating a distinct embryonic role of AAA during early embryogenesis [8].
  • Blocking acetylcholinesterase (AChE) with eserine had no effect on mEPC kinetics in embryos at 1 day and only partially slowed (by approximately 1/2) the decay rate in larvae at 6 days [9].
  • The primary neurons appear to follow a common sequence of development consisting of a withdrawal from the cell division cycle, the expression of AChE, and axogenesis [10].
  • Contrary to the predictions of this model, we find similar delay and onset kinetics of synaptic current at positive and negative muscle membrane potentials, even after inhibition of acetylcholinesterase [11].

Anatomical context of ache

  • In contrast to previous results using a catalytic-inactive allele, our analysis demonstrates that AChE is dispensable for muscle fiber development and Rohon-Beard sensory neuron growth and survival [5].
  • Moreover, we show that in the absence of AChE, acetylcholine receptor clusters at neuromuscular junctions initially assemble, but that these clusters are not maintained [5].
  • Acetylcholinesterase function is dispensable for sensory neurite growth but is critical for neuromuscular synapse stability [5].
  • ChAT-ir cells were restricted to the periventricular stratum of the optic tectum, but AChE-positive neurons were observed throughout the whole extension of the lamination except in the marginal stratum [12].
  • Presumptive cranial ganglia transiently expressed AChE activity between 14 and 24 hours of development [10].

Associations of ache with chemical compounds

  • Acetylcholinesterase inhibition and increased food consumption rate in the zebrafish, Danio rerio, after chronic exposure to parathion [13].
  • The AAA activity was sensitive to eserine and serotonin, ensuring its association with AChE [8].
  • The results showed that the observed cholinesterase activities in the whole embryo may be attributed mainly to acetylcholinesterase with a partial capability to use propionylthiocholine as a second substrate [14].
  • Besides AChE activity, a variety of other parameters were measured: whole-body protein and lactate content, consumption rate, survival, growth and reproduction [13].
  • Widespread innervation of the swim bladder was also indicated by acetylcholinesterase histochemistry, but choline acetyltransferase-immunoreactive (-IR) somata and fibers were limited to the junction of the pneumatic duct and esophagus [15].

Other interactions of ache


Analytical, diagnostic and therapeutic context of ache


  1. Carbofuran and malathion inhibit nucleotide hydrolysis in zebrafish (Danio rerio) brain membranes. Senger, M.R., Rico, E.P., de Bem Arizi, M., Rosemberg, D.B., Dias, R.D., Bogo, M.R., Bonan, C.D. Toxicology (2005) [Pubmed]
  2. Acetylcholinesterase is required for neuronal and muscular development in the zebrafish embryo. Behra, M., Cousin, X., Bertrand, C., Vonesch, J.L., Biellmann, D., Chatonnet, A., Strähle, U. Nat. Neurosci. (2002) [Pubmed]
  3. Segmental pattern of development of the hindbrain and spinal cord of the zebrafish embryo. Hanneman, E., Trevarrow, B., Metcalfe, W.K., Kimmel, C.B., Westerfield, M. Development (1988) [Pubmed]
  4. Zebrafish acetylcholinesterase is encoded by a single gene localized on linkage group 7. Gene structure and polymorphism; molecular forms and expression pattern during development. Bertrand, C., Chatonnet, A., Takke, C., Yan, Y.L., Postlethwait, J., Toutant, J.P., Cousin, X. J. Biol. Chem. (2001) [Pubmed]
  5. Acetylcholinesterase function is dispensable for sensory neurite growth but is critical for neuromuscular synapse stability. Downes, G.B., Granato, M. Dev. Biol. (2004) [Pubmed]
  6. The pesticide malathion reduces survival and growth in developing zebrafish. Cook, L.W., Paradise, C.J., Lom, B. Environ. Toxicol. Chem. (2005) [Pubmed]
  7. Enzymological differences of AChE and diazinon hepatic metabolism: correlation of in vitro data with the selective toxicity of diazinon to fish species. Keizer, J., D'Agostino, G., Nagel, R., Volpe, T., Gnemi, P., Vittozzi, L. Sci. Total Environ. (1995) [Pubmed]
  8. Expression of acetylcholinesterase (AChE) and aryl acylamidase (AAA) during early zebrafish embryogenesis. Allebrandt, K.V., Rajesh, V., Layer, P.G. Chem. Biol. Interact. (2005) [Pubmed]
  9. Maturation of neuromuscular transmission during early development in zebrafish. Nguyen, P.V., Aniksztejn, L., Catarsi, S., Drapeau, P. J. Neurophysiol. (1999) [Pubmed]
  10. Early expression of acetylcholinesterase activity in functionally distinct neurons of the zebrafish. Hanneman, E., Westerfield, M. J. Comp. Neurol. (1989) [Pubmed]
  11. Paired motor neuron-muscle recordings in zebrafish test the receptor blockade model for shaping synaptic current. Wen, H., Brehm, P. J. Neurosci. (2005) [Pubmed]
  12. Cholinergic elements in the zebrafish central nervous system: Histochemical and immunohistochemical analysis. Clemente, D., Porteros, A., Weruaga, E., Alonso, J.R., Arenzana, F.J., Aijón, J., Arévalo, R. J. Comp. Neurol. (2004) [Pubmed]
  13. Acetylcholinesterase inhibition and increased food consumption rate in the zebrafish, Danio rerio, after chronic exposure to parathion. Roex, E.W., Keijzers, R., van Gestel, C.A. Aquat. Toxicol. (2003) [Pubmed]
  14. Cholin- and carboxylesterase activities in developing zebrafish embryos (Danio rerio) and their potential use for insecticide hazard assessment. Küster, E. Aquat. Toxicol. (2005) [Pubmed]
  15. Structure and autonomic innervation of the swim bladder in the zebrafish (Danio rerio). Finney, J.L., Robertson, G.N., McGee, C.A., Smith, F.M., Croll, R.P. J. Comp. Neurol. (2006) [Pubmed]
  16. Bioaccumulation, oxidative stress, and neurotoxicity in Danio rerio exposed to different isotopic compositions of uranium. Barillet, S., Adam, C., Palluel, O., Devaux, A. Environ. Toxicol. Chem. (2007) [Pubmed]
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