Sequence analysis of the acetylcholinesterase 1 translated from messenger ribonucleic acid of the nervous system of crayfish (Cherax quadricarinatus)
Paper Details
Sequence analysis of the acetylcholinesterase 1 translated from messenger ribonucleic acid of the nervous system of crayfish (Cherax quadricarinatus)
Abstract
Crayfish are the animal models used as biomarkers of exposure to pesticides. Some compounds such as organophosphates work by blocking Acetylcholinesterase (AChE), an enzyme that hydrolyzes the neurotransmitter acetylcholine on cholinergic synapses. In insects recurrent exposure to pesticides produces resistance, and the molecular analysis has identified mutations as the cause of this resistance. Till date, there are a few sequences reported for crustaceans. Even more, there are no reports of sequences in any species of crayfish that allow make comparative studies. In this study, we obtained the specific sequence of messenger Ribonucleic acid (mRNA) for the AChE1 protein from the crayfish, Cherax quadricarinatus. The mRNA was isolated from abdominal nerve cord of C. quadricarinatus. Degenerate oligonucleotides were used and the 1242 nucleotides sequence was directly obtained from PCR products. We have deposited this sequence with the accession number [GenBank KT007499]. Analysis of the 414 amino acid residues of the putative AChE protein showed a high homology to the Esterase-lipase super family. We identified 60% to 64% similarity of AChE1 in insects and crustaceans with well-conserved AChE1 main domains. We concluded that the partial sequence analysis to this putative mRNA and the comparative studies with other species clearly shows that the sequence corresponds to the translated product Acetylcholinesterase-1.
Braun G, Mulloney B. 1994. Acetylcholinesterase activity in neurons of crayfish abdominal ganglia. Journal of Comparative Neurology 350, 272-280. http://dx.doi.org/10.1002/cne.903500210
Cha DJ, Lee SH. 2015. Evolutionary origin and status of two insect acetylcholinesterases and their structural conservation and differentiation. Evolution & Development 17, 109-119. http://dx.doi.org/10.1111/ede.12111.
Combes D, Fedon Y, Toutan JP, Arpagaus M. 2003. Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression. The European Journal of Neuroscience 18, 497-512. http://dx.doi.org/10.1046/j.1460-9568.2003027.49.x
Devi M, Fingerman M. 1995. Inhibition of Acetylcholinesterase activity in the central nervous system of the red swamp crayfish, Procambarus clarkia, by mercury, Cadmium and Lead. Bulletin of Environmental Contamination and Toxicology 55, 746-750. 10 http://dx.doi.org/.1007/BF00203762
Escartin E, Porte C. 1996. Acetylcholinesterase inhibition in the crayfish Procambarus clarkia exposed to Fenitrothion. Ecotoxicology and Environmental Safety 34, 160-164. http://dx.doi.org/10.1006/eesa.1996.0058
Habig C, Di Giulio RT, Abou-Donia MB. 1988. Comparative properties of channel catfish (Ictalurus punctatus) and blue crab (Callinectes sapidus) acetylcholinesterases. Comparative Biochemistry and Physiology C 91, 293-300. http://dx.doi.org/10.1016/0742-8413(88)90032-1
Hall LM, Spierer P. 1986. The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5’ leader. The European Molecular Biology Organization Journal 5, 2949-2954.
Huchard E, Martinez M, Alout H, Douzery EJP, Luftalla G, Berthomieu, Berticat C, Raymond M, Weill M. 2006. Acetylcholinesterase genes within the Diptera: takeover and loss in true flies. Proceedings. Biological Sciences. The Royal Society B 273, 2595-2604. http://dx.doi.org/10.1098/rspb.2006.3621
Karczmar AG. 2010. Cholinesterases (CHEs) and the cholinergic system in ontogenesis and phylogenesis, a non-classical roles of cholinesterases-A review. Chemico-Biological Interactions 187, 34-43. http://dx.doi.org/10.1016/j.cbi.2010.03.009.Epub2010 Mar 10.
Kaur K, Jorgensen Bakke M, Nilsen F, Horsberg TE. 2015. Identification and molecular characterization of two Acetylcholinesterases from the Salmon Louse Lepeophtheirus salmonis. PLoS ONE 10(5), e0125362. 1 http://dx.doi.org/0.1371/journal.pone.0125362
Kim YH, Lee SH. 2013. Which acetylcholinesterase functions as the main catalytic enzyme in the Class Insecta? Insect Biochemistry and Molecular Biology 43, 47-53. http://dx.doi.org/10.1016/j.ibmb.2012.11.004.
Massoulie J, Sussman J, Bon S, Silman I. 1993. Structure and function of acetylcholinesterase and butyrylcholinesterase. Progress in Brain Research 98, 139-146. http://dx.doi.org/10.1016/S0079-6123(08)62391-2
Mutero A, Pralavorio M, Bride JM, Fournier D. 1994. Resistance-associated point mutations in insecticide-insensitive acetylcholinesterase. Proceedings of the National Academy of Sciences of the United States of America 91, 5922-5926.
Pezzementi L, Chatonnet A. 2010. Evolution of cholinesterases in the animal kingdom. Chemico-Biological Interactions 187, 27-33. http://dx.doi.org/10.1016/j.cbi.2010.03.043
Repetto G, Sanz P, Repetto M. 1988. In vivo and in vitro Effect of Triclofon on esterases of the red crayfish Procambarus clarkia. Bulletin Environmental Contamination and Toxicology 41, 597-603. http://dx.doi.org/10.1007/BF02021006
Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor SS, Friedmann T, Taylor P. 1986. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature 319, 407-409. http://dx.doi.org/10.1038/319407a0
Silman I, Sussman JL. 2008. Acetylcholinesterase: How is structure related to function? Mini review. Chemico-Biological Interactions 175, 3-10. http://dx.doi.org/10.1016/j.cbi.2008.05.035.
Society for Neuroscience. 2015. Policies on the use of animals and humans in research. http://www.sfn.org/advocacy/policypositions/policie s-on-the-use-of-animals-and-humans-in-research.
Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silmman I. 1991. Atomic Structure of Acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science 253, 872-879. http://dx.doi.org/10.1126/science.1678899
Tamura K, Dudley J, Nei M, Kumar S. 2007. Mega 4: Molecular evolutionary genetics analysis (MEGA) Software version 4.0. Molecular Biology and Evolution 24, 1596-1599. http://dx.doi.org/10.1093/molbev/msm092
Takeuchi A, Takeuchi N. 1964. The effect on crayfish muscle of iontophoretically applied glutamate. The Journal of Physiology 170, 296-317. http://dx.doi.org/10.1113/jphysiol.1964.sp007332
Van Harreveld A, Mendelson M. 1959. Glutamate-induced contractions in crustacean muscle. Journal of Cellular and Comparative Physiology 54, 85-94. http://dx.doi.org/10.1002/jcp.1030540109
Vioque-Fernández A, Alves de Almeida E, López-Barea J. 2007. Esterases as pesticide biomarkers in crayfish (Procambarus clarkii, Crustacea): Tissue distribution, sensitivity to model compounds and recovery from inactivation.
Comparative Biochemistry and Physiology C 145, 404-412. http://dx.doi.org/10.1080/13547500902913211
Weill M, Fort P, Berthomieu A, Pierre Dubois M, Pasteur N, Raymond M. 2002. A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila. Proceedings. Biological Sciences. The Royal Society 269, 2007-2016. http://dx.doi.org/10.1098/rspb.2002.2122
Wu S, Li M, Tang PA, Felton GW, Wang JJ. 2010. Cloning and characterization of acetylcholinesterase 1 genes from insecticide-resistant field populations of Liposcelis paeta Pearman (Psocoptera: Liposcelididae). Insect Biochemistry and Molecular Biology 40, 415-424. http://dx.doi.org/10.1016/j.ibmb.2010.04.001
Zhao P, Wang Y, Jiang H. 2013. Biochemical properties, expression profiles, and tissue localization of orthologous acetylcholinesterase-2 in the mosquito, Anopheles gambiae. Insect Biochemistry and Molecular Biology 43, 260-271. http://dx.doi.org/10.1016/j.ibmb.2012.12.005
Gabina Calderón-Rosete, Juan Antonio González-Barrios, Luis Kameyama, Emma Arguijo-Hernández, Leonardo Rodríguez-Sosa, 2015. Sequence analysis of the acetylcholinesterase 1 translated from messenger ribonucleic acid of the nervous system of crayfish (Cherax quadricarinatus). Int. J. Biosci., 7(6), 32-41.
Copyright © 2015 by the Authors. This article is an open access article and distributed under the terms and conditions of the Creative Commons Attribution 4.0 (CC BY 4.0) license.