#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Cholinesterase activity assays and their use in the diagnosis of various pathological states including poisoning by neurotoxic agents


Authors: Miroslav Pohanka
Published in: Čes. slov. Farm., 2017; 66, 147-153
Category: Review Articles

Overview

Cholinesterases are enzymes important for some nerve transmissions where the enzyme acetylcholinesterase plays a crucial role. The second enzyme, butyrylcholinesterase, is not necessary for the neurotransmission but it is involved in some detoxification reactions. A survey of literature, a discussion of diagnostic importance and the methods for an activity assay are presented in this review article. Liver failures, exposure to neurotoxic compounds, genetic dispositions are outlined here. In the field of assays, spectrophotometric, colorimetric and electrochemical tests are discussed.

Key words:
acetylcholinesterase • butyrylcholinesterase • poisoning • liver function test • pesticide • nerve agent • Alzheimer disease • pathological state


Sources

1. Pohanka M. Cholinesterases, a target of pharmacology and toxicology. Biomed. Pap. Olomouc 2011; 155, 219–229.

2. Duysen E. G., Li B., Lockridge O. The butyrylcholinesterase knockout mouse a research tool in the study of drug sensitivity, bio-distribution, obesity and Alzheimer’s disease. Expert Opin. Drug Metab. Toxicol. 2009; 5, 523–528.

3. Li B., Duysen E. G., Carlson M., Lockridge O. The butyrylcholinesterase knockout mouse as a model for human butyrylcholinesterase deficiency. J. Pharmacol. Exp. Ther. 2008; 324, 1146–1154.

4. Yuan J., Yin J., Wang E. Characterization of procaine metabolism as probe for the butyrylcholinesterase enzyme investigation by simultaneous determination of procaine and its metabolite using capillary electrophoresis with electrochemiluminescence detection. J. Chromatogr. A 2007; 1154, 368–372.

5. Duysen E. G., Lockridge O. Prolonged toxic effects after cocaine challenge in butyrylcholinesterase/plasma carboxylesterase double knockout mice: a model for butyrylcholinesterase-deficient humans. Drug Metab. Dispos. 2011; 39, 1321-1323.

6. Masson P., Carletti E., Nachon F. Structure, activities and biomedical applications of human butyrylcholinesterase. Protein Pept. Lett. 2009; 16, 1215–1224.

7. Cygler M., Schrag J. D., Sussman J. L., Harel M., Silman I., Gentry M. K., Doctor B. P. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci. 1993; 2, 366–382.

8. Akoh C. C., Lee G. C., Liaw Y. C., Huang T. H., Shaw J. F. GDSL family of serine esterases/lipases. Prog. Lipid Res. 2004; 43, 534–552.

9. Myers M., Richmond R. C., Oakeshott J. G. On the origins of esterases. Mol. Biol. Evol. 1988; 5, 113–119.

10. Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H., Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D., Harel M., Silman I., Sussman J. L., Velan B. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J. Biol. Chem. 1992; 267, 17640–17648.

11. Lockridge O., Bartels C. F., Vaughan T. A., Wogn C. K., Norton S. E., Johnson L. L. Complete amino acid sequence of human serum cholinesterase. J. Biol. Chem. 1987; 262 549–557.

12. Massoulie J., Anselmet A., Bon S., Krejci E., Legay C., Morel N., Simon S. The polymorphism of acetylcholinesterase: post-translational processing, quaternary associations and localization. Chem. Biol. Interact. 1999; 120, 29–42.

13. Nawaz S. A., Ayaz M., Brandt W., Wessjohann L. A., Westermann B. Cation-π and π-π stacking interactions allow selective inhibition of butyrylcholinesterase by modified quinine and cinchonidine alkaloids. Biochem. Biophys. Res. Commun. 2011; 404, 935–940.

14. Pohanka M. Acetylcholinesterase inhibitors: a patent review (2008 – present). Expert Opin. Ther. Pat. 2012; 22, 871–886.

15. Johnson G., Moore S. W. The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design. Curr. Pharm. Des. 2006; 12, 217–225.

16. Cometa M. F., Lorenzini P., Fortuna S., Volpe M. T., Meneguz A., Palmery M. In vitro inhibitory effect of aflatoxin B-1 on acetylcholinesterase activity in mouse brain. Toxicology 2005; 206, 125–135.

17. Stepurska K. V., Soldatkin O. O., Arkhypova V. M., Soldatkin A. P., Lagarde F., Jaffrezic-Renault N., Dzyadevych S. V. Development of novel enzyme potentiometric biosensor based on pH-sensitive field-effect transistors for aflatoxin B1 analysis in real samples. Talanta 2015; 144, 1079–1084.

18. Cavalli A., Bottegoni G., Raco C., De Vivo M., Recanatini M. A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase. J. Med. Chem. 2004; 47, 3991–3999.

19. Mazzanti C. M., Spanevello R. M., Obregon A., Pereira L. B., Streher C. A., Ahmed M., Mazzanti A., Graca D. L., Morsch V. M., Schetinger M. R. Ethidium bromide inhibits rat brain acetylcholinesterase activity in vitro. Chem. Biol. Interact. 2006; 162, 121–127.

20. Wong D. M., Greenblatt H. M., Dvir H., Carlier P. R., Han Y. F., Pang Y. P., Silman I., Sussman J. L. Acetylcholinesterase complexed with bivalent ligands related to huperzine a: experimental evidence for species-dependent protein-ligand complementarity. J. Am. Chem. Soc. 2003; 125, 363–373.

21. Saxena A., Redman A. M., Jiang X., Lockridge O., Doctor B. P. Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Biochemistry 1997; 36, 14642–14651.

22. Khan I., Samad A., Khan A. Z., Habtemariam S., Badshah A., Abdullah S. M., Ullah N., Khan A., Zia-Ul-Hag M. Molecular interactions of 4-acetoxy-plakinamine B with peripheral anionic and other catalytic subsites of the aromatic gorge of acetylcholinesterase: computational and structural insights. Pharm. Biol. 2013; 51, 722–727.

23. Axelsen P. H., Harel M., Silman I., Sussman J. L. Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography. Protein Sci. 1994; 3, 188–197.

24. Gilson M. K., Straatsma T. P., McCammon J. A., Ripoll D. R., Faerman C. H., Axelsen P. H., Silman I., Sussman J. L. Open „back door“ in a molecular dynamics simulation of acetylcholinesterase. Science 1994; 263, 1276–1278.

25. Holtje H. D., Kjier L. B. Nature of anionic or alpha-site of cholinesterase. J. Pharm. Sci. 1975; 64, 418–420.

26. Marrs T. C. Organophosphate poisoning. Pharmacol. Ther. 1993; 58, 51–66.

27. Andreescu S., Marty J. L. Twenty years research in cholinesterase biosensors: from basic research to practical applications. Biomol. Eng. 2006; 23, 1–15.

28. Yu Q. S., Holloway H. W., Luo W., Lahiri D. K., Brossi A., Greig N. H. Long-acting anticholinesterases for myasthenia gravis: synthesis and activities of quaternary phenylcarbamates of neostigmine, pyridostigmine and physostigmine. Bioorg. Med. Chem. 2010; 18, 4687–4693.

29. Venkatasubban K. S., Johnson J. L., Thomas J. L., Faug A., Cusack B., Rosenberry T. L. Steric effects in the decarbamoylation of carbamoylated acetylcholinesterases. Chem. Biol. Interact. 2005; 157–158.

30. Yang Z. Z., Zhang Y. Q., Wu K., Wang Z. Z., Qi X. R. Tissue distribution and pharmacodynamics of rivastigmine after intranasal and intravenous administration in rats. Curr. Alzheimer Res. 2012; 9, 315–325.

31. Tayeb H. O., Yang H. D., Price B. H., Tarazi F. I. Pharmacotherapies for Alzheimer‘s disease: beyond cholinesterase inhibitors. Pharmacol. Ther. 2012; 134, 8–25.

32. Rai D. K., Sharma B. Carbofuran-induced oxidative stress in mammalian brain. Mol. Biotechnol. 2007; 37, 66–71.

33. Bucaretchi F., Prado C. C., Branco M. M., Soubhia P., Metta G. M., Mello S. M., de Capitani E. M., Lanaro R., Hyslop S., Costa J. L., Fernandes L. C. R., Vieira R. J. Poisoning by illegal rodenticides containing acetylcholinesterase inhibitors (chumbinho): a prospective case series. Clin. Toxicol. 2012; 50, 44–51.

34. Rampa A., Belluti F., Gobbi S., Bisi A. Hybrid-based multi-target ligands for the treatment of Alzheimer‘s disease. Curr. Top. Med. Chem. 2011; 11, 2716–2730.

35. Bai D. L., Tang X. C., He X. C. Huperzine A, a potential therapeutic agent for treatment of Alzheimer´s disease. Curr. Med. Chem. 2000; 7, 355–374.

36. Liu J., Zhang H. Y., Tang X. C., Wang B., He X. C., Bai D. L. Effects of synthetic (-)-huperzine A on cholinesterase activities and mouse water maze performance. Zhongguo Yao Li Xue Bao 1998; 19, 413–416.

37. Luo W., Li Y. P., He Y., Huang S. L., Li D., Gu L. Q., Huang Z. S. Synthesis and evaluation of heterobivalent tacrine derivatives as potential multi-functional anti-Alzheimer agents. Eur. J. Med. Chem. 2011; 46, 2609–2616.

38. Jogani V. V., Shah P. J., Mishra P., Mishra A. K., Misra A. R. Nose-to-brain delivery of tacrine. J. Pharm. Pharmacol. 2007; 59, 1199–1205.

39. Knapp M. J., Gracon S. I., Davis C. S., Solomon P. R., Pendlebury W. W., Knopman D. S. Efficacy and safety of high-dose tacrine – a 30 week evaluation Alzheimer Dis. Assoc. Dis. 1994; 8, S22–S31.

40. Davis K. L., Thal L. J., Gamzu E. R., Davis C. S., Woolson R. F., Gracon S. I., Drachman D. A., Schneider L. S., Whitehouse P. J., Hoover T. M., Morris J. C., Kawas C. H., Knopman D. S., Earl N. L., Kumar V., Doody R. S. A double-blind, placebo-controlled multicenter study of tacrine for Alzheimers-disease. New Engl. J. Med. 1992; 327, 1253–1259.

41. da Silva V. B., de Andrade P., Kawano D. F., Morais P. A. B., de Almeida J. R., Carvalho I., Taft C. A., da Silva C. In silico design and search for acetylcholinesterase inhibitors in Alzheimer’s disease with a suitable pharmacokinetic profile and low toxicity. Future Med. Chem. 2011; 3, 947–960.

42. Rainer M. Galanthamine in Alzheimer’s disease - A new alternative to tacrine? CNS Drugs 1997; 7, 89–97.

43. Lilienfeld S. Galantamine – a novel cholinergic drug with a unique dual mode of action for the treatment of patients with Alzheimer’s disease. CNS Drug. Rev. 2002; 8, 159–176.

44. Darreh-Shori T., Soininen H. Effects of cholinesterase inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzheimer’s disease: a review of recent clinical studies. Curr. Alzheimer Res. 2010; 7, 67–73.

45. Thomsen T., Kewitz H. Selective inhibition of human acetylcholinesterase by galanthamine in vitro and in vivo. Life Sci. 1990; 46, 1553–1558.

46. Berg L., Andersson C. D., Artursson E., Hornberg A., Tunemalm A. K., Linusson A., Ekstrom F. Targeting acetylcholinesterase: identification of chemical leads by high throughput screening, structure determination and molecular modeling. PLoS One 2011; 6, e26039.

47. Cheewakriengkrai L., Gauthier S. A 10-year perspective on donepezil. Expert Opin. Pharmacother. 2013; 14 331–338.

48. Pohanka M. Spectrophotomeric assay of aflatoxin B1 using acetylcholinesterase immobilized on standard microplates. Anal. Lett. 2013; 46, 1306–1315.

49. Plageman L. R., Pauletti G. M., Skau K. A. Characterization of acetylcholinesterase in Caco-2 cells. Exp. Biol. Med. (Maywood) 2002; 227, 480–486.

50. Zhukovskii Y. G. On establishment of individuality of the choliensterase enzyme in the studied preparation. J. Evol. Biochem. Physiol. 2003; 39, 281–290.

51. Giacobini E. Cholinesterases: new roles in brain function and in Alzheimer’s disease. Neurochem. Res. 2003; 28, 515–522.

52. Grigoryan H. A., Hambardzumyan A. A., Mkrtchyan M. V., Topuzyan V. O., Halabyan G. P., Asatryan R. S. alpha,beta-Dehydrophenylalanine choline esters, a new class of reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. Chem. Biol. Interact. 2008; 171, 108–116.

53. Tecles F., Ceron J. J. Determination of whole blood cholinesterase in different animal species using specific substrates. Res. Vet. Sci. 2001; 70, 233–238.

54. Debord J., Laubarie C., Dantoine T. Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates. Anal. Biochem. 2008; 373, 247–252.

55. Kamal M. A., Klein P., Luo W., Li, Y., Holloway H. W., Tweedie D., Greig N. H. Kinetics of human serum butyrylcholinesterase inhibition by a novel experimental Alzheimer therapeutic, dihydrobenzodioxepine cymserine. Neurochem. Res. 2008; 33, 745–753.

56. Nagasawa T., Sagisaki H., Tani Y., Ogatak K. Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor. Biochim. Biophys. Acta 1976; 429, 817–827.

57. Monteiro M., Quintaneiro C., Morgado F., Soares A. M., Guilhermino L. Characterization of the cholinesterases present in head tissues of the estuarine fish Pomatoschistus microps: application to biomonitoring. Ecotoxicol. Environ. Saf. 200; 5; 62, 341–347.

58. Masson P., Froment M. T., Gillon E., Nachon F., Darvesh S., Schopfer L. M. Kinetic analysis of butyrylcholinesterase-catalyzed hydrolysis of acetanilides. Biochim Biophys Acta 2007; 1774, 1139–1147.

59. Montenegro M. F., Moral-Naranjo M. T., de la Cadena P. M., Campoy F. J., Munoz-Delgado E., Vidal C. J. The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution. Chem. Biol. Interact. 2008; 175, 336–339.

60. Montenegro M. F., Maria T. M., de la Cadena M. P., Campoy F. J., Munoz-Delgado E., Vidal C. J. Human butyrylcholinesterase components differ in aryl acylamidase activity. Biol. Chem. 2008; 389, 425–432.

61. Pohanka M. Biosensors containing acetylcholinesterase and butyrylcholinesterase as recognition tools for detection of various compounds. Chem. Pap. 2015; 69, 4–16.

62. Pohanka M. Butyrylcholinesterase as a biochemical marker, a review. Brat. Med. J. 2013; 114, 726–734.

63. Pohanka M., Karasova J. Z., Kuca K., Pikula J., Holas O., Korabecny O., Cabal J. Colorimetric dipstick for assay of organophosphate pesticides and nerve agents represented by paraoxon, sarin and VX. Talanta 2010; 81, 621–624.

64. Bazire A., Gillon E., Lockridge O., Vallet V., Nachon F. The kinetic study of the inhibition of human cholinesterases by demeton-S-methyl shows that cholinesterase-based titration methods are not suitable for this organophosphate. Toxicol. Vitro 2011; 25, 754–759.

65. Bartling A., Worek F., Szinicz L., Thiermann H. Enzyme-kinetic investigation of different sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase. Toxicology 2007; 233, 166–172.

66. Gabrovska K., Marinov I., Godjevargova T., Portaccio M., Lepore M., Grano V., Diano N., Mita D. G. The influence of the support nature on the kinetics parameters, inhibition constants and reactivation of immobilized acetylcholinesterase. Int. J. Biol. Macromol. 2008; 43, 339–345.

67. Ellman G. L., Courtney K. D., Andres V., Jr., Feather-Stone R. M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961; 7, 88–95.

68. Pohanka M. Cholinesterases in biorecognition and biosensor construction, a review. Anal. Lett. 2013; 46, 1849–1868.

69. Eyer P., Worek F., Kiderlen D., Sinko G., Stuglin A., Simeon-Rudolf V., Reiner E. Molar absorption coefficients for the reduced Ellman reagent: reassessment. Anal. Biochem. 2003; 312, 224–227.

70. Sinko G., Calic M., Bosak A., Kovarik Z. Limitation of the Ellman method: Cholinesterase activity measurement in the presence of oximes. Anal. Biochem. 2007; 370, 223–227.

71. Zitova A., O’Mahony F. C., Kurochkin I. N., Papkovsky D. B. A simple screening assay for cholinesterase activity and inhibition based on optical oxygen detection Anal. Lett. 2010; 43, 1746–1755.

72. Evans O. On-line deoxygenation in reductive (and oxidative) amperometric detection: environmental applications in the liquid chromatography of organic peroxides. Analyst 1999; 124, 1811–1816.

73. No H. Y., Kim Y. A., Lee Y. T., Lee H. S. Cholinesterase-based dipstick assay for the detection of organophosphate and carbamate pesticides. Anal. Chim. Acta 2007; 594, 37–43.

74. Wu Z. L., Podust M. L. M., Guengerich F. P. Expansion of substrate specificity of cytochrome P450 2A6 by random and site-directed mutagenesis. J. Biol. Chem. 2005; 280, 41090–41100.

75. Tingfa D., Shiguang Z., Mousheng T. A new micro-detection tube for cholinesterase inhibitors in water. Enivron. Pollut. 1989; 57, 217–222.

76. Miao Y., He N., Zhu J. J. History and new developments of assay for cholinesterase activity and inhibition. Chem. Rev. 2010; 110, 5216–5234.

77. Guilbault G. G., Kramer D. N. Resorufin butyrate and indoxyl acetate as fluorogenic substrates for cholinesterase. Anal. Chem. 1965; 37, 120–123.

78. Pohanka M. Acetylcholinesterase based dipsticks with indoxylacetate as a substrate for assay of organophosphates and carbamates Anal. Lett. 2012; 45, 367–374.

79. Santarpia L., Grandone I., Contaldo F., Pasanisi F. Butyrylcholinesterase as a prognostic marker: a review of the literature. J. Cachexia Sarcopenia Muscle 2013; 4, 31–39.

80. Lockridge O. Review of human butyrylcholinesterase structure, function, genetic variants, history of use in the clinic, and potential therapeutic uses. Pharmacol. Ther. 2015; 148, 34–46.

81. Iwasaki T., Yoneda M., Nakajima A., Terauchi Y. Serum butyrylcholinesterase is strongly associated with adiposity, the serum lipid profile and insulin resistance. Intern. Med. 2007; 46, 1633–1639.

82. Ostergaard D., Viby-Moogensen J., Hanel H. K., Skovgaard L. T. Half-life of plasma cholinesterase. Acta Anaesthesiol. Scand. 1988; 32, 266–269.

83. Tajiri J., Nishizono Y., Fujiyama S., Sagara K., Sato T., Shibata H. Hypercholinesterasemia in patients with hepatocellular carcinoma: a new paraneoplastic syndrome. Gastroenterol Jpn 1983; 18, 137–141.

84. Lu W. D., Hada T., Fukui K., Imanishi H., Matsuoka N., Iwasaki A., Higashino K. Familial hypocholinesterasemia found in a family and a new confirmed mutation. Intern. Med. 1997; 36, 9–13.

85. Prellwitz W., Kapp S., Muller D. Comparative methods for the determination of the activity of serumcholinesterases (acylcholin-acyl-hydrolase E.C. 3.1.1.8) and their diagnostical value J. Clin. Chem. Clin. Biochem. 1976; 14, 93–97.

86. Duran-Ferreras E., Diaz-Narvaez F., Raffo-Marquez M. Chronic hepatic encephalopathy in a patient with primary biliary cirrhosis. Gastroenterol. Hepatol. 2011; 34, 401–405.

87. Kemkes-Matthes B., Preissner K. T., Langenscheidt F., Matthes K. J., Muller-Berghaus G. S protein/vitronectin in chronic liver diseases: correlations with serum cholinesterase, coagulation factor X and complement component C3. Eur. J. Haematol. 1987; 39, 161–165.

88. Kassa J. Review of oximes in the antidotal treatment of poisoning by organophosphorus nerve agents. J. Toxicol.-Clin. Toxicol. 2002; 40, 803–816.

89. Bajgar J. Organophosphates/nerve agent poisoning: Mechanism of action, diagnosis, prophylaxis, and treatment Adv. Clin. Chem. 2004; 38, 151–216.

90. Bajgar J. Biological monitoring of exposure to nerve agents. Brit. J. Ind. Med. 1992; 49 648–653.

91. Pohanka M. Alzheimer’s disease and related neurodegenerative disorders: implication and counteracting of melatonin. J. Appl. Biomed. 2011; 9, 185–196.

92. Hashim Y., Shepherd D., Wiltshire S., Holman R., Levy J. C., Clark A., Cull C. A. Butyrylcholinesterase K variant on chromosome 3 q is associated with Type II diabetes in white Caucasian subjects. Diabetologia 2001; 44, 2227–2230.

93. Holmes C., Ballard C., Lehmann D., Smith A. D., Beaumont H., Day I. N., Khan M. N., Lovestone S., McCulley M., Morris C. M., Munoz D. G., O’Brien K., Russ C., Del Ser T., Warden D. Rate of progression of cognitive decline in Alzheimer’s disease: effect of butyrylcholinesterase K gene variation. J. Neurol. Neurosur. Ps. 2005; 76, 640–643.

94. Kaufman S. E., Donnell R. W., Aiken D. C., Magee C. Prolonged neuromuscular paralysis following rapid-sequence intubation with succinylcholine. Ann. Pharmacother. 2011; 45, e21.

95. Kalow W., Genest K. A method for the detection of atypical forms of human serum cholinesterase; determination of dibucaine numbers. Can. J. Biochem. Physiol. 1957; 35, 339–346.

96. Yen T., Nightingale B. N., Burns J. C., Sullivan D. R., Stewart P. M. Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population. Clin. Chem. 2003; 49, 1297–1308.

97. Pohanka M. Determination of acetylcholinesterase and butyrylcholinesterase activity without dilution of biological samples. Chem. Pap. 2015; 69, 1044–1049.

Labels
Pharmacy Clinical pharmacology
Login
Forgotten password

Enter the email address that you registered with. We will send you instructions on how to set a new password.

Login

Don‘t have an account?  Create new account

#ADS_BOTTOM_SCRIPTS#