Biosensor analysis of blood esterases for organophosphorus compounds exposure assessment: Approaches to simultaneous determination of several esterases

Chemico-Biological Interactions

Volumn 187, Issue 1-3, 2010, Pages 312-317

  Sigolaeva, Larisa ^a   Makhaeva, Galina ^b   Rudakova, Elena ^b   Boltneva, Natalia ^b   Porus, Marya ^a   Dubacheva, Galina ^a   Eremenko, Arkadi ^a   Kurochkin, Ilya ^a   Richardson, Rudy J ^c  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b INSTITUTE OF PHYSIOLOGICALLY ACTIVE COMPOUNDS   (Russian Federation)

^c UNIVERSITY OF MICHIGAN   (United States)

Author keywords

Acetylcholinesterase (AChE); Biosensor assay; Blood esterases; Butyrylcholinesterase (BChE); Carboxylesterase (CaE); Neuropathy target esterase (NTE)

Indexed keywords

ACETYLCHOLINESTERASE; CARBOXYLESTERASE; CHOLINE OXIDASE; CHOLINESTERASE; ESTERASE; MONOPHENOL MONOOXYGENASE; NEUROTOXIC ESTERASE; ORGANOPHOSPHORUS COMPOUND;

ANIMAL EXPERIMENT; ARTICLE; BIOLOGICAL MONITORING; BLOOD ANALYSIS; CONTROLLED STUDY; ENZYME ASSAY; ENZYMIC BIOSENSOR; HUMAN; MALE; MOUSE; NONHUMAN; QUANTITATIVE ANALYSIS; RAT; SENSITIVITY AND SPECIFICITY; SPECTROPHOTOMETRY;

MUS; RATTUS;

EID: 77955512958     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.01.028     Document Type: Article

References (37)

1. Nagao M., Takatori T., Matsuda Y., Nakajima M., Iwase H., Iwadate K. Definitive evidence for the acute sarin poisoning diagnosis in the Tokyo subway. Toxicol. Appl. Pharmacol. 1997, 144:198-203.
2. Makhaeva G.F., Rudakova E.V., Boltneva N.P., Sigolaeva L.V., Eremenko A.V., Kurochkin I.N., Richardson R.J. Blood esterases as a complex biomarker for exposure to organophosphorus compounds. Counteraction to Chemical and Biological Terrorism in the East Europe Countries, NATO for Peace and Security Series 2009, 177-194. Springer, Dordrecht. C. Dishovsky, A. Pivovarov (Eds.).
3. Rudakova E.V., Boltneva N.P., Makhaeva G.F. Comparative analysis of " esterase status" of human and rat. Proceedings of VIII Annual International Conference of Young Scientists on Biochemical Physics 2008, 191-196.
4. Wang G., Xu J.-J., Ye L.-H., Zhu J.-J., Chen H.-Y. Highly sensitive sensors based on the immobilization of tyrosinase in chitosan. Bioelectrochemistry 2002, 57:33-38.
5. Fengli Q., Minghui Y., Jianhui J., Guoli S., Ruqin Y. Amperometric biosensor for choline based on layer-by-layer assembled functionalized carbon nanotube and polyaniline multilayer film. Anal. Biochem. 2005, 344:108-114.
6. Decher G., Lehr B., Lowack K., Lvov Y., Schmitt J. New nanocomposite films for biosensors: layer-by-layer adsorbed films of polyelectrolytes, proteins or DNA. Biosens. Bioelectronics 1994, 9:677-684.
7. Lvov Y., Decher G., Möhwald H. Assembly, structural characterization and thermal behavior of layer-by-layer deposited ultrathin films of poly(vinylsulfate) and poly(allylamine). Langmuir 1993, 9:481-486.
8. Ferreyra N., Coche-Guerente L., Labbe P. Construction of layer-by-layer self-assemblies of glucose oxidase and cationic polyelectrolyte onto glassy carbon electrodes and electrochemical study of the redox-mediated enzymatic activity. Electrochim. Acta 2004, 49:477-484.
9. Forzani E.S., Teijelo M.L., Nart F., Calvo E.J., Solís V.M. Effect of the polycation nature on the structure of layer-by-layer electrostatically self-assembled multilayers of polyphenol oxidase. Biomacromolecules 2003, 4:869-879.
10. Dubacheva G.V., Porus M.V., Sigolaeva L.V., Pergushov D.V., Tur D.R., Papkov V.S., Zezin A.B., Yaroslavov A.A., Eremenko A.V., Kurochkin I.N., Varfolomeev S.D. Nanostructured polyelectrolyte films for engineering highly sensitive tyrosinase biosensors: specifics of enzyme/polyelectrolyte structures. Nanotechnol. Russ. 2008, 3:221-227. Russian.
11. G.V. Dubacheva, A.V. Eremenko, I.N. Kurochkin, I.P. Nikitin, S.E. Nikitina, L.V. Sigolaeva, L.G. Sokolovskaya, A.A. Yaroslavov, Sensing element for the analysis of bioactive compounds in solutions, Useful model patent of The Russian Federation No. 44483, priority-from 25.11.2004, registration-from 27.03.2005.
12. Porus M.V., Dubacheva G.V., Sigolaeva L.V., Eremenko A.V., Kurochkin I.N. Determination of cholinesterase activities by using bielectrode sensor system. Sensornie Sistemi 2008, 22:88-95. Russian.
13. Kurochkin I.N., Eremenko A.V., Makhaeva G.F., Sigolaeva L.V., Dubacheva G.V., Richardson R.J. Multi-strip assay and multimodal biosensors for environmental and medical monitoring of neurotoxicants. Counteraction to Chemical and Biological Terrorism in the East Europe Countries, NATO for Peace and Security Series 2009, 219-229. Springer, Dordrecht. C. Dishovsky, A. Pivovarov (Eds.).
14. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961, 7:88-95.
15. Worek F., Mast U., Kiderlen D., Diepold C., Eyer P. Improved determination of acetylcholinesterase activity in human whole blood. Clin. Chim. Acta 1999, 288:73-90.
16. Reiner E., Bosak A., Simeon-Rudolf V. Activity of cholinesterases in human whole blood measured with acetylthiocholine as substrate and ethopropazine as selective inhibitor of plasma butyrylcholinesterase. Arh. Hig. Rada Toksikol. 2004, 55:1-4.
17. 14C] butyrate and 4-nitrophenyl butyrate. Biochem. Pharmacol. 1985, 34:2779-2785.
18. Chanda S.M., Mortensen S.R., Moser V.C., Padilla S. Tissue-specific effects of chlorpyrifos on carboxylesterase and cholinesterase activity in adult rats: an in vitro and in vivo comparison. Fundam. Appl. Toxicol. 1997, 38:148-157.
19. Johnson M.K. Improved assay of neurotoxic esterase for screening organophosphates for delayed neurotoxicity potential. Arch. Toxicol. 1977, 67:113-115.
20. Sigolaeva L.V., Makower A., Eremenko A.V., Makhaeva G.F., Malygin V.V., Kurochkin I.N., Scheller F.W. Bioelectrochemical analysis of neuropathy target esterase activity in blood. Anal. Biochem. 2001, 290:1-9.
21. Makhaeva G.F., Sigolaeva L.V., Zhuravleva L.V., Eremenko A.V., Kurochkin I.N., Malygin V.V., Richardson R.J. Biosensor detection of neuropathy target esterase in whole blood as a biomarker of exposure to neuropathic organophosphorus compounds. J. Toxicol. Environ. Health Part A 2003, 66:599-610.
22. Huang T.L., Shiotsuki T., Uematsu T., Borhan B., Li Q.X., Hammock B.D. Structure-activity relationships for substrates and inhibitors of mammalian liver microsomal carboxylesterases. Pharm. Res. 1996, 13:1495-1500.
23. De Vriese C., Gregoire F., Lema-Kisoka R., Waelbroeck M., Robberecht P., Delporte C. Ghrelin degradation by serum and tissue homogenates: identification of the cleavage sites. Endocrinology 2004, 145:4997-5005.
24. Alha A.R., Ruohonen A., Telaranta M. Blood and brain cholinesterase activity in human death cases, in normal human subjects and in some laboratory and domestic animals. Medical Protection Against Chemical Warfare Agents, SIPRI, Almqvist & Wiksell International 1976, 151-156.
25. Tuovinen K., Kaliste-Korhonen E., Hänninen O. Gender differences in activities of mouse esterase and sensitivities to DFP and sarin toxicity. Gen. Pharmacol. 1997, 29:333-335.
26. Li B., Sedlacek M., Manoharan I., Boopathy R., Duysen E.G., Masson P., Lockridge O. Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem. Pharmacol. 2005, 70:1673-1684.
27. Crow J.A., Herring K.L., Xie S., Borazjani A., Potter P.M., Ross M.K. Inhibition of carboxylesterase activity of THP1 monocytes/macrophages and recombinant human carboxylesterase 1 by oxysterols and fatty acids. Biochim. Biophys. Acta 2008, 1781:643-654.
28. Imai T. Human carboxylesterase isozymes: catalytic properties and rational drug design. Drug Metab. Pharmacokinet. 2006, 21:173-185.
29. Sakurai Y., Ma S.F., Watanabe H., Yamaotsu N., Hirono S., Kurono Y., Kragh-Hansen U., Otagiri M. Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharm. Res. 2004, 21:285-292.
30. Lockridge O., Xue W., Gaydess A., Grigoryan H., Ding S.J., Schopfer L.M., Hinrichs S.H., Masson P. Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines. J. Biol. Chem. 2008, 283:22582-22590.
31. Johnson M.K. The target for initiation of delayed neurotoxicity by organophosphorus esters: Biochemical studies and toxicological applications. Reviews in Biochemical Toxicology 1982, vol. 4:141-212. Elsevier, Amsterdam.
32. Novak R., Padilla S. An in vitro comparison of rat and chicken brain neurotoxic esterase. Fundam. Appl. Toxicol. 1986, 6:464-471.
33. Dyer K.R., Jortner B.S., Shell L.G., Ehrich M. Comparative dose-response studies of organophosphorus ester-induced delayed neuropathy in rats and hens administered mipafox. Neurotoxicology 1992, 13:745-755.
34. Makhaeva G.F., Filonenko I.V., Malygin V.V. A comparative study of the interaction of phosphoric acid dichlorovinyl esters with a neurotoxic esterase from the brain of hens and rats. Zh. Evol. Biokhim. Fiziol. 1995, 31:396-403.
35. Kohli N., Srivastava D., Sun J., Richardson R.J., Lee I., Worden R.M. Nanostructured biosensor for measuring neuropathy target esterase activity. Anal. Chem. 2007, 79:5196-5203.
36. Haigh J.R., Lefkowictz L.J., Capacio B.R., Doctor B.P., Gorton R.K. Advantages of the WRAIR whole blood cholinesterase assay: comparative analysis to the micro-Ellman, Test-mate ChE™, and Michel (ΔpH) assays. Chem. Biol. Interact. 2008, 175:417-420.
37. Richardson R.J., Worden R.M., Makhaeva G.F. Biomarkers and biosensors of delayed neuropathic agents. Handbook of Toxicology of Chemical Warfare Agents 2009, 859-876. Academic Press/Elsevier, Amsterdam. R.C. Gupta (Ed.).