Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R)

Analytical Biochemistry

Volumn 385, Issue 1, 2009, Pages 94-100

  Kanamori Kataoka, Mieko ^a   Seto, Yasuo ^a  

^a NATIONAL RESEARCH INSTITUTE OF POLICE SCIENCE   (Japan)

Author keywords

Capillary electrophoresis; Catalytic efficiency; Human serum paraoxonase; Nerve gas; Polymorphism

Indexed keywords

AFFINITY CHROMATOGRAPHY; CAPILLARY ELECTROPHORESIS; DICHLOROMETHANE; ENZYMES; HYDROLYSIS; POLYMERASE CHAIN REACTION; SORBIC ACID;

ANION EXCHANGE CHROMATOGRAPHY; CATALYTIC EFFICIENCIES; FRAGMENTATION PATTERNS; HUMAN SERUM; HYDROLYTIC ACTIVITIES; HYDROLYZING ACTIVITY; LINEWEAVER-BURK PLOTS; NERVE GAS;

POLYMORPHISM;

ARYLDIALKYLPHOSPHATASE 1; GENOMIC DNA; NERVE GAS;

AFFINITY CHROMATOGRAPHY; ARTICLE; CAPILLARY ELECTROPHORESIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME POLYMORPHISM; GENE FREQUENCY; HUMAN; HUMAN EXPERIMENT; HYDROLYSIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL;

EID: 57749179505     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.09.044     Document Type: Article

References (49)

1. Seto Y., Tsunoda N., Kataoka M., Tsuge K., and Nagano T. Toxicological analysis of Victims' blood and crime scene evidence samples in the sarin gas attack caused the Aum Shinrikyo cult. In: Tu A.T., and Gaffield W. (Eds). Natural and Selected Synthetic Toxins -Biological Implications (1999), American Chemical Society, Washington DC 318-332
2. Somani S.M., Solana R.P., and Dube S.N. Toxicodynamics of nerve agents. In: Somani S.M. (Ed). Chemical Warfare Agents (1992), Academic Press, New York 67-123
3. van der Schans M.J., Fidder A., van Oeveren D., Hulst A.G., and Noort D. Verification of exposure to cholinesterase inhibitors: generic detection of OPCW schedule 1 nerve agent adducts to human butyrylcholinesterase. J. Anal. Toxicol. 32 (2008) 125-130
4. Nakajima T., Sasaki K., Ozawa H., Sekijima Y., Morita H., Fukushima Y., and Yanagisawa N. Urinary metabolites of sarin in a patient of the Matsumoto sarin incident. Arch. Toxicol. 72 (1998) 601-603
5. Watkins L.M., Mahoney H.J., McCulloch J.K., and Raushel F.M. Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase. J. Biol. Chem. 272 (1997) 25596-25601
6. Lai K., Stolowich N.J., and Wild J.R. Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch. Biochem. Biophys. 318 (1995) 59-64
7. Mulbry W.W., and Karns J.S. Purification and characterization of three parathion hydrolases from gram-negative bacterial strains. Appl. Environ. Microbiol. 55 (1989) 289-293
8. Hoskin F.C.G., and Long R.J. Purification of a DFP-hydrolyzing enzyme from squid head ganglion. Arch. Biochem. Biophys. 150 (1972) 548-555
9. Blum M.M., Löhr F., Richardt A., Rüterjans H., and Chen J.C.H. Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism. J. Am. Chem. Soc. 128 (2006) 12750-12757
10. Draganov D.I., and La Du B.N. Pharmacogenetics of paraoxonases: a brief review. Naunyn. Schmiedebergs Arch Pharmacol. 369 (2004) 78-88
11. La Du B.N. Structural and functional diversity of paraoxonases. Nature Med. 2 (1996) 1186-1187
12. Biggadike K., Angell R.M., Burgess C.M., Garrell R.M., Hancock A.P., Harker A.J., Irving W.R., Ioannou C., Procopiou P.A., Shaw R.E., Solanke Y.E., Singh O.M., Snowden M.A., Stubbs R.J., Walton S., and Weston H.E. Selective plasma hydrolysis of glucocorticoid g-lactones and cyclic carbonates by the enzyme paraoxonase: an ideal plasma inactivation mechanism. J. Med. Chem. 43 (2000) 19-21
13. Billecke S., Draganov D., Counsell R., Stetson P., Watson C., Hsu C., and La Du B.N. Human serum paraoxonase (PON1) isozyme Q and R hydrolyze lactones and cyclic carbonate esters. Drug Metab. Dispos. 28 (2000) 1335-1342
14. Davies H.G., Richter R.J., Keifer M., Broomfield C.A., Sowalla J., and Furlong C.E. The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman, sarin. Nature Genet. 14 (1996) 334-336
15. Shih D.M., Gu L., Xia Y.-R., Navab M., Li W.-F., Hama S., Castellani L.W., Furlong C.E., Costa L.G., Fogelman A.M., and Lusis A.J. Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature 394 (1998) 284-287
16. Adkins S., Gan K.N., Mody M., and La Du B.N. Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B alloenzyme. Am. J. Hum. Genet. 53 (1993) 598-608
17. Humbert R., Adler D.A., Disteche C.M., Hassett C., Omiecinski C.J., and Furlong C.E. The molecular basis of the human serum paraoxonase activity polymorphism. Nature Genet. 3 (1993) 73-76
18. Brophy V.M., Hastings M.D., Clendenning J.B., McKinstry L.A., and Furlong C.E. Polymorphisms in the human paraoxonase (PON1) promoter. Pharmacogenetics 11 (2001) 77-84
19. Costa L.G., Richter R.J., Li W.-F., Cole T., Guizzetti M., and Furlong C.E. Paraoxonase (PON1) as a biomarker of susceptibility for organophosphate toxicity. Biomarkers 8 (2003) 1-12
20. Yamasaki Y., Sakamoto K., Watada H., Kajimoto Y., and Hori M. The Arg192 isoform of paraoxonase with low sarin-hydrolyzing activity is dominant in the Japanese. Human Genet. 101 (1997) 67-68
21. Smolen A., Eckerson H.W., Gan K.N., Hailat N., and La Du B.N. Characteristics of the genetically determined alloenzymic forms of human serum paraoxonase/arylesterase. Drug Metab. Dispos. 19 (1991) 107-112
22. Eckerson H.W., Wyte C., and La Du B.N. The serum paraoxonase/arylesterase polymorphism. Am. J. Human Genet. 35 (1983) 1126-1138
23. C. A. Broomfield, B. C. Morris, R. Anderson, D. Josse, P. Masson, Kinetics of nerve agent hydrolysis by a human plasma enzyme, CBMTS III Conference Proceedings (2000) No. 72.
24. Kingery A.F., and Allen H.E. The environmental fate of organophosphorus nerve agents: a review. Toxicol. Environ. Chem. 47 (1995) 155-184
25. Munro N.B., Talmage S.S., Griffin G.D., Waters L.C., Watson A.P., King J.P., and Hauschild V. The source, fate, and toxicity of chemical warfare agent degradation products. Environ. Health Perspect. 107 (1999) 933-990
26. Omburo G.A., Kuo J.M., Mullins L.S., and Raushel F.M. Characterization of the zinc binding site of bacterial phosphotriesterase. J. Biol. Chem. 267 (1992) 13278-13283
27. Kataoka M., Tsunoda N., Ohta H., Tsuge K., Takesako H., and Seto Y. Effect of cation-exchange pretreatment of aqueous soil extracts on the gas chromatographic-mass spectrometric determination of nerve agent hydrolysis products after tert-butyldimethylsilylation. J Chromatogr. A 824 (1998) 211-221
28. Kataoka M., Tsuge K., and Seto Y. Comparative examination of various capillary electrophoretic analysis for nerve gas hydrolysis products. Jpn. J. Sci. Technol. Ident. 4 (2000) 67-75
29. Gan K.N., Smolen A., Eckerson H.W., and La Du B.N. Purification of human serum paraoxonase/arylesterase, evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19 (1991) 100-106
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
31. Seto Y., and Kataoka M. Application of capillary electrophoresis to forensic toxicological analysis. Jpn. J. Sci. Technol. Ident. 8 (2003) 1-19
32. Pumera M. Analysis of nerve agents using capillary electrophoresis and laboratory-on-a-chip technology. J. Chromatogr. A 1113 (2006) 5-13
33. Robins W.H., and Wright B.W. Capillary electrophoretic separation of organophosphonic acids using borate esterification and direct UV detection. J. Chromatogr. A 680 (1994) 667-673
34. Rautio M. Recommended Operating Procedures for Sampling and Analysis in the Verification of Chemical Disarmament (1994), The Ministry of Foreign Affair of Finland, Helsinki
35. http://www.safe.nite.go.jp/.
36. Nakanishi M., Takanami Y., Maruyama T., Murata M., Motohashi Y., Nakano S., Uchida K., Maruyama C., Kyotani S., and Tsushima M. The ration of serum paraoxonase/arylesterase activity using an improved assay for arylesterase activity to discriminate PON1R192 from PON1Q192. J. Atherosler. Thromb. 10 (2003) 337-342
37. Itahara T., Suehiro T., Ikeda Y., Inoue M., Nakamura T., Kumon Y., Kawada M., and Hashimoto K. Serum paraoxonase and arylesterase activities in hemodialysis patients. J. Atheroscler. Thromb. 7 (2000) 152-158
38. Ueno T., Shimazaki E., Matsumoto T., Watanabe H., Tsunemi A., Takahashi Y., Mori M., Hamano R., Fujioka T., Soma M., Matsumoto K., and Kanmateuse K. Paraoxonase1 polymorphism Leu-Met55 is associated with cerebral infarction in Japanese population. Med. Sci. Monit. 9 (2003) 260-264
39. Mackness B., Mackness M.I., Arrol S., Turkie W., Julier K., Abuasha B., Miller J.E., Boulton A.J., and Durrington P.N. Serum paraoxonase (PON1) 55 and 192 polymorphism and paraoxonase activity and concentration in non-insulin dependent diabetes mellitus. Atherosclerosis 139 (1998) 341-349
40. Garin M.C., James R.W., Dussoix P., Blanché H., Passa P., Froguel P., and Ruiz J. Paraoxonase polymorphism Met-Leu54 is associated with modified serum concentration of the enzyme. A possible link between the paraoxonase gene and increased risk of cardiovascular disease in diabetes. J. Clin. Invest. 99 (1997) 62-66
41. Mackness B., Mackness M.I., Arrol S., Turkie W., and Durrington P.N. Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon. Br. J. Pharmacol. 112 (1997) 265-268
42. Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 (1934) 658-666
43. Mackness B., Durrington P.N., and Mackness M.I. Human serum paraoxonase. Gen. Pharmac. 31 (1998) 329-336
44. Josse D., Lockridge O., Xie W., Bartels C.F., Schopfer L.M., and Masson P. The active site of human paraoxonase (PON1). J. Appl. Toxicol. 21 (2001) 7-11
45. Dumas D.P., Durst H.D., Landis W.G., Raushel F.M., and Wild J.R. Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta. Arch. Biochem. Biophys. 277 (1990) 155-159
46. Josse D., Xie W., Renault F., Rochu D., Schopfer L.M., Masson P., and Lockridge O. Identification of residue essential for human paraoxonase (PON1) arylesterase/organophosphatase activities. Biochemistry 38 (1999) 2816-2825
47. Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Raveilli R.B.G., McCarthy A., Toker L., Silman I., Sussman J.L., and Tawfik D.S. Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes. Nat. Struct. Mol. Biol. 11 (2004) 412-419
48. Harel M., Brumshtein B., Meged R., Dvir H., Raveilli R.B.G., McCarthy A., Toker L., Silman I., and Sussman J.L. 3-D structure of serum paraoxonase 1 sheds light on its activity, stability, solubility and crystallizability. Arh. Hig. Rada. Toksikol. 58 (2007) 347-353
49. Koepke J., Scharff E.I., Lücke C., Rüterjans H., and Fritzsch G. Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85 Å resolution. Acta Cryst. D 59 (2003) 1744-1754