Improving the ex vivo stability of drug ester compounds in rat and dog serum: Inhibition of the specific esterases and implications on their identity

Journal of Pharmaceutical and Biomedical Analysis

Volumn 51, Issue 3, 2010, Pages 664-678

  Koitka, Matthias ^a   Höchel, Joachim ^b   Gieschen, Hille ^b   Borchert, Hans Hubert ^c  

^a Univ Limoges   (France)

^b BAYER PHARMA AG   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Drospirenone; Mass spectrometry; Methylprednisolone aceponate; Rat and dog serum esterases; Sagopilone

Indexed keywords

ALPHA 2 MACROGLOBULIN; ARYLDIALKYLPHOSPHATASE 1; CARBOXYLESTERASE; CHOLINESTERASE; DROSPIRENONE; ESTER DERIVATIVE; ESTERASE; HYDROLASE INHIBITOR; METHYLPREDNISOLONE ACEPONATE; SAGOPILONE;

AFFINITY CHROMATOGRAPHY; ANIMAL EXPERIMENT; ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; BLOOD SAMPLING; CONTROLLED STUDY; DOG; DRUG BLOOD LEVEL; DRUG DEGRADATION; DRUG EFFICACY; DRUG RESEARCH; DRUG STABILITY; DRUG STRUCTURE; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME PURIFICATION; EX VIVO STUDY; FEMALE; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIQUID CHROMATOGRAPHY; MALE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; RAT; WESTERN BLOTTING;

ANIMALS; CATTLE; CHICKENS; DOGS; DRUG STABILITY; ENZYME INHIBITORS; ESTERASES; ESTERS; FEMALE; HORSES; MALE; PHARMACEUTICAL PREPARATIONS; RATS; RATS, WISTAR; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 70449526714     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2009.09.023     Document Type: Article

References (107)

1. U.S. Department of Health and Human Services, Food and Drug Administration, Guidance for industry, Bioanalytical method validation, 2001.
2. The European Agency for the Evaluation of Medicinal Products, Pharmacokinetic studies in man, Guideline 3CC3a, 1987. Internet: http://www.emea.europa.eu/htms/human/humanguidelines/efficacy.htm (as of June 23rd, 2009).
3. The European Agency for the Evaluation of Medicinal Products, Conduct of pharmacokinetic studies in animals, Guideline 7AE3a, 1992. Internet: http://ec.europa.eu/enterprise/pharmaceuticals/eudralex/vol7_en.htm#7a (as of June 23rd, 2009).
4. The European Agency for the Evaluation of Medicinal Products, Committee for Veterinary Medicinal Products, Guidelines for the conduct of pharmacokinetic studies in target animal species, EMEA/CVMP/133/99, London, 2000.
5. Tokumura T., Muraoka A., Masutomi T., and Machida Y. Stability of spironolactone in rat plasma: strict temperature control of blood an plasma samples is required in rat pharmacokinetic studies. Biol. Pharm. Bull. 28 (2005) 1126-1128
6. Zeng J., Onthank D., Crane P., Unger S., Zheng N., Pasas-Farmer S., and Arnold M. Simultaneous determination of a selective adenosine 2A agonist, BMS-068645, and its acid metabolite in human plasma by liquid chromatography-tandem mass spectrometry-evaluation of the esterase inhibitor, diisopropyl fluorophosphate, in the stabilization of a labile ester-containing drug. J. Chromatogr. B 852 (2007) 77-84
7. Li B., Sedlacek M., Manoharan I., Boopathy R., Duysen E.G., Masson P., and Lockridge O. Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem. Pharmacol. 70 (2005) 1673-1684
8. Williams F.M. Serum enzymes of drug metabolism. Pharmacol. Ther. 34 (1987) 99-109
9. Testa B., and Mayer J.M. Hydrolysis in Drug and Prodrug Metabolism. Chemistry, Biochemistry, and Enzymology (2003), Verlag Helvetica Chemica Acta, Zürich
10. Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), See http://www.chem.qmul.ac.uk/iubmb/enzyme for continuously updated versions.
11. Brimijoin S., and Hammond P. Butyrylcholinesterase in human brain and acetylcholinesterase in human plasma: trace enzymes measured by two-site immunoassay. J. Neurochem. 51 (1988) 1227-1231
12. Boeck A.T., Schopfer L.M., and Lockridge O. DNA sequence of butyrylcholinesterase from the rat: expression of the protein and characterization of the properties of rat butyrylcholinesterase. Biochem. Pharmacol. 63 (2002) 2101-2110
13. Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Ravelli 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
14. Liederer B.M., and Borchardt R.T. Enzymes involved in the bioconversion of ester-based prodrugs. J. Pharm. Sci. 95 (2006) 1177-1195
15. Lawrence S.H., Melnick P.J., and Weimer H.E. A species comparison of serum proteins and enzymes by starch gel electrophoresis. Proc. Soc. Exp. Biol. Med. 105 (1960) 572-575
16. Augustinsson K. Electrophoresis studies on blood plasma esterases. I: Mammalian plasmata. Acta Chem. Scand. 13 (1959) 571-592
17. Liederer B.M., and Borchardt R.T. Stability of oxymethyl-modified coumarinic acid cyclic prodrugs of diastereomeric opioid peptides in biological media from various animal species including human. J. Pharm. Sci. 94 (2005) 2198-2206
18. Minagawa T., Kohno Y., Suwa T., and Tsuji A. Species differences in hydrolysis of isocarbacyclin methyl ester (TEI-9090) by blood esterases. Biochem. Pharmacol. 49 (1995) 1361-1365
19. Tsuji T., Kaneda N., Kado K., Yokokura T., Yoshimoto T., and Tsuru D. CPT-11 converting enzyme from rat serum: purification and some properties. J. Pharmacobiodyn. 14 (1991) 341-349
20. Senter P.D., Marquardt H., Thomas B.A., Hammock B.D., Frank I.S., and Svensson H.P. The role of rat serum carboxylesterase in the activation of paclitaxel and camptothecin prodrugs. Cancer Res. 56 (1996) 1471-1474
21. Crow J.A., Borazjani A., Potter P.M., and Ross M.K. Hydrolysis of pyrethroids by human and rat tissues: examination of intestinal, liver and serum carboxylesterases. Toxicol. Appl. Pharmacol. 221 (2007) 1-12
22. Quon C.Y., and Stampfli H.F. Biochemical properties of blood esmolol esterase. Drug Metab. Dispos. 13 (1985) 420-424
23. Quon C.Y., Mai K., Patil G., and Stampfli H.F. Species differences in the stereoselective hydrolysis of esmolol by blood esterases. Drug Metab. Dispos. 16 (1988) 425-428
24. Quon C.Y., and Stampfli H.F. Biochemical characterization of flestolol esterase. Res. Commun. Chem. Pathol. Pharmacol. 81 (1993) 309-322
25. Reidenberg M.M. The procaine esterase activity of serum from different mammalian species. Proc. Soc. Exp. Biol. Med. 140 (1972) 1059-1061
26. Okuyama Y., Momota K., and Morino A. Pharmacokinetics of prulifloxacin. 1st communication: absorption, distribution and excretion in rats, dogs and monkeys after a single administration. Drug Res. 47 (1997) 276-284
27. Augustinsson K. Electrophoretic separation and classification of blood plasma esterases. Nature 181 (1958) 1786-1789
28. Augustinsson K. Multiple forms of esterase in vertebrate blood plasma. Ann. N. Y. Acad. Sci. 94 (1961) 844-860
29. Ecobichon D. Characterization of the esterases of canine serum. Can. J. Biochem. 48 (1970) 1359-1367
30. Tsujita T., and Okuda H. Carboxylesterases in rat and human sera and their relationship to serum aryl acylamidases and cholinesterases. Eur. J. Biochem. 133 (1983) 215-220
31. Vincent D., Perrier H., and Rouzioux J.M. Sur les isoenzymes de la cholinestérase sérique chez quelques espèces animales. C.R. Séances Soc. Biol. Fil. 164 (1970) 1767-1769 (in French)
32. Hoffmann W.E., Solter P.F., and Wilson B.W. Clinical enzymology. In: Loeb W.F., and Quimby F.W. (Eds). The Clinical Chemistry of Laboratory Animals. second ed. (1999), Taylor & Francis, Philadelphia 399-454
33. Redinbo M.R., and Potter P.M. Mammalian carboxylesterases: from drug targets to protein therapeutics. Drug Discov. Today 10 (2005) 313-325
34. Lindegardh N., Davies G.R., Hien T.T., Farrar J., Singhasivanon P., Day N.P.J., and White N.J. Importance of collection tube during clinical studies of oseltamivir. Antimicrob. Agents Chemother. 51 (2007) 1835-1836
35. Klar U., Buchmann B., Schwede W., Skuballa W., Hoffmann J., and Lichtner R.B. Total synthesis and antitumor activity of ZK-EPO: the first fully synthetic epothilone in clinical development. Angew. Chem. Int. Ed. 45 (2006) 7942-7948
36. Krattenmacher R. Drospirenone: pharmacology and pharmacokinetics of a unique pregestogen. Contraception 62 (2000) 29-38
37. Ruzicka T. Methylprednisolone aceponate in eczema and other inflammatory skin disorders - a clinical update. Int. J. Clin. Pract. 60 (2006) 85-92
38. Koitka M., Höchel J., Obst D., Rottmann A., Gieschen H., and Borchert H.H. Determination of rat serum esterase activities by an HPLC method using S-acetylthiocholine iodide and p-nitrophenyl acetate. Anal. Biochem. 381 (2008) 113-122
39. Scopes R.K. Protein Purification. Principles and Practice. third ed. (1994), Springer, New York
40. Gan K.N., Smolen A., Eckerson H.W., and La Du B.N. Purification of human serum paraoxonase/arylesterase. Drug Metab. Dispos. 19 (1991) 100-106
41. Smith P.K., Krohn R.I., Hermanson G.T., Mallia A.K., Gartner F.H., Provenzano M.D., Fujimoto E.K., Goeke N.M., Olson B.J., and Klenk D.C. Measurement of protein using bicinchoninic acid. Anal. Biochem. 150 (1985) 76-85
42. Pierce Biotechnology, Micro BCA Protein Assay Kit, Instructions, Rockford, 2006.
43. S.R. Gallagher, One-dimensional electrophoresis using nondenaturing conditions, Current Protocols in Protein Science, Unit 10.3, 1995, doi:10.1002/0471140864.ps1003s00.
44. Matrix Science, Internet: http://www.matrixscience.com/cgi/master_results.pl?file=..%2Fdata%2FF981 122.dat&REP TYPE=concise&_sigthreshold=0.05&REPORT=AUTO (as of June 21st, 2009).
45. Invitrogen, iBlot Dry Blotting System, User Manual, Carlsbad, 2007.
46. Powers J.C., and Harper J.W. Inhibitors of serine proteinases. In: Barrett A.J., and Salvesen G. (Eds). Proteinase Inhibitors (1986), Elsevier, Amsterdam 55-152
47. Mintz G.R. An irreversible serine protease inhibitor. BioPharm 6 (1993) 34-38
48. Pond A.L., Coyne C.P., Chambers H.W., and Chambers J.E. Identification and isolation of two rat serum proteins with A-esterase activity toward paraoxon and chlorpyrifos-oxon. Biochem. Pharmacol. 52 (1996) 363-369
49. Jewell C., Ackermann C., Payne N.A., Fate G., Voorman R., and Williams F.M. Specificity of procaine and ester hydrolysis by human, minipig, and rat skin and liver. Drug Metab. Dispos. 35 (2007) 2015-2022
50. Kuo C.L., and La Du B.N. Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity. Drug Metab. Dispos. 26 (1998) 653-660
51. Fujita Y., Yaegashi T., Sawada S., Oyama H., Yoshimoto T., and Tsuru D. Partial purification and characterization of an esterase acting on the anticancer pro-drugs, 7-ethylcamptothecin derivatives. Biol. Pharm. Bull. 18 (1995) 648-652
52. 2+-binding site in human serum butyrylcholinesterase. Biochem. J. 315 (1996) 127-131
53. Zollner H. Handbook of Enzyme Inhibitors. third ed. (1999), Wiley-VCH, Weinheim
54. Barrett A.J. Introduction to the history and classification of tissue proteinases. In: Barrett A.J. (Ed). Proteinases in Mammalian Cells and Tissues (1977), Elsevier/North-Holland Biomedical Press, Amsterdam 1-55
55. 3+: comparison of the effects of metal ions on cholinesterases. Comp. Biochem. Physiol. Part C 122 (1999) 181-190
56. Borgono C.A., Michael I.P., Shaw J.L.V., Luo L.Y., Gosh M.C., Soosaipillai A., Grass L., Katsaros D., and Diamandis E.P. Expression and functional characterization of the cancer-related serine protease, human tissue kallikrein 14. J. Biol. Chem. 282 (2007) 2405-2422
57. 2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor. Protein Sci. 9 (2000) 859-866
58. 2+ reactivates the inhibited enzyme. Int. J. Biochem. 25 (1993) 1115-1120
59. Cengiz D., Cokugras A.N., Kilinc K., and Tezcan E.F. Histidine modification of human serum butyrylcholinesterase. Biochem. Mol. Med. 61 (1997) 52-57
60. Oboh O.T., and Lamago N.S. Liver prenylated methylated protein methyl esterase is the same enzyme as Sus scrofa carboxylesterase. J. Biochem. Mol. Toxicol. 22 (2008) 51-62
61. Richter D., and Croft P.G. Blood esterases. Biochem. J. 36 (1942) 746-757
62. Mukerjee P., and Mysels K.J. Critical micelle concentration of aqueous surfactant systems. Nat. Stand. Ref. Data Ser., Nat. Bur. Stand. (U.S.) 36 (1971) Washington
63. Khersonsky O., and Tawfik D.S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44 (2005) 6371-6382
64. Furlong C.E., Richter R.E., Chapline C., and Crabb J.W. Purification of rabbit and human serum paraoxonase. Biochemistry 30 (1991) 10133-10140
65. Huang Y.S., Woods L., and Sultatos L.G. Solubilization and purification of A-esterase from mouse hepatic microsomes. Biochem. Pharmacol. 48 (1994) 1273-1280
66. Gil F., Gonzalvo M.C., Hernandez A.F., Villanueva E., and Pla A. Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver. Biochem. Pharmacol. 48 (1994) 1559-1568
67. Billecke S., Draganov D., Counsell R., Stetson P., Watson C., Hsu C., and La Du B.N. Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters. Drug Metab. Dispos. 28 (2000) 1335-1342
68. Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., and La Du B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46 (2005) 1239-1247
69. George S.T., and Balasubramanian A.S. The aryl acylamidases and their relationship to cholinesterases in human serum, erythrocyte and liver. Eur. J. Biochem. 121 (1981) 177-186
70. Rao R.V., and Balasubramanian A.S. Localization of the peptidase activity of human serum butyrylcholinesterase in a -50-kDa fragment obtained by limited α-chymotrypsin digestion. Eur. J. Biochem. 188 (1990) 637-643
71. Hashinotsume M., Higashino K., Hada T., and Yamamura Y. Purification and enzymatic properties of rat serum carboxylesterase. J. Biochem. 84 (1978) 1325-1333
72. Yan B., Yang D., Bullock P., and Parkinson A. Rat serum carboxylesterase. Cloning, expression, regulation, and evidence of secretion from rat liver. J. Biol. Chem. 270 (1995) 19128-19134
73. Van Lith H.A., Haller M., Van Hoof I.J.M., Van Der Wouw M.J.A., Van Zutphen B.F.M., and Beynen A.C. Characterization of rat plasma esterase ES-1A concerning its molecular and catalytic properties. Arch. Biochem. Biophys. 301 (1993) 265-274
74. Hirose T., Morita A., Yamada M., Nikaido H., Hayakawa J., and Nikaido O. Selective purification of sex-influenced esterase from rat serum by immunoaffinity chromatographies. Eur. J. Biochem. 189 (1990) 431-435
75. Darvesh S., Kumar R., Roberts S., Walsh R., and Martin E. Butyrylcholinesterase-mediated enhancement of the enzymatic activity of trypsin. Cell. Mol. Neurobiol. 21 (2001) 285-296
76. Checler F., Grassi J., and Vincent J.P. Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities. J. Neurochem. 62 (1994) 756-763
77. Alexson S.E.H., Finlay T.H., Hellman U., Svensson L.T., Diczfalusy U., and Eggertsen G. Molecular cloning and identification of a rat carboxylesterase expressed in the liver. J. Biol. Chem. 269 (1994) 17118-17124
78. Tsujita T., Nagai K., and Okuda H. Purification and properties of human serum esterase. Biochim. Biophys. Acta 570 (1979) 88-95
79. Satoh T., and Hosokawa M. The mammalian carboxylesterases: from molecules to functions. Ann. Rev. Pharmacol. Toxicol. 38 (1998) 257-288
80. Furihata T., and Hosokawa M. Dexamethasone-induced methylprednisolone hemisuccinate hydrolase: its identification as a member of the rat carboxylesterase 2 family and its unique existence in plasma. Biochem. Pharmacol. 69 (2005) 1287-1297
81. Rodrigo L., Gil F., Hernandez A.F., Lopez O., and Pla A. Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties. Biochem. J. 376 (2003) 261-268
82. Myers C., Lockridge O., and La Du B.N. Hydrolysis of methylprednisolone acetate by human serum cholinesterase. Drug Metab. Dispos. 10 (1982) 279-280
83. Salvesen G.S., and Nagase H. Inhibition of proteolytic enzymes. In: Beynon R., and Bond J.S. (Eds). Proteolytic Enzymes. second ed. (2001), Oxford University Press, Oxford 105-130
84. 2-Macroglobulin and related thiol ester plasma proteins. In: Putnam F. (Ed). The Plasma Proteins, vol. V. second ed. (1987), Academic Press, Orlando 191-291
85. Andersson M., Jönsson U., and Olsson A. A slow form of alpha-2-macroglobulin in diseased and healthy dogs. J. Comp. Pathol. 127 (2002) 37-44
86. Travis J., and Pannell R. Selective removal of albumin from plasma by affinity chromatography. Clin. Chim. Acta 49 (1973) 49-52
87. Naval J., Calvo M., Lampreave F., and Pineiro A. Interactions of different albumins and animal sera with insolubilized Cibacron Blue. Evaluation of apparent affinity constants. Comp. Biochem. Physiol. 71B (1982) 403-407
88. Cimasoni G. Inhibition of cholinesterases by fluoride in vitro. Biochem. J. 99 (1966) 133-137
89. Montenegro M.F., Moral-Naranjo M.T., Páez de la Cadena M., Campoy F.J., Muñoz-Delgado E., and Vidal C.J. The level of aryl acylamidase activity displayed by human butyrylcholinesterase depends on its molecular distribution. Chem. Biol. Interact. 175 (2008) 336-339
90. Rao R.V., and Balasubramanian A.S. Isolation of a galactose-free 20-kDa fragment exhibiting butyrylcholine esterase and aryl acylamidase activity from human serum butyrylcholine esterase by limited α-chymotrypsin digestion. Eur. J. Biochem. 179 (1989) 639-644
91. Boopathy R., and Balasubramanian A.S. Chemical modification of the bifunctional human serum pseudocholinesterase. Eur. J. Biochem. 151 (1985) 351-360
92. Darvesh S., McDonald R.S., Darvesh K.V., Mataija D., Mothana S., Cook H., Carneiro K.M., Richard N., Walsh R., and Martin E. On the active site for hydrolysis of aryl amides and choline esters by human cholinesterases. Bioorg. Med. Chem. 14 (2006) 4586-4599
93. Golmanesh L., Mehrani H., and Tabei M. Simple procedures for purification and stabilization of human serum paraoxonase-1. J. Biochem. Biophys. Methods 70 (2008) 1037-1042
94. Kuo C.L., and La Du B.N. Comparison of purified human and rabbit paraoxonases. Drug Metab. Dispos. 23 (1995) 935-944
95. Draganov D.I., and La Du B.N. Pharmacogenetics of paraoxonases: a brief review. Naunyn-Schmiedeberg's Arch. Pharmacol. 369 (2004) 78-88
96. Motta S., Letellier C., Ropert M., Motta C., and Thiébault J.J. Protecting effect of vitamin E supplementation on submaximal exercise-induced oxidative stress in sedentary dogs as assessed by erythrocyte membrane fluidity and paraoxonase-1 activity. Vet. J. 181 (2009) 288-295
97. Leone C.A., and Anthony R.L. Serum esterases among registered breeds of dogs as revealed by immunoelectrophoretic comparisons. Comp. Biochem. Physiol. 18 (1966) 359-368
98. Primo-Parmo S.L., Sorenson R.C., Teiber J., and La Du B.N. The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics 33 (1996) 498-507
99. Connelly P.W., Maguire G.F., Picardo C.M., Teiber J.F., and Draganov D. Development of an immunoblot assay with infrared fluorescence to quantify paraoxonase 1 in serum and plasma. J. Lipid Res. 49 (2008) 245-250
100. Thomas-Moya E., Gianotti M., Llado I., and Proenza A.M. Effects of caloric restriction and gender on rat serum paraoxonase 1 activity. J. Nutr. Biochem. 17 (2006) 197-203
101. Rousseau G. Medium ring lactones. Tetrahedron 51 (1995) 2777-2849
102. Fishbein W.N., and Bessman S.P. Purification and properties of an enzyme in human blood and rat liver microsomes catalyzing the formation and hydrolysis of γ-lactones. II: Metal ion effects, kinetics, and equilibria. J. Biol. Chem. 241 (1966) 4842-4847
103. Khersonsky O., and Tawfik D.S. The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases. J. Biol. Chem. 281 (2006) 7649-7656
104. McCracken N.W., Blain P.G., and Williams F.M. Nature and role of xenobiotic metabolizing esterases in rat liver, lung, skin and blood. Biochem. Pharmacol. 45 (1993) 31-36
105. Teiber J.F., Billecke S.S., La Du B.N., and Draganov D.I. Estrogen esters as substrates for human paraoxonases. Arch. Biochem. Biophys. 461 (2007) 24-29
106. Marathe G.K., Zimmerman G.A., and McIntyre T.M. Platelet-activating factor acetylhydrolase, and not paraoxonase-1, is the oxidized phospholipid hydrolase of high density lipoprotein particles. J. Biol. Chem. 278 (2003) 3937-3947
107. Kriska T., Marathe G.K., Schmidt J.C., McIntyre T.M., and Girotti A.W. Phospholipase action of platelet-activating factor acetylhydrolase, but not paraoxonase-1, on long fatty acyl chain phospholipid hydroperoxides. J. Biol. Chem. 282 (2007) 100-108