| Name | Paraoxonase |
|---|---|
| Synonyms | A esterase 1; Aromatic esterase 1; Arylesterase; ESA; Esterase A; K 45; PON; PON 1… |
| Name | chlorpyrifos |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9745924 | Furlong CE, Li WF, Costa LG, Richter RJ, Shih DM, Lusis AJ: Genetically determined susceptibility to organophosphorus insecticides and nerve agents: developing a mouse model for the human PON1 polymorphism. Neurotoxicology. 1998 Aug-Oct;19(4-5):645-50. Do these interindividual differences in rates of substrate hydrolysis by PON1 reflect an individual's sensitivity or resistance to OP compounds processed through the P450/PON1 pathway? Injection of purified PON1 into mice clearly demonstrates the protective effect of having high serum levels of PON1 against toxicity by chlorpyrifos oxon or chlorpyrifos. |
45(0,1,2,10) | Details |
| 9685159 | Shih DM, Gu L, Xia YR, Navab M, Li WF, Hama S, Castellani LW, Furlong CE, Costa LG, Fogelman AM, Lusis AJ: Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature. 1998 Jul 16;394(6690):284-7. Compared with their wild-type littermates, PON1-deficient mice were extremely sensitive to the toxic effects of chlorpyrifos oxon, the activated form of chlorpyrifos, and were more sensitive to chlorpyrifos itself. |
42(0,1,2,7) | Details |
| 12519632 | Costa LG, Richter RJ, Li WF, Cole T, Guizzetti M, Furlong CE: Paraoxonase (PON 1) as a biomarker of susceptibility for organophosphate toxicity. Biomarkers. 2003 Jan-Feb;8(1):1-12. Paraoxonase (PON1) is an A-esterase capable of hydrolysing the active metabolites (oxons) of a number of organophosphorus (OP) insecticides such as parathion, diazinon and chlorpyrifos. |
38(0,1,1,8) | Details |
| 10602389 | Sams C, Mason HJ: Detoxification of organophosphates by A-esterases in human serum. Hum Exp Toxicol. 1999 Nov;18(11):653-8. Specific A-esterase activity to each OP substrate was measured in the serum of 100 individuals using established spectrophotometric methods for paraoxonase and chlorpyrifos-oxonase and a novel assay for malaoxonase activity. 3. |
31(0,1,1,1) | Details |
| 11099640 | Karanth S, Pope C: Carboxylesterase and A-esterase activities during maturation and aging: relationship to the toxicity of chlorpyrifos and parathion in rats. Toxicol Sci. 2000 Dec;58(2):282-9. AEs (e.g., chlorpyrifos oxonase and paraoxonase) catalytically inactivate while CEs stoichiometrically eliminate OP anticholinesterases. |
31(0,1,1,1) | Details |
| 11022865 | Furlong CE, Li WF, Brophy VH, Jarvik GP, Richter RJ, Shih DM, Lusis AJ, Costa LG: The PON1 gene and detoxication. Neurotoxicology. 2000 Aug;21(4):581-7. Injected PON1 protected against paraoxon toxicity in rats and chlorpyrifos oxon toxicity in mice. |
30(0,0,4,10) | Details |
| 17132760 | Mutch E, Daly AK, Williams FM: The Relationship between PON1 phenotype and PON1-192 genotype in detoxification of three oxons by human liver. Drug Metab Dispos. 2007 Feb;35(2):315-20. Epub 2006 Nov 28. The aims of this study were to define the influence of PON1-192 genotype and phenotype on the capacity of human liver microsomes (n = 27) to detoxify the oxons diazoxon, chlorpyrifos-oxon, and paraoxon. |
21(0,0,3,6) | Details |
| 10421480 | Costa LG, Li WF, Richter RJ, Shih DM, Lusis A, Furlong CE: The role of paraoxonase (PON1) in the detoxication of organophosphates and its human polymorphism. Chem Biol Interact. 1999 May 14;119-120:429-38. Furthermore, protection by PON1 is also provided toward the parent compound chlorpyrifos. |
18(0,0,1,13) | Details |
| 7539166 | Li WF, Furlong CE, Costa LG: Paraoxonase protects against chlorpyrifos toxicity in mice. Toxicol Lett. 1995 Apr;76(3):219-26. |
18(0,0,2,8) | Details |
| 7693961 | Li WF, Costa LG, Furlong CE: Serum paraoxonase status: a major factor in determining resistance to organophosphates. J Toxicol Environ Health. 1993 Oct-Nov;40(2-3):337-46. Rabbit paraoxonase hydrolyzes chlorpyrifos-oxon with a much higher turnover number than does rat paraoxonase, resulting in a very high resistance of rabbits to chlorpyrifos toxicity. |
18(0,0,2,8) | Details |
| 17936934 | Furlong CE: Genetic variability in the cytochrome P450-paraoxonase 1 (PON1) pathway for detoxication of organophosphorus compounds. J Biochem Mol Toxicol. 2007;21(4):197-205. The detoxication of the oxon forms of diazinon and chlorpyrifos is achieved by hydrolysis to the respective aromatic and diethyl phosphates primarily by paraoxonase 1 (PON1), a plasma enzyme tightly associated with high-density lipoprotein particles and also found in liver. |
17(0,0,2,7) | Details |
| 10794389 | Furlong CE, Li WF, Richter RJ, Shih DM, Lusis AJ, Alleva E, Costa LG: Genetic and temporal determinants of pesticide sensitivity: role of paraoxonase (PON1). Neurotoxicology. 2000 Feb-Apr;21(1-2):91-100. Phenylacetate is hydrolyzed at approximately the same rate by both PON1 isoforms and chlorpyrifos oxon (CPO) slightly faster by the PON1R192 isoform. |
16(0,0,1,11) | Details |
| 16835048 | Holland N, Furlong C, Bastaki M, Richter R, Bradman A, Huen K, Beckman K, Eskenazi B: Paraoxonase polymorphisms, haplotypes, and enzyme activity in Latino mothers and newborns. Environ Health Perspect. 2006 Jul;114(7):985-91. The goals of this study were to examine in the Center for Health Assessment of Mothers and Children of Salinas (CHAMACOS) birth cohort of Latina mothers and their newborns living in the Salinas Valley, California, the frequencies of five PON1 polymorphisms in the coding region (192QR and 55LM) and the promoter region (-162AG, -909CG, and -108CT) and to determine their associations with PON1 plasma levels [phenylacetate arylesterase (AREase) ] and enzyme activities of paraoxonase (POase) and chlorpyrifos oxonase (CPOase) . |
15(0,0,1,10) | Details |
| 15037822 | Nakanishi M, Takanami Y, Maruyama T, Murata M, Motohashi Y, Nakano S, Uchida K, Maruyama C, Kyotani S, Tsushima M: The ratio of serum paraoxonase/arylesterase activity using an improved assay for arylesterase activity to discriminate PON1 (R192) from PON1 (Q192). J Atheroscler Thromb. 2003;10(6):337-42. The PON1 (Q192) isoform has a higher rate of in vitro hydrolysis of diazoxon, sarin, and soman, whereas the PON1 (R192) isoform has higher activity for the hydrolysis of paraoxon and chlorpyrifos oxon. |
14(0,0,1,9) | Details |
| 20045427 | Huen K, Harley K, Bradman A, Eskenazi B, Holland N: Longitudinal changes in PON1 enzymatic activities in Mexican-American mothers and children with different genotypes and haplotypes. Toxicol Appl Pharmacol. 2010 Apr 15;244(2):181-9. Epub 2010 Jan 4. In non-pregnant mothers, PON1 polymorphisms and haplotypes accounted for almost 2-fold more variation of arylesterase (AREase) and chlorpyrifos-oxonase (CPOase) activity than in mothers at delivery. |
15(0,0,1,10) | Details |
| 10898114 | Brophy VH, Jarvik GP, Richter RJ, Rozek LS, Schellenberg GD, Furlong CE: Analysis of paraoxonase (PON1) L55M status requires both genotype and phenotype. Pharmacogenetics. 2000 Jul;10(5):453-60. PON1 also hydrolyses the bioactive oxon forms of organophosphorus pesticides such as parathion, diazinon and chlorpyrifos. |
15(0,0,1,10) | Details |
| 19907334 | Manthripragada AD, Costello S, Cockburn MG, Bronstein JM, Ritz B: Paraoxonase 1, agricultural organophosphate exposure, and Parkinson disease. Epidemiology. 2010 Jan;21(1):87-94. METHODS: We examined associations between Parkinson disease and the organophosphates diazinon, chlorpyrifos, and parathion, and the influence of a functional polymorphism at position 55 in the coding region of the PON1 gene (PON1-55). |
15(0,0,2,5) | Details |
| 16495777 | Furlong CE, Holland N, Richter RJ, Bradman A, Ho A, Eskenazi B: PON1 status of farmworker mothers and children as a predictor of organophosphate sensitivity. Pharmacogenet Genomics. 2006 Mar;16(3):183-90. Average PON1 levels in newborns were comparable with reported hPON1 levels in transgenic mice expressing human PON1Q192 or PON1R192, allowing for prediction of relative sensitivity to chlorpyrifos oxon (CPO) and DZO. |
14(0,0,1,9) | Details |
| 19146843 | Huen K, Richter R, Furlong C, Eskenazi B, Holland N: Validation of PON1 enzyme activity assays for longitudinal studies. Clin Chim Acta. 2009 Apr;402(1-2):67-74. Epub 2008 Dec 24. However, after 7 y, arylesterase, paraoxonase, and chlorpyrifos-oxonase activities decreased more noticeably. |
13(0,0,1,8) | Details |
| 19071155 | Richter RJ, Jarvik GP, Furlong CE: Paraoxonase 1 (PON1) status and substrate hydrolysis. Toxicol Appl Pharmacol. 2009 Feb 15;235(1):1-9. Epub 2008 Nov 13. On the other hand, PON1 (R192) is significantly more efficient in hydrolyzing chlorpyrifos oxon (CPO) than PON1 (Q192) and provides better protection against CPO exposure. |
13(0,0,1,8) | Details |
| 19922610 | Gaidukov L, Bar D, Yacobson S, Naftali E, Kaufman O, Tabakman R, Tawfik DS, Levy-Nissenbaum E: In vivo administration of BL-3050: highly stable engineered PON1-HDL complexes. BMC Clin Pharmacol. 2009 Nov 17;9:18. The in vivo efficacy of recombinant PON1 and BL-3050 were tested with an animal model of chlorpyrifos-oxon poisoning. |
13(0,0,1,8) | Details |
| 11191881 | Li WF, Costa LG, Richter RJ, Hagen T, Shih DM, Tward A, Lusis AJ, Furlong CE: Catalytic efficiency determines the in-vivo efficacy of PON1 for detoxifying organophosphorus compounds. Pharmacogenetics. 2000 Dec;10(9):767-79. In-vivo analysis, where PON1-knockout mice received the same amount of either PON1 (192) isoform via intraperitoneal (i.p.) injection 4 h prior to exposure, showed that both isoforms provided a similar degree of protection against diazoxon, while PON1R192 conferred better protection against chlorpyrifos-oxon than PON1Q192. |
12(0,0,1,7) | Details |
| 17129656 | Amitai G, Adani R, Yacov G, Yishay S, Teitlboim S, Tveria L, Limanovich O, Kushnir M, Meshulam H: Asymmetric fluorogenic organophosphates for the development of active organophosphate hydrolases with reversed stereoselectivity. Toxicology. 2007 Apr 20;233(1-3):187-98. Epub 2006 Oct 13. We have previously identified three key positions in PON1 that affect OP hydrolysis: Leu69, Val346 and His115, that significantly enhance the hydrolysis of cyclosarin (GF), soman, chlorpyrifos-oxon (ChPo), O-isopropyl-O-(p-nitrophenyl) methylphosphonate (IMP-pNP) and diisopropyl fluorophosphate (DFP). |
12(0,0,1,7) | Details |
| 15707963 | Fu AL, Wang YX, Sun MJ: Naked DNA prevents soman intoxication. Biochem Biophys Res Commun. 2005 Mar 25;328(4):901-5. Paraoxonase (Q isoenzyme, PON1) can effectively hydrolyze chlorpyrifos-oxon (CPO), soman, sarin, and other organophosphates. |
11(0,0,1,6) | Details |
| 16112327 | Furlong CE, Cole TB, Jarvik GP, Pettan-Brewer C, Geiss GK, Richter RJ, Shih DM, Tward AD, Lusis AJ, Costa LG: Role of paraoxonase (PON1) status in pesticide sensitivity: genetic and temporal determinants. Neurotoxicology. 2005 Aug;26(4):651-9. PON1 knockout (PON1 (-/-)) and wild-type mice were exposed chronically (PN4 to PN21) to low levels of chlorpyrifos oxon (CPO). |
11(0,0,1,6) | Details |
| 16640555 | Amitai G, Gaidukov L, Adani R, Yishay S, Yacov G, Kushnir M, Teitlboim S, Lindenbaum M, Bel P, Khersonsky O, Tawfik DS, Meshulam H: Enhanced stereoselective hydrolysis of toxic organophosphates by directly evolved variants of mammalian serum paraoxonase. FEBS J. 2006 May;273(9):1906-19. Subsequently, nine directly evolved PON1 variants, selected for increased hydrolytic rates with a fluorogenic diethylphosphate ester, were tested for detoxification of cyclosarin, soman, O-isopropyl-O-(p-nitrophenyl) methyl phosphonate (IMP-pNP), DFP, and chlorpyrifos-oxon (ChPo). |
11(0,0,1,6) | Details |
| 16007003 | Cole TB, Walter BJ, Shih DM, Tward AD, Lusis AJ, Timchalk C, Richter RJ, Costa LG, Furlong CE: Toxicity of chlorpyrifos and chlorpyrifos oxon in a transgenic mouse model of the human paraoxonase (PON1) Q192R polymorphism. Pharmacogenet Genomics. 2005 Aug;15(8):589-98. |
10(0,0,1,5) | Details |
| 18577432 | Farid AS, Horii Y: Gastrointestinal nematode infection increases organophosphate toxicity in rats. Toxicol Lett. 2008 Jul 30;180(1):33-7. Epub 2008 Jun 3. In the present study we investigated the effects of decreased serum PON1 activity due to N. brasiliensis infection on acute toxicity induced by chlorpyrifos oxon (CPO) and paraoxon (PO) in rats. |
10(0,0,1,5) | Details |
| 8896566 | Davies HG, Richter RJ, Keifer M, Broomfield CA, Sowalla J, Furlong CE: The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat Genet. 1996 Nov;14(3):334-6. In 1990, there were 1.36 million kg of chlorpyrifos, 4.67 million kg of diazinon and 1.23 million kg of ethyl parathion manufactured in the USA (data supplied by the USEPA). |
9(0,0,0,9) | Details |
| 20221870 | Cole TB, Jansen K, Park S, Li WF, Furlong CE, Costa LG: The Toxicity of Mixtures of Specific Organophosphate Compounds is Modulated by Paraoxonase 1 Status. Adv Exp Med Biol. 2010;660:47-60. Chlorpyrifos oxon (CPO), diazoxon (DZO), and paraoxon (PO) are potent inhibitors of CaE, both in vitro and in vivo. |
9(0,0,0,9) | Details |
| 18597495 | Sogorb MA, Garcia-Arguelles S, Carrera V, Vilanova E: Serum albumin is as efficient as paraxonase in the detoxication of paraoxon at toxicologically relevant concentrations. Chem Res Toxicol. 2008 Aug;21(8):1524-9. Epub 2008 Jul 3. However, paraoxonase activity associated with lipoprotein was more effective than paraoxonase activity associated with albumin at toxicologically relevant chlorpyrifos-oxon concentrations. |
8(0,0,1,3) | Details |
| 20183530 | Ginsberg G, Neafsey P, Hattis D, Guyton KZ, Johns DO, Sonawane B: Genetic polymorphism in paraoxonase 1 (PON1): Population distribution of PON1 activity. J Toxicol Environ Health B Crit Rev. 2009;12(5-6):473-507. Detailed kinetic studies and population studies found that the *192Q (wild type) allele is more active toward some substrates (such as sarin, soman, and diazoxon) and less active toward others (such as paraoxon or chlorpyrifos) relative to the variant *192R allele. |
8(0,0,0,8) | Details |
| 12243863 | Timchalk C, Kousba A, Poet TS: Monte Carlo analysis of the human chlorpyrifos-oxonase (PON1) polymorphism using a physiologically based pharmacokinetic and pharmacodynamic (PBPK/PD) model. Toxicol Lett. 2002 Sep 5;135(1-2):51-9. |
7(0,0,1,2) | Details |
| 19371602 | Jansen KL, Cole TB, Park SS, Furlong CE, Costa LG: Paraoxonase 1 (PON1) modulates the toxicity of mixed organophosphorus compounds. Toxicol Appl Pharmacol. 2009 Apr 15;236(2):142-53. Epub 2009 Feb 9. Chlorpyrifos oxon (CPO), diazoxon (DZO), and paraoxon (PO) are potent inhibitors of carboxylesterases (CaE). |
7(0,0,0,7) | Details |
| 9732404 | Pond AL, Chambers HW, Coyne CP, Chambers JE: Purification of two rat hepatic proteins with A-esterase activity toward chlorpyrifos-oxon and paraoxon. J Pharmacol Exp Ther. 1998 Sep;286(3):1404-11. The protein hydrolyzed chlorpyrifos-oxon and paraoxon, suggesting that arylesterase and A-esterase activities are attributable to the same liver protein (s). |
6(0,0,1,1) | Details |
| 16915393 | Lee CH, Kamijima M, Kim H, Shibata E, Ueyama J, Suzuki T, Takagi K, Saito I, Gotoh M, Hibi H, Naito H, Nakajima T: levels in human leukocyte and urine according to exposure to organophosphorus pesticides and paraoxonase 1 genotype. Int Arch Occup Environ Health. 2007 Jan;80(3):217-27. Epub 2006 Aug 17. Sprayers were primarily exposed to OP insecticides (mainly fenitrothion, dichlorvos, chlorpyrifos, and diazinon), and partially to pyrethroids (mainly permethrin) and carbamates (mainly propoxur). |
5(0,0,0,5) | Details |
| 10421440 | Josse D, Xie W, Masson P, Lockridge O: Human serum paraoxonase (PON1): identification of essential amino acid residues by group-selective labelling and site-directed mutagenesis. Chem Biol Interact. 1999 May 14;119-120:71-8. The catalytic constants k (cat) and Km (relative to k (cat) and Km of the wild-type) determined with four different substrates (phenylacetate, paraoxon, diazoxon, chlorpyrifos oxon), were not significantly changed for the following mutants: W193A, W201A, W253A, H160N, H245N, H250N, H347N, E32A, E48A, D88A, D107A, D121A, D273A. |
5(0,0,0,5) | Details |
| 9170151 | Li WF, Matthews C, Disteche CM, Costa LG, Furlong CE: Paraoxonase (PON1) gene in mice: sequencing, chromosomal localization and developmental expression. Pharmacogenetics. 1997 Apr;7(2):137-44. Serum paraoxonase activities toward three substrates, paraoxon, chlorpyrifos-oxon and diazoxon, were very low at birth and increased with age reaching adult levels at 20 days in mice and 25 days in rats. |
5(0,0,0,5) | Details |
| 10421441 | Josse D, Xie W, Masson P, Schopfer LM, Lockridge O: residue (s) as major components of the human serum paraoxonase active site. Chem Biol Interact. 1999 May 14;119-120:79-84. |
4(0,0,0,4) | Details |
| 11350209 | Cowan J, Sinton CM, Varley AW, Wians FH, Haley RW, Munford RS: Gene therapy to prevent organophosphate intoxication. Toxicol Appl Pharmacol. 2001 May 15;173(1):1-6. The specific hydrolytic activity of PON1 paraoxonase/arylesterase enzymes in liver and blood provides a natural barrier against the entry of organophosphate toxins into the central and peripheral nervous systems. To test whether boosting serum levels of PON1 enzymes by gene therapy might provide increased protection, we compared the degree of inactivation of whole brain acetylcholinesterase of mice exposed to chlorpyrifos 4 days after intravenous injection of recombinant adenoviruses containing PON1-LQ or PON1-LR genes or no PON1 gene. |
4(0,0,0,4) | Details |
| 18711144 | Stevens RC, Suzuki SM, Cole TB, Park SS, Richter RJ, Furlong CE: Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning. Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12780-4. Epub 2008 Aug 18. Experiments with mice lacking PON1 (PON1 (-/-) mice) have established that plasma PON1 protects against chlorpyrifos/chlorpyrifos-oxon and diazinon/diazoxon (DZO) exposure but does not protect against parathion/paraoxon or nerve agents. |
4(0,0,0,4) | Details |
| 19223938 | Albers JW, Garabrant DH, Berent S, Richardson RJ: Paraoxonase status and plasma butyrylcholinesterase activity in chlorpyrifos manufacturing workers. J Expo Sci Environ Epidemiol. 2010 Jan;20(1):79-89. Epub 2009 Feb 18. PON1 polymorphisms include a (Q)/ (R) substitution at position 192 (PON1 (Q192R)) that affects hydrolysis of OP substrates, with the PON1 (192Q) allotype hydrolyzing chlorpyrifos oxon less efficiently than the PON1 (192R) allotype, a variation potentially important in determining susceptibility to chlorpyrifos. |
170(2,2,3,5) | Details |
| 14998758 | Berkowitz GS, Wetmur JG, Birman-Deych E, Obel J, Lapinski RH, Godbold JH, Holzman IR, Wolff MS: In utero pesticide exposure, maternal paraoxonase activity, and head circumference. Environ Health Perspect. 2004 Mar;112(3):388-91. However, when the level of maternal PON1 activity was taken into account, maternal levels of chlorpyrifos above the limit of detection coupled with low maternal PON1 activity were associated with a significant but small reduction in head circumference. |
89(1,1,2,4) | Details |
| 12655035 | Poet TS, Wu H, Kousba AA, Timchalk C: In vitro rat hepatic and intestinal metabolism of the organophosphate pesticides chlorpyrifos and diazinon. Toxicol Sci. 2003 Apr;72(2):193-200. Epub 2003 Mar 7. In addition, A-esterase (PON1) metabolism of CPF- and DZN-oxon also forms TCP and IMHP. |
4(0,0,0,4) | Details |
| 20156521 | Povey AC: Gene-environmental interactions and organophosphate toxicity. Toxicology. 2010 Feb 13. OP oxons are inactivated by serum paraoxonase (PON1) and mice lacking PON1 activity are susceptible to oxon and parent OP induced toxicity. Diazinon, like chlorpyrifos, is an organothiophosphate which is metabolised, particularly by cytochrome p450s, to the corresponding active oxon form. |
3(0,0,0,3) | Details |
| 20176005 | Otto TC, Kasten SA, Kovaleva E, Liu Z, Buchman G, Tolosa M, Davis D, Smith JR, Balcerzak R, Lenz DE, Cerasoli DM: Purification and characterization of functional human paraoxonase-1 expressed in Trichoplusia ni larvae. Chem Biol Interact. 2010 Feb 20. T. ni larvae expressing HuPON1 were remarkably resistant to the pesticide chlorpyrifos. |
2(0,0,0,2) | Details |
| 16002382 | Searles Nielsen S, Mueller BA, De Roos AJ, Viernes HM, Farin FM, Checkoway H: Risk of brain tumors in children and susceptibility to organophosphorus insecticides: the potential role of paraoxonase (PON1). Environ Health Perspect. 2005 Jul;113(7):909-13. Organophosphorus insecticides (OPs) target the developing nervous system, and until recently, the most common residential insecticides were chlorpyrifos and diazinon, two OPs metabolized in the body through the cytochrome P450/paraoxonase 1 (PON1) pathway. |
87(1,1,1,7) | Details |
| 8393745 | Furlong CE, Costa LG, Hassett C, Richter RJ, Sundstrom JA, Adler DA, Disteche CM, Omiecinski CJ, Chapline C, Crabb JW, et al.: Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification. Chem Biol Interact. 1993 Jun;87(1-3):35-48. Toxicity studies showed that raising rat plasma paraoxonase levels by i.v. administration of partially purified rabbit paraoxonase protected animals against cholinesterase inhibition by paraoxon and chlorpyrifos oxon. |
87(1,1,1,7) | Details |
| 16343727 | Timchalk C, Poet TS, Kousba AA: Age-dependent pharmacokinetic and pharmacodynamic response in preweanling rats following oral exposure to the organophosphorus insecticide chlorpyrifos. Toxicology. 2006 Mar 1;220(1):13-25. Epub 2005 Dec 15. Metabolism involves CYP450 activation and detoxification of CPF to CPF-oxon and 3,5,6-trichloro-2-pyridinol (TCP), as well as cholinesterase (acetyl- and butyrylcholinesterase), carboxylesterase (CaE), and A-esterase (PON-1) detoxification of CPF-oxon to TCP. |
1(0,0,0,1) | Details |
| 20211614 | Sogorb MA, Vilanova E: Serum albumins and detoxication of anti-cholinesterase agents. Chem Biol Interact. 2010 Mar 6. Serum albumin displays an esterase activity that is capable of hydrolysing the anti-cholinesterase compounds carbaryl, paraoxon, chlorpyrifos-oxon, diazoxon and O-hexyl, O-2,5-dichlorphenyl phosphoramidate. We conclude the need for a structure-activity relationship study into the albumin-associated esterase activities because this protein is universally present in vertebrates and could compensate for reduced levels of other esterases, i.e., lipoprotein paraoxonase, in some species. |
1(0,0,0,1) | Details |