Xanthine Oxidase and Paraoxonase – 1 as a new markers in the diagnosis and prognosis of organophosphorus pesticide poisoning
About this article
Abstract
Background: Acetylcholinesterase is already well known marker for organophosphorus poisoning in human beings. But, our interest was to known for another new markers. There is high limited study on xanthine oxidase and paraoxonase 1 in human beings having organophosphorus poisoning. Thus, aim of our this research was to estimate and correlate activities of xanthine oxidase and paraoxonase 1 in different stages of organophosphorus poisoning in a way to find out potential of these enzymes as marker of organophosphorus poisoning in human beings.
Method: Xanthine oxidase (XO) activity was determined by Roussos method while paraoxonase (PON1) activity was determined by spectrophotometric method.
Result: As compared to healthy controls, the activities of paraoxonase 1 were continuously and significantly decreased (p < 0.01) from group I to group V, while, the activities of xanthine oxidase were continuously and significantly increased (p < 0.01) from group I to group V in organophosphorus poisoned patients.
Conclusion: We found a proportional increase in xanthine oxidase (XO) and a proportional decrease in paraoxonase 1 activity with severity of organophosphorus poisoning. Increase in xanthine oxidase activity is less significant compared to decrease in activity of paraoxonase 1. However, xanthine oxidase activity is a marker of oxidative stress developed in organophosphorus poisoning. Thus, paraoxonase 1 (PON1) can be used as a potent biochemical marker in the diagnosis and prognosis of organophosphorus poisoning along with xanthine oxidase (XO).
References
[1] V Ubale et.al. Text book of organic chemistry B.Sc.-part III, Paper – VII 2nd edition (2007) :10.1-15
[2] M Ellenhorn , S Schonwald, G Ordog, J Wasserberger. Ellenhorn's Medical Toxicology: Diagnosis and Treatment of Human Poisoning, Williams & Wilkins 4th edition, (1997):1614-63.
[3] L James. How to prevent and treat pesticide poisoning. NSW agriculture, (2003):1-3.
[4] Q Haque, F Jamal, S Rastogi. Effect of organophosphorus on biochemical parameters on agriculture workers on mango orchards. Asian J Biochemistry, 7 (1), (2012): 37-45.
[5] M Sungur et.al. Intensive care management of organophosphate insecticide poisoning. Critical care; 5(4), (2001):211-5.
View more references (29)
[6] T Satoh, S Suzuki, N Kawai, T Nakamura, M Hosokawa. Toxicological significance in the cleavage of esterase–beta-glucuronidase complex in liver microsomes by organophosphorus compounds. Chem Biol Interact; 119 (1999) : 471–478.
[7] S Inayat-Hussain, S Lubis, N Sakian et al. Is plasma beta-glucuronidase a novel human biomarker for monitoring anticholinesterase pesticides exposure? A Malaysian experience. Toxicol Appl Pharmacol; 219 (2007) : 210–216.
[8] C Aaron. Organophosphatase and Carbamates. Ford: Clinical Toxicology, 1st edition (2001):819-26.
[9] M Johnson, D Jacobsen, T Meredith, P Eyer, A Heath, D Ligtenstein et al. The IPCS working group on antidotes for organophosphorus pesticide poisoning, WHO. Evaluation of antidotes for poisoning by organophosphorus pesticides. Emerg Med 12, (2000):22-37.
[10] E Robenshtok, Z Tashma, A Hourvitz et.al. Adverse reaction to atropine and the treatment of organophosphate intoxication. IMAJ; 4, (2002):535-9.
[11] G Quistad, J Casida et.al. Blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants. Toxicol Sci ,86(2), (2005):291–9.
[12] B Sharma, S Bano et.al. Human acetyl cholinesterase inhibition by pesticide exposure. J Chinese Clin Med; 4 (1),(2009):55-60.
[13] J Vidyasagar, N Karunakar, D Krishna et.al. Oxidative stress and antioxidant status in acute organophosphorus insecticide poisoning. Ind J Pharmacol; 36/2 (2004): 76 –9.
[14] B La Du. Human serum paraoxonase/arylesterase. In: Kalow W, ed. Pharmacogenetics of Drug Metabolism. New York, NY: Pergamon Press, Inc; (1992):51-91.
[15] S Adkins, K Gan, M Mody. Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes. Am J Hum Genet.52; (1993):598-608.
[16] R Humbert, D Adler, C Disteche, C Hassett, C Omiecinski, C Furlong. The molecular basis of the human serum paraoxonase activity polymorphism. Nat Genet. 3 (1993):73-6.
[17] W Li, L Costa, C Furlong. Serum paraoxonase status: a major factor in determining resistance to organophosphates. J Toxicol Environ Health.40: (1993):337-46.
[18] C Enroth, B Eger, K Okamoto, T Nishino, E Pai. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. 97 (20); (2000):10723–8.
[19] T Ardan, J Kovaceva, J Cejkova. Comparative histochemical and immunohistochemical study on xanthine oxidoreductase/xanthine oxidase in mammalian corneal epithelium. Acta Histochem. 106 (1); (2004):69–75.
[20] R Hille. Molybdenum-containing hydroxylases. Arch. Biochem. Biophys. 433 (1); (2005):107–16.
[21] R Harrison. Structure and function of xanthine oxidoreductase: where are we now? Free Radic. Biol. Med.33 (6);(2002):774–97.
[22] N Krupesh, T Chandrashekar. Organophosphorus poisoning – still a challenging proposition. Ind J Anaesth, 46(1); (2002):40–3.
[23] G Roussos. Xanthine oxidase from bovine small intestine. Methods in Enzymology. New York (NY): Academic Press; 3rd edition, vol – XII A, (1967):5-16.
[24] S Suleyman et.al. Serum arylesterase and paraoxonase activity in patients with chronic hepatitis. World J Gastroenterol. 11(46); (2005):7351-4.
[25] C Bergmeier, R Siekmeier, W Gross. Distribution spectrum of paraoxonase activity in HDL fractions. Clin. Chem. 50 (12); (2004):2309–15.
[26] H Li, D Liu, C Liang. Paraoxonase gene polymorphisms, oxidative stress, and diseases. J Molecular Medicine. 81 (12); (2003):766–79.
[27] C Ng, D Wadleigh, A Gangopadhyay et al. Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J. Biol. Chem. 276 (48); (2001):44444–9.
[28] S Reddy, D Wadleigh, V Grijalva et.al. Human paraoxonase-3 is an HDL-associated enzyme with biological activity similar to paraoxonase-1 protein but is not regulated by oxidized lipids. Arterioscler. Thromb. Vasc. Biol. 21 (4); (2001):542–7.
[29] T Nishino, K Okamoto, Y Kawaguchi et.al. Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cystein disulphide bonds and crystal structure of a non-convertible rat xanthine oxidase mutant. J Biol Chem. 280; (2005):24888-94.
[30] C Berry and J Hare. Xanthine oxidoreductase and cardiovascular diseases: molecular mechanisms and pathophysiological implications. J Physiol. 555; (2004):589-606.
[31] M Wajner and R Harkness. Distribution of xanthine dehydrogenase and oxidase activities in human and rabbit tissues. Biochim Biophys Acta. 991; (1989):79-84.
[32] A Ranjbar, H Solhi, F Mashayekhi et.al. Oxidative stress in acute human poisoning with organophosphorus insecticide: a case control study. Environ Toxicol Pharmacol. 20; (2005):88-91.
[33] M Eddleston, F Mohamed, J Davies et.al. Respiratory failure in acute organophosphorus pesticide self-poisoning. QJM 99; (2006):513-22.
[34] L Ji. Oxidative stress during exercise implication of antioxidant nutrients. Free Rad. Biol. Med. 18; (1995):1079-86.