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M. Kulka, J. Kołodziejska-Lesisz and W. Kluciński

conditions, and liver function in transition dairy cows. J Dairy Sci 90: 1740-1750. Bin Ali A, Zhang Q, Lim YK, Fang D, Retnam L, Lim SK (2003) Expression of major HDL-associated antioxidant PON-1 is gender dependent and regulated during inflammation. Free Radic Biol Med 34: 824-829. Blatter MC, James RW, Messer S, Barja F, Pometta D (1993) Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase. Eur J Biochem 211: 871

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M. Kulka

during atherosclerosis development. Free Radic Biol Med 37: 1304-1316. Aviram M, Rosenblat M, Bisgaier CL, Newton RS, Primo-Parmo SL, La Du BN (1998B) Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase. J Clin Invest 101: 1581-1590. Azarsiz E, Kayikcioglu M, Payzin S, Yildirim Sözmen E (2003) PON1 activities and oxidative markers of LDL in patients with angiographically proven coronary artery disease. Int J Cardiol 91: 43-51. Bauchart D (1993

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Irina Ilea, Iulia Lupan, Daniel Corneliu Leucuta, Caius Romulus Duncea and Maria Dronca

References 1. Mackness B, Durrington PN, Mackness MI. The paraoxonase gene family and coronary heart disease. Curr Opinion Lipidol 2002; 13: 357-62. 2. Draganov, D. I., and B. N. La DuPharmacogenetics of paraoxonases: a brief review. Naunyn Schmiedebergs Arch Pharmacol 2004; 369: 78-88. 3. Furlong CE, Richter RJ, Li WF, Brophy VH, Carlson C, Rieder M, Nickerson D, Costa LG, Ranchalis J, Lusis AJ, Shih DM, Tward A, Jarvik GP., The functional consequences of polymorphisms in the PON1 gene. In: The

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Elzbieta Kimak, Iwona Baranowicz-Gaszczyk and Tomasz Bialopiotrowicz

. Mol. Biol., 376, 997, 2008. 7. Guha M., Gursky O.: Effects of Oxidation on Structural Stability and Remodeling of Human Very Low Density Lipoprotein. Biochemistry, 49, 9584, 2010. 8. Gungor O. et al. Serum paraoxonase 1 activity predicts arterial stiffness in renal transplant recipients. J. Atheroscler. Thromb., 18, 901, 2011. 9. Hine D., Mackness B., Mackness M.: Coincubation of PON1, apoAI, and LCAT increases the time HDL is able to prevent LDL oxidation. IUBMB Life, 64, 157, 2012. 10. Jonas A

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Mostafa Saadat

References 1. Mackness M, Mackness B. Human paraoxonase- 1 (PON1): Gene structure and expression, promiscuous activities and multiple physiological roles. Gene 67: 12-21, 2015. 2. La Du BN. The human serum paraoxonase/arylesterase polymorphism. Am J Hum Genet 43: 227-2279, 1988. 3. Shih DM, Gu L, Xia YR et al. Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature 394: 284-287, 1998. 4. Wei LK, Au A, Menon S et al. Polymorphisms of MTHFR, eNOS, ACE

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Michal Harel, Boris Brumshtein, Ran Meged, Hay Dvir, Raimond Ravelli, Andrew McCarthy, Lilly Toker, Israel Silman and Joel Sussman

by human serum paraoxonase. Biochem J 2001;354:1-7. Ahmed Z, Ravandi A, Maguire GF, Emili A, Draganov D, La Du BN, Kuksis A, Connelly PW. Apolipoprotein A-I promotes the formation of phosphatidylcholine core aldehydes that are hydrolyzed by paraoxonase (PON-1) during high density lipoprotein oxidation with a peroxynitrite donor. J Biol Chem 2001;276:24473-81. Jakubowski H. Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J Biol Chem

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Manel Araoud, Fadoua Neffeti, Wahiba Douki, Abderraouf Kenani and Mohamed Fadhel Najjar

References 1. Costa LG, Vitalone A, Cole TB, Furlong CE. Modulation of paraoxonase (PON1) activity. Biochem Pharmaco. 2005; 69:541-50. 2. Akgür SA, Oztürk P, Solak I, Moral AR, Ege B. Human serum paraoxonase (PON1) activity in acute organophosphorus insecticide poisoning. Forensic Sci Int. 2003; 133:136-40. 3. Rochu D, Chabriere E, Masson P. Human paraoxonase: A promising approach for pre-treatment and therapy of organophosphorus poisoning. Toxicology. 2007; 233:47-59. 4. James RW, Leviev I

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Fatma Ceyla Eraldemir, Nihal Üren, Tuğba Kum, Burcu Erbay, Deniz Şahin, Emel Ergül, Esra Acar, Doğa Özsoy, Mustafa Çekmen, Hale Kır and Zafer Utkan

oxidative stress. Oxidative stress may cause cell transformation process raising the risk of cancer development ( 3 ). Paraoxonase 1 (PON1) and arylesterase (ARE) are high-density lipoprotein (HDL)-bound enzyme system of antioxidants which protect LDL and HDL from oxidation. Lipid peroxides and hydrogen peroxide are neutralised by PON1 ( 4 ). PON1 activity is decreased in diabetic patients ( 4 , 5 ). Polymorphism in PON1 gene leads to amino acid differences in position 192 of PON1 enzyme ( 4 ). Additionally, PON1 enzyme has got ARE enzyme activity and that part of

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Lorena Ciumărnean, Ştefan C. Vesa, Eleonora Dronca, Dorel P. Sâmpelean, Vasile C. Vlad, Maria S. Moldovan and Cadariu A. Achimaş

References 1. She Z-G, Chen H-Z, Yan Y, Li H, Liu D-P. The Human Paraoxonase Gene Cluster as a Target in the Treatment of Atherosclerosis. Antioxid Redox Signal. 2012 Mar 15;16(6):597-632. 2. Kedage V, Muttigi MS, Shetty MS, Suvarna R, Rao SS, Joshi C, et al. Serum Paraoxonase 1 Activity Status in Patients with Liver Disorders. Saudi J Gastroenterol. 2010;16(2):79-83. 3. Beltowski J, Wójcicka G, Jamroz A. Leptin decreases plasma paraoxonase 1 (PON1) activity and induces oxidative stress: the possible

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Hamit Yasar Ellidag, Esin Eren, Ozgur Aydin, Salim Neselioglu and Necat Yilmaz

-7. 13. Tang WH, Hartiala J, Fan Y, Wu Y, Stewart AF, Erd mann J. Clinical and genetic association of serum para oxo - na se and arylesterase activities with cardiovascular risk. Arterio scler Thromb Vasc Biol 2012; 32(11): 2803-12. 14. Dai-Hua F, Cong-Hai F, Qiang J, Bo-Xiang Q, Juan L, Lu W. Differential effects of paraoxonase 1 (PON1) polymorphisms on cancer risk: evidence from 25 published studies. Molecular Biology Reports 2012; 39: 6801-9. 15. Aksoy-Sagirli P, Cakmakoglu B, Isbir T, Kaytan SE, Kizir A, Topuz E, et al. Paraoxonase-1