Abstract
Biomarkers are used in many areas of health to diagnose the presence of disease, monitor disease progression, track drug distribution in the body, or determine exposure to chemicals. The increase of free radicals damages biochemical macromolecules and increases the formation of new toxic compounds such as enhanced oxidation protein products. Organophosphate (OP) compound exposure, oxidative stress, and lipid peroxide have been associated with DNA damage, various types of cancer, aging, degenerative disease, and inflammatory diseases in humans. For this section, the evaluation of paraoxonase (PON1), a liver enzyme that can hydrolyze toxic OP compounds, is bound to HDL (High-density lipoprotein) in serum and draws attention with its strong antioxidant properties, as a biomarker is discussed. In this chapter, PON1 as a toxicological biomarker was reviewed in three cases: organophosphate exposure, lipid peroxidation, and liver toxicity. PON1 status against toxic damage; both serum PON1 level and PON1 polymorphisms were discussed together in the light of studies. Finding new reliable biomarkers is an area of research that has become increasingly important in recent years.
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Abbreviations
- AChE:
-
Acetylcholinesterase
- BuChE:
-
Butyrylcholinesterase
- CB:
-
N-Methyl-carbamate
- CHD :
-
Coronary heart disease
- ChE:
-
Cholinesterase
- CLD :
-
Chronic liver disease
- DZO:
-
Diazoxon
- HDL:
-
High-density lipoprotein
- His-His :
-
Histidine-histidine
- HTL :
-
Homocysteine thiolactone
- Km :
-
Michaelis constant
- LDL:
-
Low-density lipoprotein
- LDLs:
-
Low-density lipoproteins
- OP:
-
Organophosphate
- PCR :
-
Polymerase chain reaction
- PON1:
-
Paraoxonase 1
- Vmax:
-
Maximum velocity
References
Aviram M, Rosenblat M, Bisgaier CL, et al. Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase. J Clin Invest. 1998;101:1581–90.
Aviram M, Hardak E, Vaya J, et al. Human serum paraoxonases (PON1) Q and R selectively decrease lipid peroxides in human coronary and carotid atherosclerotic lesions: PON1 esterase and peroxidase-like activities. Circulation. 2000;101:2510–7.
Bobe G, Young JW, Beitz DC. Invited review: pathology, etiology, prevention, and treatment of fatty liver in dairy cows. J Dairy Sci. 2004;87(10):3105–24.
Burlina A, Galzigna L. Serum arylesterase isoenzymes in chronic hepatitis. Clin Biochem. 1974;7:202–5.
Camps J, Marsillach J, Joven J. Measurement of serum paraoxonase-1 activity as a potential biomarker for chronic liver impairment. Clin Chim Acta. 2007;386:114–5.
Camps J, Iftimie S, Heredia AG, et al. Paraoxonases and infectious diseases. Clin Biochem. 2017;50(13–14):804–11.
Costa LG, Vitalone A, Cole TB, et al. Modulation of paraoxonase (PON1) activity. Biochem Pharmacol. 2005;69:541–50.
Davies H, Richter RJ, Keifer M, et al. The human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat Genet. 1996;14:334–6.
Deakin S, Leviev I, Gomaraschi M, et al. Enzymatically active paraoxonase-1 is located at the external membrane of producing cells and released by a high affinity, saturable, desorption mechanism. J Biol Chem. 2002;277:4301–8.
Deakin S, Moren X, James RW. Very low density lipoproteins provide a vector for secretion of paraoxonase-1 from cells. Atherosclerosis. 2005;179:17–25.
Farid AS, Honkawa K, Fath EM, et al. Serum paraoxonase-1 as biomarker for improved diagnosis of fatty liver in dairy cows. BMC Vet Res. 2013;9:73.
Ferré N, Marsillach J, Camps J, et al. Genetic association of paraoxonase-1 polymorphisms and chronic hepatitis C virus infection. Clin Chim Acta. 2005;361:206–10.
Furlong CE, Richter RJ, Chapline C, et al. Purification of rabbit and human serum paraoxonase. Biochemistry. 1991;30:10133–40.
Gan KN, Smolen A, Eckerson HW, et al. Purification of human serum paraoxonase/ arylesterase: evidence for one esterase catalyzing both activities. Drug Metab Dispos. 1991;19:100–6.
Gençer N, Arslan O. Purification human PON1Q192 and PON1R192 isoenzymes by hydrophobic interaction chromatography and investigation of the inhibition by metals. J Chromatogr B. 2009;87(3):134–40.
Goswami B, Tayal D, Gupta N, et al. Paraoxonase: a multifaceted biomolecule. Clin Chim Acta. 2009;410(1–2):1–12.
James RW. A long and winding road: defining the biological role and clinical importance of paraoxonases. Clin Chem Lab Med. 2006;44:1052–9.
Jarvik GP, Jampsa R, Richter RJ, et al. Novel paraoxonase (PON1) nonsense and missense mutations predicted by functional genomic assay of PON1 status. Pharmacogenetics. 2003;13(5):291–5.
Katoh N. Relevance of apolipoproteins in the development of fatty liver and fatty liver-related peripartum diseases in dairy cows. J Vet Med Sci. 2002;64(4):293–307.
Li WF, Costa LG, Richter RJ, et al. Catalytic efficiency determines the in vivo efficacy of PON1 for detoxifying organophosphates. Pharmacogenetics. 2000;10:767–99.
Mackness M, Mackness B. Human paraoxonase-1 (PON1) gene structure and expression, promiscuous activities and multiple physiological roles. Gene. 2015;567:12–21.
Mackness M, Arrol S, Durrington PN. Paraoxonase prevents accumulation of lipoperoxides in low-density lipoprotein. FEBS Lett. 1991;286:152–4.
Mackness M, Mackness B, Durrington PN, et al. Paraoxonase: biochemistry, genetics and relationship to plasma lipoproteins. Curr Opin Lipidol. 1996;7(2):69–76.
Mackness B, Hunt R, Durrington PN, et al. Increased immunolocalization of paraoxonase, clusterin, and apolipoprotein A-I in the human artery wall with the progression of atherosclerosis. Arterioscler Thromb Vasc Biol. 1997;17:1233–8.
Marsillach J, Ferre N, Vila MC, et al. Serum paraoxonase-1 in chronic alcoholics: relationship with liver disease. Clin Biochem. 2007;40:645–50.
Marsillach J, Mackness B, Mackness M, et al. Immunohistochemical analysis of paraoxonases-1, 2, and 3 expression in normal mouse tissues. Free Radic Biol Med. 2008;45:146–57.
McClain CJ, Barve S, Deaciuc I, et al. Cytokines in alcoholic liver disease. Semin Liver Dis. 1999;19:205–19.
Navab M, Yu R, Gharavi N, et al. High-density lipoprotein: antioxidant and anti-inflammatory properties. Curr Atheroscler Rep. 2007;9:244–8.
Schrader C, Rimbach G. Determinants of paraoxonase 1 status: genes, drugs and nutrition. Curr Med Chem. 2011;18(36):5624–43.
Visser K, van der Heijde DM. Risk and management of liver toxicity during methotrexate treatment in rheumatoid and psoriatic arthritis: a systematic review of the literature. Clin Exp Rheumatol. 2009;27:1017–25.
Watson AD, Berliner JA, Hama SY, et al. Protective effect of high density lipoprotein associated paraoxonase-inhibition of the biological activity of minimally oxidised low-density lipoprotein. J Clin Invest. 1995;96:2882–91.
Xu GY, Lv GC, Chen Y, et al. Monitoring the level of serum paraoxonase 1 activity in liver transplantation patients. Hepatobiliary Pancreat Dis Int. 2005;4:178–81.
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Gökçe, B. (2022). Serum Paraoxonase 1 as a Biomarker in Toxicology. In: Patel, V.B., Preedy, V.R., Rajendram, R. (eds) Biomarkers in Toxicology. Biomarkers in Disease: Methods, Discoveries and Applications. Springer, Cham. https://doi.org/10.1007/978-3-030-87225-0_3-1
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DOI: https://doi.org/10.1007/978-3-030-87225-0_3-1
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