Abdullah TAŞKIN, Hakim ÇELİK, Harun TOY, Gakan CAMUZCUOĞLU, Aysun CAMUZCUOĞLU, Mehmet VURAL

Serum paraoxonase and arylesterase activities in iron deficiency anemia during pregnancy

To investigate serum paraoxonase and arylesterase activities, and lipid hydroperoxide levels in pregnant women with iron deficiency anemia. Materials and methods: Paraoxonase and arylesterase activities, and lipid hydroperoxide levels were assessed for pregnant women with iron deficiency anemia (n = 50) and controls (n = 70). Serum basal and salt-stimulated paraoxonase, and arylesterase activities were measured spectrophotometrically. The lipid hydroperoxide levels were measured by ferrous ion oxidation xylenol orange assay. In addition, lipid parameters were determined by routine laboratory methods. Results: Basal and salt-stimulated paraoxonase, and arylesterase activities were significantly lower (P = 0.026, P = 0.031, and P = 0.018, respectively) in pregnant women with iron deficiency anemia when compared to the controls, while lipid hydroperoxide levels were significantly higher (P = 0.004). A significant positive correlation was found between paraoxonase activity and hemoglobin levels (r = 0.329, P = 0.020), while there was inverse correlation between lipid hydroperoxide and hemoglobin levels (r = -0.457, P = 0.001). Among iron deficiency anemia, serum paraoxonase activity was inversely correlated with lipid hydroperoxide levels (r = -0.535, P < 0.001). Conclusion: The findings of the present study have shown that diminished serum paraoxonase and arylesterase activities, and increased lipid hydroperoxide levels may play a role in the early pathogenesis of atherosclerotic heart disease in pregnant women with iron deficiency anemia.

Anahtar Kelimeler:

Key words: Iron deficiency anemia, pregnancy, paraoxonase, arylesterase, lipid hydroperoxide levels

Serum paraoxonase and arylesterase activities in iron deficiency anemia during pregnancy

Keywords:

Key words: Iron deficiency anemia, pregnancy, paraoxonase, arylesterase, lipid hydroperoxide levels,

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Stocker R, Keaney JF, Jr. Role of oxidative modifications in atherosclerosis. Physiol Rev 2004; 84: 1381-1478.
Watson AD, Berliner JA, Hama SY, La Du BN, Faull KF, Fogelman AM et al. Protective effect of high density lipoprotein associated paraoxonase. Inhibition of the biological activity of minimally oxidized low density lipoprotein. J Clin Invest 1995; 96: 2882-91.
Aviram M, Rosenblat M, Bisgaier CL, Newton RS, Primo- Parmo SL, La Du BN. Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase. J Clin Invest 1998; 101: 1581- 90.
Ayub A, Mackness MI, Arrol S, Mackness B, Patel J, Durrington PN. Serum paraoxonase after myocardial infarction. Arterioscler Thromb Vasc Biol 1999; 19: 330-35.
Mackness MI, Harty D, Bhatnagar D, Winocour PH, Arrol S, Ishola M et al. Serum paraoxonase activity in familial hypercholesterolaemia and insulin-dependent diabetes mellitus. Atherosclerosis 1991; 86: 193-99.
Eckerson HW, Wyte CM, La Du BN. The human serum paraoxonase/arylesterase polymorphism. Am J Hum Genet 1983; 35: 1126-38.
Haagen L, Brock A. A new automated method for phenotyping arylesterase (EC 3.1.1.2) based upon inhibition of enzymatic hydrolysis of 4-nitrophenyl acetate by phenyl acetate. Eur J Clin Chem Clin Biochem 1992; 30: 391-95.
Nourooz-Zadeh J. Ferrous ion oxidation in presence of xylenol orange for detection of lipid hydroperoxides in plasma. Methods Enzymol 1999; 300: 58-62.
Isler M, Delibas N, Guclu M, Gultekin F, Sutcu R, Bahceci M et al. Superoxide dismutase and glutathione peroxidase in erythrocytes of patients with iron deficiency anemia: effects of different treatment modalities. Croat Med J 2002; 43: 16-9.
Jansson LT, Perkkio MV, Willis WT, Refino CJ, Dallman PR. Red cell superoxide dismutase is increased in iron deficiency anemia. Acta Haematol 1985; 74: 218-21.
Blatter MC, James RW, Messmer S, Barja F, Pometta D. 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 1993; 211: 871-79.
Mackness B, Durrington PN, Mackness MI. Human serum paraoxonase. Gen Pharmacol 1998; 31: 329-36.
Shih DM, Gu L, Xia YR, Navab M, Li WF, Hama S et al. Mice lacking serum paraoxonase are susceptible to organophosphate toxicity and atherosclerosis. Nature 1998; 394: 284-87.
Tward A, Xia YR, Wang XP, Shi YS, Park C, Castellani LW et al. Decreased atherosclerotic lesion formation in human serum paraoxonase transgenic mice. Circulation 2002; 106: 484-90.
Mackness MI, Durrington PN, Ayub A, Mackness B. Low serum paraoxonase: a risk factor for atherosclerotic disease? Chem Biol Interact 1999; 119-120: 389-97.
Merono T, Sorroche P, Rosso LA, Casanas L, Boero LE, Arbelbide JA et al. Proatherogenic disturbances in lipoprotein profile, associated enzymes and transfer proteins in women with iron deficiency anaemia. Clin Biochem 2010; 43: 416-23.