Paraoxonase and arylesterase activity of paraoxonase 1 and oxidative stress parameters in cervical intraepithelial neoplasia

Author:

Rajković Marija Grdić1,Rašić Dubravka2,Stojanović Ivana3,Turčić Petra4,Miletić Tomislav5,Tomašković Andrea Hulina1,Kačkov Maslać Sanja6,Ćelap Ivana7,Butorac Dražan3

Affiliation:

1. Department of Medical biochemistry and Hematology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb, Croatia

2. Unit of Toxicology, Institute for Medical Research and Occupational Health, Zagreb, Croatia

3. Clinic of Gynecology and Obstetrics, Sestre milosrdnice University Hospital Center, Zagreb, Croatia

4. Department of Pharmacology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb, Croatia

5. Polyclinic Aviva, Zagreb, Croatia

6. Medical biochemistry laboratory, Polyclinic Bonifarm, Zagreb, Croatia

7. Department of Clinical Chemistry, Sestre milosrdnice University Hospital Center, Zagreb, Croatia

Abstract

IntroductionParaoxonase 1 (PON1) is the enzyme that removes carcinogenic radicals from lipids. The aim of the study was to investigate the differences in PON1 activity and oxidation stress parameters between patients with cervical intraepithelial neoplasia (CIN) and healthy controls. Materials and methodsThe study included 65 women with CIN and 109 healthy women. Lipid parameters were determined on Cobas Integra 400 plus (Roche, Mannheim, Germany). Tiols and reduced glutathione (GSH) were determined spectrophotometric using Eliman reagent. Activity of PON1 was assessed with two substrates, paraoxon and phenylacetate by spectrophotometric method. Malondialdehyde (MDA) was determined by high performance liquid chromatography (Shimadzu Corporation, Kyoto, Japan). Mann-Whitney-test, t-test, χ2-test, correlation and logistic regression was used in statistical analysis. P < 0.05 was considered statistically significant. ResultsThe basal (P = 0.929) and NaCl-stimulated (P = 0.985) PON1 activity and activities standardised on the concentration of high-density lipoprotein (HDL; P = 0.076; P = 0.065, respectively) and apolipoprotein AI (apo AI; P = 0.444; P = 0.499, respectively) as well as PON1 phenotypes (P = 0.842) did not differ significantly between the groups. The PON1 arylesterase activity (53±19 kU/L vs. 77±17 kU/L; P < 0.001) and HDL-standardized activity (37 (28-44) kU/mmol vs. 43 (37-50) kU/mmol; P < 0.001) and apoAI (29±11 kU/g vs. 44±11 kU/g; P < 0.001) was significantly reduced in the CIN group. The concentration of the thiol groups was similar (P = 0.519), of MDA was lower (0.39 (0.27-0.55) µmol/L vs. 0.76 (0.57-1.15) µmol/L; P < 0.001) and of GSH was higher (112.0 (66.0-129.6) µg/mL vs. 53.4 (34.8-134.4) µg/mL; P < 0.001) in the CIN group. ConclusionReduced PON1 arylesterase activity, lower MDA and higher GSH concentration were observed in CIN patients.

Publisher

Croatian Society for Medical Biochemistry and Laboratory Medicine

Subject

Biochemistry (medical),Clinical Biochemistry

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