Abstract
BackgroundSerum paraoxonase 1 (PON1), an enzyme associated with high – density lipoproteins (HDL) particles, inhibits the oxidation of serum lipoproteins and cell membranes. PON1 activity is lower in patients with atherosclerosis and in inflammatory diseases. The systemic inflammatory response provoked during cardiopulmonary bypass grafting may contribute to the development of postoperative complications. The aim of the present study was to estimate the dynamic changes in paraoxonase 1 (PON1) activity towards paraoxon and phenyl acetate during and after coronary artery surgery.MethodsTwenty six patients with coronary heart disease undergoing coronary artery bypass grafting (CABG) were enrolled into the study. Venous blood samples were obtained preoperatively, after aortic clumping, after the end of operation, at 6, 18, 30 and 48 h after operation. Paraoxonase activity was measured spectrophotometrically in 50 mM glycine/NaOH buffer (pH 10.5) containing 1.0 mM paraoxon, and 1.0 mM CaCl2. Arylesterase activity was measured in 20 mM TrisCl buffer (pH 8.0) containing 1 mM phenyl acetate and 1 mM CaCl2.ResultsPON1 activity toward paraoxon and phenyl acetate significantly decreased after aorta cross clumping and increased directly after operation. PON1 activity towards paraoxon in preoperative period and PON1 activity towards phenyl acetate in seventh stage of experiment tended to inversely correlate with the occurrence of postoperative complications.ConclusionThe paraoxonase 1 plasma activity is markedly reduced during CABG surgery.
Highlights
Serum paraoxonase 1 (PON1), an enzyme associated with high – density lipoproteins (HDL) particles, inhibits the oxidation of serum lipoproteins and cell membranes
PON1 activity is inversely related to atherosclerosis: it is lower in diseases accelerating development of atherosclerosis and it is reduced in inflammatory diseases [4, 5]
Paraoxonase activity towards paraoxon and phenyl acetate before, during and after coronary artery bypass grafting (CABG) surgery is shown on Figs. 1 and 2
Summary
Serum paraoxonase 1 (PON1), an enzyme associated with high – density lipoproteins (HDL) particles, inhibits the oxidation of serum lipoproteins and cell membranes. Human serum paraoxonase 1 (PON1), a high density lipoprotein (HDL) associated serum esterase has been shown to be responsible for antioxidative properties of HDL. Recent studies have shown that HDL can prevent accumulation of lipid peroxides in LDL and PON1 enzyme is one of the compounds of HDL responsible for this activity. It has PON1 activity is inversely related to atherosclerosis: it is lower in diseases accelerating development of atherosclerosis and it is reduced in inflammatory diseases [4, 5]. Several types of evidence suggest that low levels of PON1 protein raise the risk of development of premature atherosclerosis and low activity of PON1 is a strong independent risk factor for coronary heart
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