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      Plasma Glutathione Peroxidase Activity Is Reduced in Haemodialysis Patients

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          Cardiovascular disease is the major cause of morbidity and mortality in patients with end-stage renal failure. Increased free radical production and antioxidant depletion may contribute to the greatly increased risk of atherosclerosis in these patients. Glutathione peroxidase (GPX) is an important antioxidant, the plasma form of which is synthesized mainly in the kidney (eGPX). The aim of this study was to assess the activity of eGPX in patients with end-stage renal failure on haemodialysis. Venous blood was collected from 87 haemodialysis patients immediately prior to and after dialysis and from 70 healthy controls. Serum eGPX activity was measured using hydrogen peroxide as substrate and immunoreactivity determined by ELISA. eGPX activity was significantly reduced in dialysis patients when compared to controls (106 ± 2.7 and 281 ± 3.6 U/l respectively, p < 0.001). Following haemodialysis, eGPX activity rose significantly to 146 ± 3.8 U/l, p < 0.001, although remaining below control values (p < 0.005). Immunoreactive eGPX, however, was similar in all groups (pre-dialysis 14.10 ± 1.26 µg/ml, post-dialysis 14.58 ± 1.35 µg/ml, controls 15.20 ± 1.62 µg/ml, p = NS). A decrease was observed in the specific activity of eGPX in patients when compared to controls (8.81 ± 1.14, 10.71 ± 1.54 and 21.97 ± 1.68 U/mg respectively, p < 0.0001). eGPX activity is impaired in patients undergoing haemodialysis and so may contribute to atherogenesis in renal failure.

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          Most cited references 3

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          Lipoperoxidation in plasma and red blood cells of patients undergoing haemodialysis: Vitamins A, E, and iron status

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            Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides.

            The reactivities of a selenoenzyme, glutathione peroxidase isolated from plasma, against phosphatidylcholine hydroperoxides and photoperoxidized erythrocyte ghosts have been investigated. Glutathione peroxidase isolated from plasma was found to catalyze the reduction of phosphatidylcholine hydroperoxides to the corresponding hydroxy derivatives. The enzyme is also capable of reducing the hydroperoxides in photoperoxidized ghosts. Thin layer chromatographic analysis of enzyme-treated ghosts revealed that plasma glutathione peroxidase can reduce phospholipid-derived hydroperoxides but cannot reduce cholesterol hydroperoxides. These studies demonstrate that the three known glutathione peroxidase (cellular, plasma, and phospholipid hydroperoxide) differ from each other in substrate specificity.
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              The human plasma glutathione peroxidase-encoding gene: organization, sequence and localization to chromosome 5q32


                Author and article information

                S. Karger AG
                March 1999
                26 February 1999
                : 81
                : 3
                : 278-283
                Departments of aClinical Biochemistry and b Medicine, The Queen’s University of Belfast, Royal Victoria Hospital, Belfast, and c The Regional Nephrology Unit, Belfast City Hospital, Northern Ireland
                45293 Nephron 1999;81:278–283
                © 1999 S. Karger AG, Basel

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                Page count
                Figures: 4, Tables: 1, References: 25, Pages: 6
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/45293
                Original Paper


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