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      Roles of Paraoxonase and Oxidative Stress in Adolescents with Uraemic, Essential or Obesity-Induced Hypertension

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          Background/Aims: Paraoxonase 1 (PON1) is associated with high-density lipoproteins in the plasma, and is capable of hydrolysing oxidized lipids and preventing the oxidation of low-density lipoproteins. Oxidative stress and the PON1 (activity and Q192R polymorphism) were analysed in adolescent patients with essential (n = 49) or obesity-induced hypertension (n = 79), uraemic patients (n = 20), and also in obese normotensive patients (n = 60) and age-matched controls (n = 57). Methods: The PON1 activity was measured via paraoxon hydrolysis. The PON1 genotype was determined by real-time PCR. The levels of oxidized and reduced glutathione, the end-products of nitric oxide, cysteine, homocysteine and lipid peroxidation in the plasma were measured and related to the PON1 status. Results: There were no significant differences between the patient groups and the control group in the genotype distributions and the allele frequencies of the Q192R polymorphism. The PON activity was significantly lower (p < 0.001) in the uraemic hypertensive group than in the controls. The MDA concentration was significantly higher in the uraemic hypertensive (p < 0.001) and obese hypertensive (p < 0.05) patients. The plasma NO<sub>x</sub> concentrations were significantly lower (p < 0.001) and the ratio MDA/NO<sub>x</sub> were significantly higher in all four patient groups. The GSH levels were significantly lower in the patients with hypertension (p < 0.001) and obesity-induced hypertension (p < 0.05) than in the controls, while the GSSG level (p < 0.01) and the ratio GSSG/GSH (p < 0.05) was significantly higher in the uraemic hypertensive group. The plasma homocysteine level was significantly higher (p < 0.001) in the uraemic hypertensive patients as compared with the controls. Conclusions: We found no significant correlation between the biochemical parameters and neither genotypes nor enzyme activities. The PON1 status and the levels of certain biochemical parameters are independently associated with the hypertension in hypertensive and obese hypertensive patients, and the elevated levels of lipid peroxides and plasma homocysteine may contribute to the increased risk of cardiovascular complications in patients on haemodialysis.

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          Most cited references 18

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          Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues

           Frank Tietze (1969)
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            Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase.

            We have investigated the Cu2+ induced generation of lipid peroxides in low density lipoprotein (LDL) incubated with high density lipoprotein (HDL) and with purified paraoxonase, an enzyme normally resident on HDL. HDL (1.5 mg) and paraoxonase (20 micrograms) inhibited lipid peroxide generation in LDL by 32% and 25%, respectively after 24 h of incubation (both P < 0.01). The decrease in LDL lipid peroxides both with HDL and with paraoxonase were concentration dependent. The degree of protection offered by HDL tended to relate to its paraoxonase activity (R = 0.47; P < 0.06). Neither purified paraoxonase nor HDL chelated Cu2+ sufficiently to account for the decrease in LDL oxidation. Purified paraoxonase did not affect LDL oxidation when it had been heat inactivated. Mass transfer of lipid peroxides from LDL to HDL did not explain the protection of LDL against oxidation: the total lipid peroxides accumulating during incubation was decreased both by HDL and by paraoxonase. These results suggest a direct role for HDL in preventing atherosclerosis probably by an enzymic process which prevents the accumulation of lipid peroxides on LDL. Paraoxonase is an example of an enzyme which might possibly be involved.
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              Cellular glutathione and thiols metabolism.

              Low molecular weight thiol-containing compounds have an essential role in many biochemical and pharmacological reactions due to the ease with each they are oxidized, and the rapidity with which they can be regenerated. Thioredoxin and glutathione (GSH) are two of the major small molecular weight thiol-containing compounds synthesized de novo in mammalian cells that participate in those functions. Understanding the mechanisms of thiol metabolism has special relevance to understanding the cell's defense against toxicant exposure and as the focal point in redox signaling. This commentary will, however, focus on GSH consumption and synthesis, and the role of thiols in signaling. The chemical reactions of GSH, including conjugation reactions mediated by glutathione S-transferases (GST) and oxidation reactions mediated by glutathione peroxidases will be described. The regulation of GSH synthesis will be illustrated from a compilation of studies designed to understand the various levels at which enzymatic GSH biosynthesis is controlled, and the signaling pathways that mediate them. The response of the cell to 4-hydroxynonenal (4HNE), a reactive aldehyde produced physiologically in response to inflammation and various air pollutants, will be explored in detail. Finally, the direct role of thiols as signaling molecules will be addressed, with particular attention given to "redox state." It is our aim that this commentary will lead the reader to appreciate that studies investigating the signaling for and regulation of thiol metabolism must never be generalized, and that perturbations in any of step of thiol metabolism may have etiological roles in genetically, virally, and environmentally borne pathologies.

                Author and article information

                Kidney Blood Press Res
                Kidney and Blood Pressure Research
                S. Karger AG
                October 2006
                06 October 2006
                : 29
                : 3
                : 144-151
                Department of Paediatrics, University of Szeged, Szeged, Hungary
                95124 Kidney Blood Press Res 2006;29:144–151
                © 2006 S. Karger AG, Basel

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                Figures: 3, Tables: 2, References: 36, Pages: 8
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