Glutathione peroxidase activity in patients with renal disorders

被引:43
作者
El-Far M.A. [1 ]
Bakr M.A. [2 ]
Farahat S.E. [2 ]
Abd El-Fattah E.A. [2 ]
机构
[1] Division of Biochemistry, Chemistry Department, Mansoura University, Mansoura
[2] Urology and Nephrology Center, Mansoura University, Mansoura
关键词
Erythrocytes; Glutathione peroxidase; Plasma; Renal disorders;
D O I
10.1007/s10157-005-0343-1
中图分类号
学科分类号
摘要
Background. Glutathione peroxidase (GPx) protects cells from oxidative damage by catalyzing the reduction of both organic and hydrogen peroxides, using glutathione as a reducing agent. Both plasma GPx (P-GPx) and erythrocyte GPx (E-GPx) have been identified in human blood. Kidney proximal tubular cells are the main source of GPx activity in the plasma. Oxidative damage has been reported to participate in the progression and complications of renal diseases. Methods. The activities of both E-GPx and P-GPx were determined, using Randox commercial kits, in 12 patients with nephrotic syndrome (NS), 48 patients with renal impairment (RI), and 50 patients with chronic renal failure on maintenance hemodialysis (HD; before as well as immediately after dialysis), and in 50 healthy volunteers who served as controls. Results. Compared to the results in healthy controls, P-GPx activity was reduced in the HD group and the RI group, whereas the NS group showed no significant difference from the control. The HD group showed a higher drop in P-GPx (reduced to 36.6% of the mean control value) than the RI group (reduced to 61.8% of the mean control value). Further analysis of the RI group showed a highly significant negative correlation between P-GPx activity and serum creatinine level (r = -0.691; P < 0.001). Also, a highly significant negative correlation was found between P-GPx and blood urea nitrogen (r = -0.792; P < 0.001). However, E-GPx activity showed no significant correlation with either serum creatinine or blood urea nitrogen. E-GPx was reduced to 55.2% and 68.9% of the mean control 1 value in the NS group and the RI group respectively, while the HD group showed no significant change. Further analysis of the RI group found that E-GPx activity showed no significant correlation with either serum creatinine or blood urea nitrogen. In HD patients, GPx activity was measured before and immediately after hemodialysis. E-GPx activity was similar before and after dialysis, without a significant difference (pre-dialysis, 37.7 ± 13.5 U/g hemoglobin [Hb]; post-dialysis, 38.72 ± 12.31 U/g Hb). However, P-GPx activity was significantly increased (pre-dialysis, 254.4 ± 62.6 U/ml; post-dialysis, 296.98 ± 74.04 U/ml; P < 0.001), but it was still significantly lower when compared to that in the healthy controls. Conclusions. P-GPx activity is an important test to assess the oxidative damage in patients with kidney diseases. The progression of renal disorders is accompanied by a decrease in P-GPx activity, but not by a decrease in E-GPx activity. Thus, we conclude that P-GPx activity largely depends on physiological renal function, whereas E-GPx activity does not. © Japanese Society of Nephrology 2005.
引用
收藏
页码:127 / 131
页数:4
相关论文
共 19 条
[1]  
Tappel A.L., Glutathione peroxidase and hydroperoxides, Methods Enzymol, 52, pp. 506-13, (1978)
[2]  
Levander O.A., A global view of human selenium nutrition, Annu Rev Nutr, 7, pp. 227-50, (1983)
[3]  
Esterbauer H., Gebicki J., Puhl H., Jürgens G. the role of lipid peroxidation and antioxidants in oxidative modification of LDL, Free Radic Biol Med, 13, pp. 341-90, (1992)
[4]  
Rikans L.E., Hornbrook K.R., Lipid peroxidation, anti-oxidant protection and aging, Biochim Biophys Acta, 1362, pp. 116-27, (1997)
[5]  
Grazioli V., Schiavo R., Casari E., Et al., Antioxidant enzymatic activities and lipid peroxidation in cultured human chondrocytes from vertebral plate cartilage, FEBS Lett, 431, pp. 149-53, (1998)
[6]  
Sigalov A.B., Stern L.J., Enzymatic repair of oxidative damage to human apolipoprotein A-I, FEBS Lett, 433, pp. 196-200, (1998)
[7]  
Klemm A., Voigt C., Friedrich M., Et al., Determination of erythrocyte antioxidant capacity in haemodialysis patients using electron paramagnetic resonance, Nephrol Dial Transplant, 16, pp. 2166-217, (2001)
[8]  
Sundle R.A., Molecular biology of selenoproteins, Annu Rev Nutr, 10, pp. 451-74, (1990)
[9]  
Avissar N., Ornt D., Yagil Y., Et al., Human kidney proximal tubules are the main source of plasma glutathione peroxidase, Am J Physiol, 266, pp. 367-75, (1994)
[10]  
Gwinner W., Deters-Evers U., Brandes R., Et al., Antioxidant-oxidant balance in the glomerulus and proximal tubule of the rat kidney, J Physiol, 509, pp. 599-606