Study of the activity of glutathione-peroxidase, glutathione-transferase, and glutathione-reductase in renal transplants

Vega, Libia; Pérez, Rebeca; Mateo, M. C. Martín; Bustamante, Jesús; Bustamante, Andrea P.; Herrero, Agueda; Munguira, E. Bustamante

doi:10.1016/s0041-1345(03)00475-5

Cited by 16 publications

(4 citation statements)

References 8 publications

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“…Glutathione reductase (GR) (42,43) likely minimizes concentrations of GSSG, at least in healthy (nonoxidatively stressed) cells, and TrxR (26) also drives oTrx toward rTrx. High intracellular GSH concentrations (1-5 mM) would suggest that rTrx (and rTrx-SNO) likely predominate in vivo under normal conditions.…”

Section: Discussionmentioning

confidence: 99%

Site-specific and redox-controlled S-nitrosation of thioredoxin

Barglow

Knutson²,

Wishnok³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Protein S-nitrosation on cysteine residues has emerged as an important posttranslational modification in mammalian cells. Previous studies have suggested a primary role for thioredoxin (Trx) in controlling protein S-nitrosation reactions. Human Trx contains five conserved Cys, including two redox-active catalytic Cys (Cys32 and Cys35) and three non-active-site Cys (Cys62, Cys69, and Cys73), all of which have been reported as targets of S-nitrosation. Prior reports have studied thermodynamic end points of nitrosation reactions; however, the kinetics of Trx nitrosation has not previously been investigated. Using the transnitrosation agent, S-nitrosoglutathione, a kinetic analysis of the selectivity and redox dependence of Trx nitrosation at physiologically relevant concentrations and times was performed, utilizing a mass spectrometry-based method for the direct analysis of the nitrosated Trx. Reduced Trx (rTrx) was nitrosated 2.7-times faster than oxidized Trx (oTrx), and rTrx was nitrosated selectively on Cys62, whereas oTrx was nitrosated only on Cys73. These sites of nitrosation were confirmed at the peptide level using a novel modification of the biotin-switch technique called the reductive switch. These results suggest separate signaling pathways for Trx-SNO under different cellular redox states.cysteine | nitric oxide | S-nitrosoglutathione | transnitrosation

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Section: Discussionmentioning

confidence: 99%

Site-specific and redox-controlled S-nitrosation of thioredoxin

Barglow

Knutson²,

Wishnok³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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“…This implies that cells whose development has been affected by riboflavin deficiency at the crucial stage in their development where they are about to differentiate are subsequently unable to divide properly. Riboflavin adequacy is central to synthesis of reduced glutathione, a substrate for glutathione peroxidase, and the xenobiotic-metabolizing enzyme glutathione-S-transferase [19,40]. Whilst the controlled use of media would not suggest that levels of trace elements are responsible for the alteration of gene expression associated with metal binding and metabolism, it may be indicative of cells Relative quantification by RT-PCR for a subset of two genes.…”

Section: Discussionmentioning

confidence: 99%

Riboflavin Depletion Impairs Cell Proliferation in Adult Human Duodenum: Identification of Potential Effectors

et al. 2010

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“…However, there is evidence that antioxidant enzyme activity is lowered in patients suffering from CRF. 23 Reports further indicate that the renal transplantation is not connected with the normalization of the activity of these enzymes which usually remain lower than those of healthy individuals. 7,17,24 In this study, we found changes in the erythrocyte activity of SOD and CAT following KT that was probably linked to the partial elimination of OS.…”

Section: The Effect Of Immunosuppressivesmentioning

confidence: 99%

Stabilization of Oxidative Stress 1 Year after Kidney Transplantation: Effect of Calcineurin Immunosuppressives

et al. 2012

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Kidney transplantation (KT) is one of the best treatments for patients with chronic renal disease. It leads to improved kidney function, but the oxidative stress (OS) is only partially eliminated after KT. This study evaluated the effect of KT on outcomes, such as (a) specific kidney functions, (b) metabolic parameters, as well as (c) OS-related markers in 70 patients (46 males, 24 females; mean age ¼ 54 AE 11) before and 1 year after KT. Post KT, the patients were divided into two groups: those receiving only cyclosporine A (N ¼ 36) and those receiving only tacrolimus (N ¼ 34). Improved kidney function (creatinine, urea, and glomerular filtration rate) and biochemical and hematological parameters were found 1 year after KT. OS-related markers (total antioxidant capacity, advanced oxidation protein, and lipid peroxidation products) decreased, but glutathione level increased after KT. Alterations in superoxide dismutase and catalase activities were also found. Glutathione peroxidase levels were unchanged. The level of oxidized low-density lipoprotein was surprisingly, not significantly increased. There was no significant difference between calcineurin inhibitors in any of the measured parameters. Improved renal function after KT is linked to reduction in OS but independent of immunosuppressive therapy.

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Study of the activity of glutathione-peroxidase, glutathione-transferase, and glutathione-reductase in renal transplants

Cited by 16 publications

References 8 publications

Site-specific and redox-controlled S-nitrosation of thioredoxin

Site-specific and redox-controlled S-nitrosation of thioredoxin

Riboflavin Depletion Impairs Cell Proliferation in Adult Human Duodenum: Identification of Potential Effectors

Stabilization of Oxidative Stress 1 Year after Kidney Transplantation: Effect of Calcineurin Immunosuppressives

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