Glutathione reductase is expressed at high levels in pancreatic islet cells

Nagaoka, Yuki; Iuchi, Yoshihito; Ikeda, Yoshitaka; Fujii, Junichi

doi:10.1179/135100004225006812

Cited by 15 publications

(9 citation statements)

References 13 publications

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“…Considering tissue mass, the total content of Prx-4 is highest in the liver, and thus it is more likely that the supply of the protein to the blood largely depends on the liver. As previously described, Prx-4 appears to be highly expressed in exocrine pancreas rather than islets (37), and another study also reported that another Prx isoform is highly expressed in pancreatic islet cells (38). Consistent with these findings, it would be reasonable that no significant alteration of Prx-4 levels in the serum would be observed in the experiments using streptozotocininduced diabetic rats.…”

Section: Discussionsupporting

confidence: 77%

Measurement of peroxiredoxin-4 serum levels in rat tissue and its use as a potential marker for hepatic disease

Ito

Takahashi

Ihara

et al. 2012

Molecular Medicine Reports

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Abstract. Peroxiredoxin (Prx)-4, a secretable endoplasmic reticulum (ER)-resident isoform of the mammalian Prx family, functions as a thioredoxin-dependent peroxidase. It is acknowledged that Prx-4 plays a role in the detoxification of hydrogen peroxide, and potentially other peroxides, which may be generated during the oxidative folding of proteins and oxidative stress in the ER. The present study was undertaken in order to specifically quantify the tissue levels of Prx-4. To accomplish this, an enzyme-linked immunosorbent assay was developed using a specific polyclonal antibody produced by immunizing a rabbit with native recombinant rat Prx-4 protein. The assay was used to detect Prx-4 in the range of 0.1 and 10 ng/ml, and to investigate tissue distribution in rats. Using this immunoassay, we found that the serum levels of Prx-4 were substantially lower in asymptomatic Long-Evans Cinnamon rats, a rat model of Wilson's disease, compared to normal rats. In addition, the treatment of rat hepatoma cells with N-acetylcysteine led to a significant increase in the release of Prx-4 protein into the medium; thus, it appears likely that the secretion of Prx-4 is associated with the redox state within cells. These results suggest that serum Prx-4 has potential for use as a biomarker for hepatic oxidative stress.

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Section: Discussionsupporting

confidence: 77%

Measurement of peroxiredoxin-4 serum levels in rat tissue and its use as a potential marker for hepatic disease

Ito

Takahashi

Ihara

et al. 2012

Molecular Medicine Reports

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“…These enzymes often contain a CXXC redox active dithiol motif and catalyze thiol-disulfide exchange reactions with different substrate specificities. In particular, Trx and Grx systems are generally described as protein disulfide reductants and are assigned an “antioxidant” function [99–101]. More recently, Srx, a monothiol enzyme, was shown to reduce glutathionylated proteins.…”

Section: Leadmentioning

confidence: 99%

Biomedical Implications of Heavy Metals Induced Imbalances in Redox Systems

Sharma

Singh

Siddiqi

2014

BioMed Research International

323

221

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Several workers have extensively worked out the metal induced toxicity and have reported the toxic and carcinogenic effects of metals in human and animals. It is well known that these metals play a crucial role in facilitating normal biological functions of cells as well. One of the major mechanisms associated with heavy metal toxicity has been attributed to generation of reactive oxygen and nitrogen species, which develops imbalance between the prooxidant elements and the antioxidants (reducing elements) in the body. In this process, a shift to the former is termed as oxidative stress. The oxidative stress mediated toxicity of heavy metals involves damage primarily to liver (hepatotoxicity), central nervous system (neurotoxicity), DNA (genotoxicity), and kidney (nephrotoxicity) in animals and humans. Heavy metals are reported to impact signaling cascade and associated factors leading to apoptosis. The present review illustrates an account of the current knowledge about the effects of heavy metals (mainly arsenic, lead, mercury, and cadmium) induced oxidative stress as well as the possible remedies of metal(s) toxicity through natural/synthetic antioxidants, which may render their effects by reducing the concentration of toxic metal(s). This paper primarily concerns the clinicopathological and biomedical implications of heavy metals induced oxidative stress and their toxicity management in mammals.

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“…The endogenously produced hydrogen peroxide is reduced by reduced glutathione (GSH) in the presence of GSHPx (Świderska-Kołacz, Klusek, & Kołątaj, 2007). However, the intracellular GSH level is maintained in the reduced form by the NADPH-requiring enzyme glutathione reductase (Nagaoka, Iuchi, Ikeda, & Fujii, 2004). Therefore, changes in glutathione reductase activity are particularly important because the enzyme substitutes the reduced form of glutathione during NADPH oxidation, when high amounts of glutathione disulphide are formed in the cell.…”

Section: Blood Serum and Muscle Oxidative Statusmentioning

confidence: 99%