Disulfide S-Monoxides Convert Xanthine Dehydrogenase into Oxidase in Rat Liver Cytosol More Potently Than Their Respective Disulfides

Sakuma, Satoru; Fujita, Junko; Nakanishi, Masahiko; Wada, Shun-ich; Fujimoto, Yohko

doi:10.1248/bpb.31.1013

Cited by 8 publications

(5 citation statements)

References 19 publications

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“…In creatures without mammals, XOR is found only as XDH form, which utilizes nicotinamide adenine dinucleotide (NAD + ) as an electron acceptor and does not produce reactive oxygen species (ROS), while in mammals, XOR is found not only as XDH form but also as XO form, which utilizes oxygen molecule as an electron acceptor and generates ROS such as superoxide anion radicals and hydrogen peroxide [ 12 ]. XDH and XO are single-gene products [ 13 ] and XDH→XO conversion is caused by disulfide compounds via reversible or nonreversible oxidation of the thiol group in XDH [ 14 ].…”

Section: Discussionmentioning

confidence: 99%

Relationship between Xanthine Oxidoreductase Redox and Oxidative Stress among Chronic Kidney Disease Patients

Terawaki

Hayashi

Murase³

et al. 2018

Oxidative Medicine and Cellular Longevity

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Xanthine oxidase (XO), an isoform of xanthine oxidoreductase (XOR), is thought to increase the cardiovascular burden among chronic kidney disease (CKD) patients via oxidative radical production. Plasma XOR redox, which is characterized by the ratio of XO to total XOR, changes under different oxidative conditions associated with kidney dysfunction. However, the relationship between plasma XOR redox and oxidative stress (OS) is unclear. Thus, we aimed to clarify whether OS is related to XOR redox. We used the redox state of human serum albumin (HSA) as a marker to investigate the status of OS in CKD patients. HSA is composed of human mercaptoalbumin (HMA), which possesses not oxidized cysteine residues, reversibly oxidized human nonmercaptoalbumin-1 (HNA-1), and strongly oxidized human nonmercaptoalbumin-2 (HNA-2). The subjects included 13 nondialysis patients (7 males and 6 females) with varying degrees of kidney function. We found that ƒ(HMA) was negatively (R = −0.692, P = 0.0071) and ƒ(HNA-1) was positively (R = 0.703, P = 0.0058) correlated with plasma XO/XOR. ƒ(HNA-2) showed no correlation with XO/XOR (R = 0.146, P = 0.6412), indicating that plasma XOR redox is not related to the irreversible oxidation of HSA. In conclusion, plasma XOR redox is closely related to HSA redox, particularly reversible oxidation of HSA.

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Section: Discussionmentioning

confidence: 99%

Relationship between Xanthine Oxidoreductase Redox and Oxidative Stress among Chronic Kidney Disease Patients

Terawaki

Hayashi

Murase³

et al. 2018

Oxidative Medicine and Cellular Longevity

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“…Sakuma et al reported that XDH → XO conversion is caused by disulfide compounds via reversible or non-reversible oxidation of thiol group in XDH [10]. Because thiol oxidation of serum albumin is enhanced in correlation with kidney dysfunction [4], plasma XO/XOR, which reflects XO/XOR of the capillary endothelium [11], might also be increased among advanced CKD patients.…”

Section: Introductionmentioning

confidence: 99%

The Relationship between Xanthine Oxidoreductase and Xanthine Oxidase Activities in Plasma and Kidney Dysfunction

Terawaki¹,

Murase²,

Nakajima³

et al. 2017

J Clin Exp Nephrol

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Background: Oxidative stress (OS) is thought to play a role in detrimental events among patients with chronic kidney disease (CKD). Although the mechanism of OS increases in CKD patients is unclear, it has been suggested that increased activity of xanthine oxidase (XO), the superoxideproducing form of xanthine oxidoreductase (XOR), plays a large role in enhancing OS. Therefore, we measured the activities of plasma XOR and XO among CKD patients.

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“…We have previously shown that the XO formed by the treatment of copper, zinc and selenium ions, peroxynitrite and disulfide S -monoxides is completely reconverted to XD by dithiothreitol (DTT), a sulfhydryl reagent. (6,15,17) Thus, in an attempt to clarify the mechanism by which TAA converts XD into XO, we examined the effect of DTT on XO converted from XD by TAA (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

“…(15–17) The activities of XD and XO were assayed by monitoring uric acid formation using the HPLC method. XO activity was determined by measuring uric acid formation in the absence of NAD + .…”

Section: Methodsmentioning

confidence: 99%

All-trans Arachidonic acid generates reactive oxygen species via xanthine dehydrogenase/xanthine oxidase interconversion in the rat liver cytosol in vitro

Sakuma

Kitamura

Kuroda

et al. 2012

J. Clin. Biochem. Nutr.

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We previously reported that the all-cis isomer of arachidonic acid, the most naturally occurring isoform of this fatty acid, reduced cuprous copper ion-induced conversion of xanthine dehydrogenase into its reactive oxygen species generating form, xanthine oxidase. In the present study, the effects of all-trans isomer of arachidonic acid, in comparison with cis isomer of arachidonic acid, on the xanthine dehydrogenase/xanthine oxidase interconversion were explored. cis isomer of arachidonic acid alone did not have any significant effect on the activities of xanthine dehydrogenase and xanthine oxidase, but it inhibited the cuprous copper ion-induced conversion of xanthine dehydrogenase to xanthine oxidase in rat liver cytosol in vitro. In contrast, trans isomer of arachidonic acid elicited an increase in xanthine oxidase activity concomitant with a decrease in xanthine dehydrogenase activity, and further potentiated the cuprous copper ion-induced xanthine dehydrogenase/xanthine oxidase interconversion. In primary rat hepatocyte cultures, trans isomer of arachidonic acid increased 2',7'-dichlorofluorescein-fluorescence intensity in the cytosolic fraction from 2',7'-dichlorodihydrofluorescein, an indicator of reactive oxygen species generation. The pretreatment of allopurinol, an xanthine oxidase inhibitor, diminished the trans isomer of arachidonic acid-induced increase in the 2',7'-dichlorofluorescein-fluorescence intensity, indicating the role of xanthine dehydrogenase/xanthine oxidase in mediating trans isomer of arachidonic acid-induced reactive oxygen species generation. These observations suggest that, in contrast to all-cis arachidonic acid, all-trans arachidonic acid has the potential to enhance reactive oxygen species generation via xanthine dehydrogenase/xanthine oxidase interconversion in the liver cytosol in vitro.

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Disulfide S-Monoxides Convert Xanthine Dehydrogenase into Oxidase in Rat Liver Cytosol More Potently Than Their Respective Disulfides

Cited by 8 publications

References 19 publications

Relationship between Xanthine Oxidoreductase Redox and Oxidative Stress among Chronic Kidney Disease Patients

Relationship between Xanthine Oxidoreductase Redox and Oxidative Stress among Chronic Kidney Disease Patients

The Relationship between Xanthine Oxidoreductase and Xanthine Oxidase Activities in Plasma and Kidney Dysfunction

All-trans Arachidonic acid generates reactive oxygen species via xanthine dehydrogenase/xanthine oxidase interconversion in the rat liver cytosol in vitro

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