Liver xanthine dehydrogenase and iron mobilization

Topham, Richard W.; Walker, Mark C.; Calisch, Melissa P.

doi:10.1016/0006-291x(82)91910-6

Cited by 50 publications

(18 citation statements)

References 11 publications

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“…Ubiquitously distrib-*To whom all correspondence should be addressed: Byung Pal Yu, Ph.D. Department of Molecular Biology Pusan National University, Gumjung-ku, Pusan, Korea, 609-735 Telephone: 82-51-510-2212 Facsimile: 82-51-581-1509 E-mail: vubD @ hvowon.eusan.ac.kr uted, XDH and XOD are commonly known as the ratelimiting enzymes in nucleic acid degradation and purine catabolism. However, their wide involvement is also found in the antimicrobial activity in various tissues (2-4), in iron metabolism (5), and in the hepatic detoxification process (6). Furthermore, XDH and XOD are implicated in certain pathological conditions such as xanthinuria (7), ethanol toxicity (8), influenza virus infection (9), atherosclerosis (10), and gout (11).…”

Section: Introductionmentioning

confidence: 99%

Significance of hepatic xanthine oxidase and uric acid in aged and dietary restricted rats

Chung

2000

AGE

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Xanthine oxidase (XOD), one of the major intracellular sources of superoxide production, is well characterized as a causative factor in ischemia/ reperfusion related damage. In the present study, we investigated age-effect on the status of XOD, an enzyme interconvertible with xanthine dehydrogenase (XDH) under oxidative stress. We also examined the modulation of the enzyme using the antioxidative action of dietary restriction (DR). We obtained evidence showing XOD activity to be significantly increased by DR, peaking at 24 months, although no progressive, age-related changes were noticed. On the other hand, while XDH activity decreased in ad libitum fed rats with age, DR maintained higher activity levels at 18 and 24 months of age. During aging, the conversion of XDH to XOD was slightly increased, as indicated by the XOD/ XDH ratio. One novel finding of the present study is DR's ability to elevate the uric acid level, which likely augments the anti-oxidative defense system, thereby buffering against oxidatively stressed conditions during aging. Based on what is known about the antioxidative abilities of DR and uric acid, we propose that the high uric acid levels we observed in DR rats may well serve as part of a defense strategy to protect redox balance.

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Section: Introductionmentioning

confidence: 99%

Significance of hepatic xanthine oxidase and uric acid in aged and dietary restricted rats

Chung

2000

AGE

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“…It is of note that IRP 1 and 2 are redox-sensitive [43], meaning that sensing and control of free cytoplasmic iron is linked directly to the intracellular oxidant tension at the molecular level. Ferritin can store up to 4,500 atoms of ferric iron per molecule; mobilization of ferric iron requires reduction to ferrous iron and the superoxide radical has been shown to bring about release of iron from ferritin [44]. Sulfur amino acid deprivation (SAAD) increases oxidative stress through a decrease in cellular GSH content.…”

Section: Determinants Of Free Ironmentioning

confidence: 99%

Intravenous Iron: The Iatrogenic Kick to Lose Control over Oxygen?

Deicher

Hörl²

2002

Kidney Blood Press Res

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“…In addition to above prominent activities, an XOR-generated ROS are responsible for Iron mobilization from ferritin in the liver [63], iron absorption in the intestinal mucosal [64] and the induction of proliferation [65][66][67]. It was also postulated that free radical generation by XOR and various metabolic pathways in developmental animals believed to be influenced the development [3].…”

Section: Signal Transductionmentioning

confidence: 99%

Biochemical Role of Xanthine Oxidoreductase and Its Natural Inhibitors: An Overview

Mandava¹,

Batchu²

2016

Int J Pharm Pharm Sci

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Xanthine oxidoreductase (XOR) is a widely distributed housekeeping enzyme in mammals that catalyzes the last two steps in human purine catabolism to produce uric acid. The enzyme exists as a homodimer with independent electron transfer in each monomer. This has been studied extensively as a major constituent of the milk fat globule membrane (MFGM) which surrounds fat globules in cow's milk even though purine catabolism is the most accepted function of XOR. A huge number of literature highlights on the different catalytic forms of XOR and their importance in the generation of reactive oxygen species/reactive nitrogen species (ROS/RNS) and synthesis of uric acid which are involved in many physiological and pathological processes. However, a slight ambiguity resides in their biochemical functions. The aim of this article was to review the literature published on the structural, catalytical, physiological and pathological role of XOR and to resolve the ambiguity in biochemical processes and to firm up various natural inhibitors of XOR collectively. Uric acid, the product of purine catabolism shows antioxidant activity, and XOR-derived ROS and RNS play a role in innate immunity, milk secretion and also be involved in signaling and metabolism of xenobiotics. Furthermore, XOR is likely to be engaged in pathology because of excessive production of uric acid and ROS/RNS. This review also reports natural XOR inhibitors in plants which inhibit the enzyme to treat XOR associated pathology.

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Liver xanthine dehydrogenase and iron mobilization

Cited by 50 publications

References 11 publications

Significance of hepatic xanthine oxidase and uric acid in aged and dietary restricted rats

Significance of hepatic xanthine oxidase and uric acid in aged and dietary restricted rats

Intravenous Iron: The Iatrogenic Kick to Lose Control over Oxygen?

Biochemical Role of Xanthine Oxidoreductase and Its Natural Inhibitors: An Overview

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