The DOI matches its Crossref record; 304 of the 308 references it cites were found in a registry or an index.
Pathophysiology of circulating xanthine oxidoreductase: New emerging roles for a multi-tasking enzyme
Open accessAbstract
The enzyme xanthine oxidoreductase (XOR) catalyses the last step of purine degradation in the highest uricotelic primates as a rate-limiting enzyme in nucleic acid catabolism. Although XOR has been studied for more than a century, this enzyme continues to arouse interest because its involvement in many pathological conditions is not completely known. XOR is highly evolutionarily conserved; moreover, its activity is very versatile and tuneable at multiple-levels and generates both oxidant and anti-oxidant products. This review covers the basic information on XOR biology that is essential to understand its enzymatic role in human pathophysiology and provides a comprehensive catalogue of the experimental and human pathologies associated with increased serum XOR levels. The production of radical species by XOR oxidase activity has been intensively studied and evaluated in recent decades in conjunction with the cytotoxic consequences and tissue injuries of various pathological conditions. More recently, a role has emerged for the activity of endothelium-bound enzymes in inducing the vascular response to oxidative stress, which includes the regulation of pro-inflammatory and pro-thrombotic activities of endothelial cells. The possible physiological functions of circulating XOR and the products of its enzyme activity are presented here together with their implications in cardiovascular and metabolic diseases.
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“The binding of plasma XO to ECs can lead to vascular dysfunction (45, 71, 562, 612, 1010).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [71]
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1 retracted
Aoki, N. (2006) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.60142 · Cited by 48 · cited 1×
“as a membrane-associated protein in the secretion of milk lipids during lactation in mice [87,88] (reviewed in [89]).”
BackgroundRetractedOxygen-Derived Free Radicals in Postischemic Tissue Injury
Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399 · cited 2×
“In particular, attention has been focused on the role of XOR-derived ROS in the pathogenesis of tissue lesions induced by reperfusion after ischaemia (reviewed in [16,146]).”
BackgroundEndothelial dysfunction in cardiovascular diseases: the role of oxidant stress
Cai, H., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.87.10.840 · Cited by 3,839
Ames, B. N., Cathcart, R., Schwiers, E., & Hochstein, P. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.11.6858 · Cited by 2,915 · cited 1×
“advantage for uricotelic primates over ureotelic mammals [36] (reviewed in [37]).”
BackgroundUric Acid and Cardiovascular Risk
Feig, D. I., Kang, D., & Johnson, R. J. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0800885 · Cited by 2,467
Elevated Uric Acid Increases Blood Pressure in the Rat by a Novel Crystal-Independent Mechanism
Mazzali, M., Hughes, J., Kim, Y.-G., Jefferson, J. A., Kang, D., GORDON, K. L., Lan, H. Y., Kivlighn, S. D., & Johnson, R. J. (2001) · Hypertension · doi:10.1161/hy1101.092839 · Cited by 1,298 · cited 1×
“either by inhibiting XOR activity, which produces uric acid, or by inducing uricosuria, which eliminates uric acid [281,282].”
BackgroundPacher, P., Nivorozhkin, A., & Szabó, C. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.1.6 · Cited by 1,218 · cited 3×
“same purpose, the XOR inhibitor allopurinol has been used in many experimental and clinical studies (reviewed in [150]).”
BackgroundInfluentialThe Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,196 · cited 1×
“When oxygen is the electron acceptor, the reaction occurs via a one-electron reduction, producing superoxide ions [13], and a two-electron reduction, generating hydrogen peroxide (reviewed in [12]).”
BackgroundA causal role for uric acid in fructose-induced metabolic syndrome
Nakagawa, T., Hu, H., Zharikov, S. I., Tuttle, K. R., Short, R., Glushakova, O. Y., Ouyang, X., Feig, D. I., Block, E. R., Herrera-Acosta, J., et al. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00140.2005 · Cited by 1,111 · cited 1×
“prevented with allopurinol or reversed with a uricosuric agent [284] (reviewed in [272,285]).”
BackgroundJohnson, R. J., Segal, M. S., Sautin, Y., Nakagawa, T., Feig, D. I., Kang, D.-H., Gersch, M. S., Benner, S., & Sánchez-Lozada, L. G. (2007) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/86.4.899 · Cited by 1,075
Research works printed but not linked: 1
- Nguyen, 1986, Plant xanthine dehydrogenase: its distribution, properties and function, Physiol. Vég., 24, 263
Cited by
Sorted by citations
Items 201–260 of 260
Kurajoh, M., Fukumoto, S., Akari, S., Murase, T., Nakamura, T., Ihara, Y., Imai, T., Nagata, Y., Morioka, T., Mori, K., et al. (2023) · IJC Heart & Vasculature · doi:10.1016/j.ijcha.2023.101264 · Cited by 3
“Although XOR is mainly expressed in the liver and intestines of humans [34,35], it leaks from cells in those organs and enters the circulation, then binds to sulphated glycosaminoglycans on the surface of endothelial cells, resulting in partial migration to intracellular compartments via endocytosis [7,8,36,37].”
BackgroundImplication of changes in xanthine oxidase activity following hemodialysis
Fujioka, H., Koike, T., Imamura, T., Kakeshita, K., Yamazaki, H., & Kinugawa, K. (2023) · BMC Nephrology · doi:10.1186/s12882-023-03062-z · Cited by 2
“Xanthine oxidase family is stored in the liver [2].”
BackgroundBedei, A., Cabrera, P. R., Oliveira, L., Castellini, L., Grazia, G. D., & Remiddi, S. (2025) · Clinical ophthalmology · doi:10.2147/opth.s480668 · Cited by 2
King, R. D., Chapa, M. G., Chen, I.-M. A., Giromini, A. G., Kelley, E. E., & Khoo, N. K. H. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.02.023 · Cited by 2
Griffith, J. A., Schafner, K. J., Garner, K. L., DeVallance, E., Lewis, S. E., Nurkiewicz, T. R., Kelley, E. E., Maxwell, B. A., Goldsmith, W. T., & Bowdridge, E. C. (2025) · Cardiovascular Toxicology · doi:10.1007/s12012-025-10022-6 · Cited by 2
Teimoori-Boghsani, Y., Bagherieh‐Najjar, M. B., & Mianabadi, M. (2018) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 2
Oki, R., Hamasaki, Y., Komaru, Y., Miyamoto, Y., Matsuura, R., Akari, S., Nakamura, T., Murase, T., Doi, K., & Nangaku, M. (2021) · Nephrology · doi:10.1111/nep.13983 · Cited by 2
“Hepatocellular damage caused by hypoxia, toxic agents and viral infection induces XOR release in blood.(7)”
BackgroundWatanabe, K., Arimoto, T., Watanabe, T., Otaki, Y., Murase, T., Nakamura, T., Kobayashi, Y., Aono, T., Saito, Y., Koyama, K., et al. (2023) · Journal of Cardiology · doi:10.1016/j.jjcc.2023.02.003 · Cited by 2
Pioglitazone‐induced alterations of purine metabolism in healthy male subjects
Kang, J.-H., Li, Y., Lee, S., Yu, K., & Cho, J. (2024) · Clinical and Translational Science · doi:10.1111/cts.13834 · Cited by 2
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Mansour, H. M. (2024) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-031-62131-4_2 · Cited by 1
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Alexandre, E. C., Curiel, A. A., Dias, J. M., Silva, F. H., Antunes, E., & de Oliveira, M. G. (2025) · Autonomic Neuroscience · doi:10.1016/j.autneu.2025.103355 · Cited by 1
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Goswami, S. K. (2019) · Springer eBooks · doi:10.1007/978-981-13-8946-7_17 · Cited by 1
Ghaeli, T., Karimi, B., Kojouri, G., DEHKORDI, R. R., & Ahadi, A. M. (2022) · Journal of Equine Veterinary Science · doi:10.1016/j.jevs.2022.104134 · Cited by 1
Xanthine oxidoreductase: structure, distribution and physioloical role
Александровна, Б. С., Mozgovaya, E. E., Сергеевна, С. С., Мамус, М. А., & Trofimenko, A. S. (2024) · Успехи физиологических наук · doi:10.31857/s0301179824030037 · Cited by 1
Panina, S., Krolevets, I. V., Milyutina, N. P., Ananyan, A. A., Zabrodin, M. A., & Внуков, В. В. (2018) · Clinical Medicine (Russian Journal) · doi:10.18821/0023-2149-2018-96-1-60-65 · Cited by 1
Heslinga, M., Nurmohamed, M. T., & Gerritsen, M. (2017) · Technical report · doi:10.1016/b978-0-12-803997-7.00018-1
Uric acid, blood pressure, and gout management
Scheepers (2017) · Research Publications (Maastricht University) · doi:10.26481/dis.20170707ls
“These ROS inhibit endothelial nitric oxide (NO) production and consequently impair the vasodilatory reaction.(8,10,11) In addition, the ROS produced by XO activity induce the adherence of leukocytes to endothelial cells, which in turn leads to more ROS generation and the initiation of proinflammatory events.”
BackgroundMethodHa, O., & Fasola, F. (2020) · American Journal of Laboratory Medicine · doi:10.11648/j.ajlm.20200502.13
“XO has the ability to stick to vascular cells because it binds to sulphated glycosaminoglycans on the endothelial cell surface which is heparin reversible in studies with cultured endothelial cells [26].”
BackgroundIn-Silico Analysis of Secondary Metabolites that Modulates Enzymes of Cholesterol TargetPreprint
Marahatha, R., Basnet, S., Bhattarai, B. R., Budhathoki, P., Aryal, B., Adhikari, B., Lamichhane, G., Poudel, D. K., & Parajuli, N. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.24.219998
“It is the rate-limiting enzyme involved in the catabolism of purine nucleotides, the step that oxidizes xanthine to uric acid [20], [21].”
BackgroundMozgovaya, E. E., Александровна, Б. С., Trofimenko, A. S., Мамус, М. А., Тихомирова, Е. А., Сергеевна, С. С., & Zborovskaya, I. A. (2020) · Современные проблемы науки и образования · doi:10.17513/spno.30171
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Kovalenko, Y. L., Melekhovets, O. K., & Melekhovets, Y. V. (2019) · Photobiology and Photomedicine · doi:10.26565/2076-0612-2019-28-01
Александровна, Б. С., Mozgovaya, E. E., Trofimenko, A. S., Мамус, М. А., Сергеевна, С. С., & Zborovskaya, I. A. (2021) · Современные проблемы науки и образования · doi:10.17513/spno.30783
“окислительный стресс, в том числе после гипоксии/реоксигенации и ишемии/реперфузии – процессов, наблюдаемых при РА [7].”
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Mozgovaya, E. E., Александровна, Б. С., Мамус, М. А., Trofimenko, A. S., & Сергеевна, С. С. (2021) · Siberian Journal of Life Sciences and Agriculture · doi:10.12731/2658-6649-2021-13-3-288-304
Okuyama, T., Shirakawa, J., Nakamura, T., Murase, T., Miyashita, D., Inoue, R., Kyohara, M., Togashi, Y., & Terauchi, Y. (2021) · Research Square · doi:10.21203/rs.3.rs-26599/v3
Okuyama, T., Shirakawa, J., Nakamura, T., Murase, T., Miyashita, D., Inoue, R., Kyohara, M., Togashi, Y., & Terauchi, Y. (2020) · Research Square · doi:10.21203/rs.3.rs-26599/v2
Uric Acid as a Predictor of Peripheral Arterial Disease as Indicated by Ankle Brachial Index
Mansour, H., Shahen, S., Sultan, H., AboElNeel, H. A., & Shehata, H. (2022) · The Egyptian Journal of Hospital Medicine · doi:10.21608/ejhm.2022.241952
“Uric acid has been assumed to have a role in the initiation of inflammation & the upsurge in oxidative stress because of its accumulation in the arterial wall & activation of the Xanthine Oxidoreductase (XOR) enzyme((4)).”
BackgroundSporadic amyotrophic lateral sclerosis: integral model of pathogenesis and therapy optionsPreprint
Doroshenko, O. (2022) · Research Square · doi:10.21203/rs.3.rs-1643391/v1
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Doroshenko, O. (2022) · Research Square · doi:10.21203/rs.3.rs-1643391/v2
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Babayemi, D. O. D. O., Adeyi, O. E., Akinhanmi, T. F., Onunkwor, B. O., Akamo, A. J., Akanni, O. I., Keyede, O. O., Adeleke, M. A., Michael, M. O., Idhove, F. E., et al. (2022) · Journal of Chemical Society of Nigeria · doi:10.46602/jcsn.v47i4.783
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Gajdán, N., & Ábrahám, G. (2022) · Cardiologia Hungarica · doi:10.26430/chungarica.2022.52.4.331
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Düğeroğlu, H., & Özgenoğlu, M. (2023) · Disease and Diagnosis · doi:10.34172/ddj.2023.490
“Ischemia or hypoxia may trigger severe sepsis and septic shock; this may further increase the conversion of xanthine/hypoxanthine to uric acid mediated by xanthine oxidase activation in microvascular endothelium (19,20).”
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Lin, Z., Xie, Y., Zhao, M.-C., Hou, P.-P., Tang, J., & Chen, G. (2021) · Figshare · doi:10.6084/m9.figshare.16590494
Lin, Z., Xie, Y., Zhao, M.-C., Hou, P.-P., Tang, J., & Chen, G. (2021) · Figshare · doi:10.6084/m9.figshare.16590497
Kataoka, N., & Imamura, T. (2024) · Journal of Arrhythmia · doi:10.1002/joa3.13047
Гуляев, А. Е., Sergazy, S., Urazbayeva, A., Shulgau, Z., & Бенберин, В. В. (2024) · Farmaciâ Kazahstana · doi:10.53511/pharmkaz.2024.93.64.013
Alotaibi, F. M., Almazam, . A., Alotaibi, ., Emam, . M., Alqahtani, . S., Alheggi, . I., Alanazi, . F., Alharbi, . K., Alhamed, . A., Ali, . I. A., et al. (2021) · International Journal of Health Sciences · doi:10.53730/ijhs.v5ns1.15088
“Non-enzymatic ROS sources include the mitochondrial respiratory chain, NADPH oxidase, XOR, uncoupled endothelial NOS, cytochrome P450 enzymes, lipoxygenase, and COX (Sena and Chandel, 2012; Battelli et al., 2014a).”
Kurajoh, M., Fukumoto, S., Akari, S., Nakamura, T., Miki, Y., Nagata, Y., Morioka, T., Mori, K., Imanishi, Y., Watanabe, T., et al. (2025) · Metabolism Open · doi:10.1016/j.metop.2025.100374
Marahatha, R., Basnet, S., Bhattarai, B. R., Budhathoki, P., Aryal, B., Adhikari, B., Lamichhane, G., Poudel, D. K., & Parajuli, N. (2021) · Figshare · doi:10.6084/m9.figshare.13514018
Lin, Z., Xie, Y., Zhao, M.-C., Hou, P.-P., Tang, J., & Chen, G. (2021) · Figshare · doi:10.6084/m9.figshare.16590491
Gao, L., Rafaels, N. M., Dudenkov, T. M., Damarla, M., Damico, R., Maloney, J. P., Moss, M., Martin, G. S., Sevransky, J., Shanholtz, C. B., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23640001
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“[13,14]”
Wang, Y., Xin, L., Ge, W., Yan, W., Su, Y., Hu, X., Liang, F., Xiao, Y., Fu, W., Han, D., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07914-8
“Additionally, urate production process also generates reactive oxygen species that can lead to oxidative stress, endothelial dysfunction, and impairments in cardiac and vascular functions [39, 40].”
Skinner, S. C. (2018) · theses.fr (ABES) · doi:10.70675/bad1111dz9f48z4cb3z82b1z01030b2c1ced
Li, R., Li, Y. H., Zhang, C. Y., Liu, H., Jiang, J., Yao, D., & Wei, X. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178917
Features of lipid peroxidation in patients with autoimmune thyroiditis under wartime conditions
Karachentsev, Y. I., Gopkalova, I., Dubovyk, V. M., Ashurov, E. M., & Герасименко, Л. В. (2026) · INTERNATIONAL JOURNAL OF ENDOCRINOLOGY (Ukraine) · doi:10.22141/2224-0721.22.3.2026.1704
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Hung, M.-Y., Li, C., Lee, H., Ke, H., Shiue, Y.-L., Yeh, H., Wu, W. J., Wei, Y., & Li, W.-M. (2026) · Discover Oncology · doi:10.1007/s12672-026-05270-z
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Pan, X., Pei, Z., Wu, J., Jiang, N., Li, Q., Yang, Y., Cao, J., Huang, Y., Sun, S., Du, Q., et al. (2026) · Advanced Science · doi:10.1002/advs.76726
Battelli, M. G., Bortolotti, M., Bolognesi, A., & Polito, L. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.08.007
Self-citationKhushal, A., Khan, S., Farooq, U., Khan, M. N., Hafeez, M., & Sarwar, R. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110441
Muwanguzi, D., Asmare, M. M., & Yun, S. (2026) · Research Square · doi:10.21203/rs.3.rs-10663484/v1
Experimental workflows for the accurate identification of mitochondrial redox events
Hernansanz‐Agustín, P., Bolaños, J. P., Borrás, C., Cabiscol, E., Campuzano, V., de Cubas, L., Enrı́quez, J. A., Fabregat, I., Gonfaus-Ortiz, G., Hidalgo, E., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104387
“XOR is ubiquitously expressed [106], although its highest expression and activity are found in the liver, small intestine, and lactating mammary glands [107].”
Li, N.-C., Xin, M.-L., Song, X., Wang, H.-Y., Yang, F.-Y., Li, J.-D., & Sun, W.-L. (2026) · Food & medicine homology. · doi:10.26599/fmh.2027.9420159
Kim, S., Ju, S., & Jung, Y. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18091187
“The gut is among the human organs with the highest XO activity, which increases further under inflammatory conditions [12–15].”
Design, Synthesis, and Bio‐Evaluation of Salicylic Acid Derivatives as Potent XO Inhibitor
Cao, Y., Liu, C., Hu, P., He, R., Lin, M., Zhang, C., Hong‐Lei, L. I., & Shi, D. (2026) · ChemistrySelect · doi:10.1002/slct.202505765
Metadata
- Authors
- Battelli, M. G., Bolognesi, A., & Polito, L.
- Affiliations
- University of Bologna (IT)
- Corresponding author
- Bolognesi, Andrea
- Polito, Letizia
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2014-09
- Volume
- 1842
- Issue
- 9
- Pages
- 1502-1517
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2073007450
- Cited by
- 256
- References
- 308
- Citations by year
- 2026: 15 · 2025: 10 · 2024: 23 · 2023: 29 · 2022: 20 · 2021: 30 · 2020: 30 · 2019: 24 · 2018: 20 · 2017: 21 · 2016: 16 · 2015: 17 · 2014: 1
- FWCI
- 2.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (submittedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by-nc-nd)
- Funders
- Alma Mater Studiorum‐University of Bologna
- Pallotti Legacies for Cancer Research
- Topics
- Health Sciences › Medicine › Nephrology › Gout, Hyperuricemia, Uric Acid
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- xanthine oxidoreductase, purine degradation, uric acid, oxidative stress, reactive oxygen species, endothelial cells, vascular response, inflammation, thrombosis, cardiovascular disease, metabolic disorders, serum enzyme levels
- MeSH terms
- Animals, Cardiovascular Diseases, Humans, Xanthine Dehydrogenase, Metabolic Syndrome
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