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Gene Review

Uox  -  urate oxidase

Rattus norvegicus

Synonyms: UOX-2, Urate oxidase, Uri, Uri2, Uricase
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Disease relevance of Uox


High impact information on Uox


Chemical compound and disease context of Uox


Biological context of Uox

  • The deduced amino acid sequence of rat liver uricase shares 40% homology with that of soybean nodulin-specific uricase and has an N-terminal extension of 7 amino acids [14].
  • In contrast, soybean uricase has a C-terminal extension of 12 amino acids, which is presumably the result of local gene duplication [14].
  • A 867-base open reading frame coding for 289 amino acids, corresponding to a molecular mass of 33,274 daltons, was confirmed by matching eight sequences of a total of 53 amino acids from peptide sequence analyses of the fragments generated by lysyl endopeptidase digestion of purified rat liver uricase [14].
  • The uricase gene was isolated from rat genomic DNA libraries [15].
  • The organization of the rat uricase gene is so greatly different from that of the soybean gene that the difference may not have been caused only by the removal of some ancestral introns during the period of widely separated evolution [16].

Anatomical context of Uox

  • A cDNA clone for rat liver uricase (EC, which is localized in the core of peroxisomes, was isolated from a rat liver cDNA library in lambda gt11 [17].
  • Uricase and catalase were immunoprecipitable from translation products directed by free polysomes or phenol-extracted free polysomal mRNA but not from products of membrane-bound polysomes [8].
  • The functionally of this human ACOX promoter was further demonstrated by linking it to a beta-galactosidase reporter gene or to a rat urate oxidase cDNA and establishing stably transfected African green monkey kidney (CV1) cell lines expressing reporter protein [18].
  • These studies demonstrate that the renal cortical plasma membranes contain urate-binding proteins, which have some functional and immunological homology to the hepatic peroxisomal core protein, uricase [19].
  • Immunostaining of 1-micron sections with the antibody against uricase followed by protein A-gold-silver showed fine granules in hepatocytes, which exhibited distinct fluorescence when examined in a microscope equipped with epifluorescence illumination [20].

Associations of Uox with chemical compounds


Other interactions of Uox

  • The 5'-flanking region of the UOX gene reveals a sequence, TTAGTAATT at nt -276 from the tsp, which appears to be complementary to the underlined part of the liver-specific LF-B1/HNF-1 consensus sequence, GTTAATNATTAAC (where N = A, C, T, G or no nt) [24].
  • Mitochondrial glutamate dehydrogenase and peroxisomal urate oxidase reached maximal activities per g of liver at two and five weeks of age, respectively [25].
  • During in vitro studies, 1 mmol/L AA-193 had no effect on liver uricase activity and 0.2 mmol/L AA-193 did not inhibit xanthine dehydrogenase activity [26].
  • One group consisted of oxidoreductases, including ceruloplasmin, uricase, branched-chain alpha-keto acid dehydrogenase, NADH ubiquinone oxidoreductase, P450, NAD+-isocitrate dehydrogenase, and cytochrome c oxidase, which may be related to ethanol-induced oxidative stress [27].
  • Cold exposure increases the oxidative capacity of the whole peroxisomal compartment; in the Pe fraction the palmitoyl-CoA oxidase and uricase specific activity ratio is constant (about 0.1), during cold exposure, but in the sPe fraction this ratio increases significantly (from 0.05 to 0.09) [28].

Analytical, diagnostic and therapeutic context of Uox

  • Isolation and sequence determination of a cDNA clone for rat peroxisomal urate oxidase: liver-specific expression in the rat [21].
  • Identification of an amino acid residue involved in the substrate-binding site of rat liver uricase by site-directed mutagenesis [22].
  • Immunofluorescence and electron microscopic examination revealed that the overexpressed recombinant urate oxidase is present in both the cytoplasm and the nucleus of infected insect cells as numerous 1- to 3-microns discrete particles [1].
  • Since the antibody that reacts with the affinity-purified urate-binding proteins on Western blot selectively inhibits urate transport in intact membrane vesicles, it is concluded that at least one of the affinity-purified urate-binding proteins is a uricase-like urate transporter [19].
  • Northern blot analysis revealed a 1.3-kb transcript and immunoblot analysis confirmed the presence of urate oxidase in the stably transfected cells [4].


  1. Rat urate oxidase produced by recombinant baculovirus expression: formation of peroxisome crystalloid core-like structures. Alvares, K., Widrow, R.J., Abu-Jawdeh, G.M., Schmidt, J.V., Yeldandi, A.V., Rao, M.S., Reddy, J.K. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  2. A role for uric acid in the progression of renal disease. Kang, D.H., Nakagawa, T., Feng, L., Watanabe, S., Han, L., Mazzali, M., Truong, L., Harris, R., Johnson, R.J. J. Am. Soc. Nephrol. (2002) [Pubmed]
  3. Hyperuricemia exacerbates chronic cyclosporine nephropathy. Mazzali, M., Kim, Y.G., Suga, S., Gordon, K.L., Kang, D.H., Jefferson, J.A., Hughes, J., Kivlighn, S.D., Lan, H.Y., Johnson, R.J. Transplantation (2001) [Pubmed]
  4. Functional expression and peroxisomal targeting of rat urate oxidase in monkey kidney cells. Yeldandi, A.V., Chu, R., Reddy, S.K., Pan, J., Usuda, N., Lin, Y., Rao, M.S., Reddy, J.K. Gene Expr. (1995) [Pubmed]
  5. Experimental meningitis in the rat: protection by uric acid at human physiological blood concentrations. Kastenbauer, S., Koedel, U., Becker, B.F., Pfister, H.W. Eur. J. Pharmacol. (2001) [Pubmed]
  6. Induction and origin of hepatocytes in rat pancreas. Reddy, J.K., Rao, M.S., Qureshi, S.A., Reddy, M.K., Scarpelli, D.G., Lalwani, N.D. J. Cell Biol. (1984) [Pubmed]
  7. Structure, composition, physical properties, and turnover of proliferated peroxisomes. A study of the trophic effects of Su-13437 on rat liver. Leighton, F., Coloma, L., Koenig, C. J. Cell Biol. (1975) [Pubmed]
  8. Biogenesis of peroxisomes: intracellular site of synthesis of catalase and uricase. Goldman, B.M., Blobel, G. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  9. Alterations of renal function during dietary-induced hyperuricemia in the rat. Spencer, H.W., Yarger, W.E., Robinson, R.R. Kidney Int. (1976) [Pubmed]
  10. Hypouricemic effect of the novel xanthine oxidase inhibitor, TEI-6720, in rodents. Osada, Y., Tsuchimoto, M., Fukushima, H., Takahashi, K., Kondo, S., Hasegawa, M., Komoriya, K. Eur. J. Pharmacol. (1993) [Pubmed]
  11. Synthesis and structure-activity relationships of 1-phenylpyrazoles as xanthine oxidase inhibitors. Ishibuchi, S., Morimoto, H., Oe, T., Ikebe, T., Inoue, H., Fukunari, A., Kamezawa, M., Yamada, I., Naka, Y. Bioorg. Med. Chem. Lett. (2001) [Pubmed]
  12. Degradation of low molecular weight uremic solutes by oral delivery of encapsulated enzymes. O'Loughlin, J.A., Bruder, J.M., Lysaght, M.J. ASAIO journal (American Society for Artificial Internal Organs : 1992) (2004) [Pubmed]
  13. Regulation of purine nucleotide metabolism in hypoxic liver and intestine of rats: radical scavenging effects of allopurinol and oxypurinol. Gerber, G., Siems, W., Werner, A., Stoesser, R., Foeldes-Papp, Z., Kowalewski, J., Schneider, W., Grune, T. Adv. Exp. Med. Biol. (1989) [Pubmed]
  14. Cloning and sequence analysis of cDNA for rat liver uricase. Motojima, K., Kanaya, S., Goto, S. J. Biol. Chem. (1988) [Pubmed]
  15. Structural analysis of the gene encoding rat uricase. Ito, M., Nakamura, M., Ogawa, H., Kato, S., Takagi, Y. Genomics (1991) [Pubmed]
  16. Organization of rat uricase chromosomal gene differs greatly from that of the corresponding plant gene. Motojima, K., Goto, S. FEBS Lett. (1990) [Pubmed]
  17. Nucleotide sequence of cDNA and predicted amino acid sequence of rat liver uricase. Ito, M., Suzuki, M., Takagi, Y. Eur. J. Biochem. (1988) [Pubmed]
  18. Identification of a peroxisome proliferator-responsive element upstream of the human peroxisomal fatty acyl coenzyme A oxidase gene. Varanasi, U., Chu, R., Huang, Q., Castellon, R., Yeldandi, A.V., Reddy, J.K. J. Biol. Chem. (1996) [Pubmed]
  19. Isolation and immunolocalization of a rat renal cortical membrane urate transporter. Knorr, B.A., Lipkowitz, M.S., Potter, B.J., Masur, S.K., Abramson, R.G. J. Biol. Chem. (1994) [Pubmed]
  20. Localization of urate oxidase in the crystalline cores of rat liver peroxisomes by immunocytochemistry and immunoblotting. Völkl, A., Baumgart, E., Fahimi, H.D. J. Histochem. Cytochem. (1988) [Pubmed]
  21. Isolation and sequence determination of a cDNA clone for rat peroxisomal urate oxidase: liver-specific expression in the rat. Reddy, P.G., Nemali, M.R., Reddy, M.K., Reddy, M.N., Yuan, P.M., Yuen, S., Laffler, T.G., Shiroza, T., Kuramitsu, H.K., Usuda, N. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  22. Identification of an amino acid residue involved in the substrate-binding site of rat liver uricase by site-directed mutagenesis. Ito, M., Kato, S., Nakamura, M., Go, M., Takagi, Y. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  23. NO2 reactive absorption substrates in rat pulmonary surface lining fluids. Postlethwait, E.M., Langford, S.D., Jacobson, L.M., Bidani, A. Free Radic. Biol. Med. (1995) [Pubmed]
  24. Rat urate oxidase: cloning and structural analysis of the gene and 5'-flanking region. Wang, X.D., Kawano, H., Alvares, K., Reddy, P.G., Getto, H., Rao, M.S., Reddy, J.K. Gene (1991) [Pubmed]
  25. Postnatal development of peroxisomal and mitochondrial enzymes in rat liver. Krahling, J.B., Gee, R., Gauger, J.A., Tolbert, N.E. J. Cell. Physiol. (1979) [Pubmed]
  26. Hypouricemic and uricosuric actions of AA-193 in a hyperuricemic rat model. Dan, T., Yoneya, T., Onoma, M., Onuma, E., Ozawa, K. Metab. Clin. Exp. (1994) [Pubmed]
  27. Microarray analysis of gene expression in rat hippocampus after chronic ethanol treatment. Saito, M., Smiley, J., Toth, R., Vadasz, C. Neurochem. Res. (2002) [Pubmed]
  28. Morphological and functional modifications of rat liver peroxisomal subpopulations during cold exposure. Goglia, F., Liverini, G., Lanni, A., Iossa, S., Barletta, A. Experimental biology. (1989) [Pubmed]
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