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Gene Review

DUOX2  -  dual oxidase 2

Homo sapiens

Synonyms: Dual oxidase 2, LNOX2, Large NOX 2, Long NOX 2, NADH/NADPH thyroid oxidase p138-tox, ...
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Disease relevance of DUOX2


Psychiatry related information on DUOX2

  • Our observations suggest that Duox1 and Duox2 are novel H2O2 sources that can support LPO-mediated antimicrobial defense mechanisms on mucosal surfaces [6].

High impact information on DUOX2

  • By data mining of a massively parallel signature sequencing tissue expression data base, we identified an uncharacterized gene named DUOX maturation factor (DUOXA2) arranged head-to-head to and co-expressed with DUOX2 [1].
  • Dual oxidase 2 (DUOX2), an NADPH:O(2) oxidoreductase flavoprotein, is a component of the thyroid H(2)O(2) generator crucial for hormone synthesis at the apical membrane [1].
  • Duox2 (and probably Duox1) is a glycoflavoprotein involved in thyroid hormone biosynthesis, as the thyroid H2O2 generator functionally associated with Tpo (thyroperoxidase) [7].
  • Using a spin-trapping technique combined with electron paramagnetic resonance spectroscopy, we confirmed this result but also demonstrated that the partially glycosylated form of Duox2, located in the endoplasmic reticulum, generates superoxide in a calcium-dependent manner [7].
  • These results suggest that post-translational modifications during the maturation process of Duox2 could be implicated in the mechanism of H2O2 formation by favoring intramolecular superoxide dismutation [7].

Chemical compound and disease context of DUOX2


Biological context of DUOX2

  • METHODS: We studied the complete coding sequence of the human DUOX2 gene by single-strand conformational polymorphism (SSCP) analysis of DNA from 17 unrelated patients with iodide organification defects [4].
  • Both siblings resulted compound heterozygotes for two novel DUOX2 variants, a nonsense mutation (c.2524C>T, p.Arg842X) and a missense substitution (c.1126C>T, p.Arg376Trp), undetected in 140 control alleles [3].
  • Different neonatal iodine supply apparently acted as disease modifier, justifying the discrepant results at TSH screening in the two siblings with same DUOX2 genotype and suggesting that mild dyshormonogenic defects may remain undisclosed in areas characterized by elevated iodine intake [3].
  • The function of DUOX2 in thyroid hormonogenesis has been firmly established by linking the congenital hypothyroid phenotype "total iodide organification defect" to biallelic inactivating DUOX2 mutations [9].
  • In addition, missense mutations of four cysteines (Cys-351, -370, -568, or -582) completely inhibited the emergence of pig Duox2-Q686X from the ER compartment, indicating their importance in Duox2 maturation [10].

Anatomical context of DUOX2


Associations of DUOX2 with chemical compounds

  • CONCLUSIONS: Two previously unknown compound heterozygous mutations in the DUOX2 gene, p.Q36H/p.S965fsX994 and p.G418fsX482/g.IVS19-2A>C, are responsible for iodide organification defects in 2 unrelated families [4].
  • Carbohydrate content analysis revealed that complex type-specific Golgi apparatus (GA) oligosaccharides were present on pig Duox2-Q686X, whereas human truncated Duox2 carried only high mannose-type sugar chains characteristic of the ER [10].
  • BACKGROUND: Iodide organification defects are associated with mutations in the dual oxidase 2 (DUOX2) gene and are characterized by a positive perchlorate discharge test [4].
  • Increasing evidence supports the hypothesis that the dual function NAD(P)H oxidases/peroxidases, Duox1 and Duox2, are important sources of regulated H2O2 production in respiratory tract epithelium [5].
  • Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium [5].

Other interactions of DUOX2

  • A Ca2+/NADPH-dependent H2O2-generating system was associated with Duox2 protein expression, which had the same biochemical characteristics as the NADPH oxidase in the thyroid [11].

Analytical, diagnostic and therapeutic context of DUOX2

  • Northern blot analysis of 23 different human tissues demonstrated that LNOX2 messenger RNA (mRNA) is strongly expressed only in the thyroid gland, although blast analysis of expressed sequence tags databases indicated that LNOX genes are also expressed in some nonthyroid cells [12].
  • Western blot analysis identified Duox2 as the same two molecular species (M(r) 165 and 175 kDa) as detected in the thyroid [11].
  • Accordingly, we examined Duox1 and Duox2 mRNA expression by real-time PCR in primary respiratory tract epithelial cultures after treatment with multiple cytokines [5].


  1. Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. Grasberger, H., Refetoff, S. J. Biol. Chem. (2006) [Pubmed]
  2. Expression of nicotinamide adenine dinucleotide phosphate oxidase flavoprotein DUOX genes and proteins in human papillary and follicular thyroid carcinomas. Lacroix, L., Nocera, M., Mian, C., Caillou, B., Virion, A., Dupuy, C., Filetti, S., Bidart, J.M., Schlumberger, M. Thyroid (2001) [Pubmed]
  3. Persistent mild hypothyroidism associated with novel sequence variants of the DUOX2 gene in two siblings. Vigone, M.C., Fugazzola, L., Zamproni, I., Passoni, A., Di Candia, S., Chiumello, G., Persani, L., Weber, G. Hum. Mutat. (2005) [Pubmed]
  4. Three mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A>C) in the dual oxidase 2 gene responsible for congenital goiter and iodide organification defect. Varela, V., Rivolta, C.M., Esperante, S.A., Gruñeiro-Papendieck, L., Chiesa, A., Targovnik, H.M. Clin. Chem. (2006) [Pubmed]
  5. Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium. Harper, R.W., Xu, C., Eiserich, J.P., Chen, Y., Kao, C.Y., Thai, P., Setiadi, H., Wu, R. FEBS Lett. (2005) [Pubmed]
  6. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. Geiszt, M., Witta, J., Baffi, J., Lekstrom, K., Leto, T.L. FASEB J. (2003) [Pubmed]
  7. Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. Ameziane-El-Hassani, R., Morand, S., Boucher, J.L., Frapart, Y.M., Apostolou, D., Agnandji, D., Gnidehou, S., Ohayon, R., Noël-Hudson, M.S., Francon, J., Lalaoui, K., Virion, A., Dupuy, C. J. Biol. Chem. (2005) [Pubmed]
  8. Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. Moreno, J.C., Bikker, H., Kempers, M.J., van Trotsenburg, A.S., Baas, F., de Vijlder, J.J., Vulsma, T., Ris-Stalpers, C. N. Engl. J. Med. (2002) [Pubmed]
  9. Physiology and Pathophysiology of the DUOXes. Ris-Stalpers, C. Antioxid. Redox Signal. (2006) [Pubmed]
  10. Targeting of the dual oxidase 2 N-terminal region to the plasma membrane. Morand, S., Agnandji, D., Noel-Hudson, M.S., Nicolas, V., Buisson, S., Macon-Lemaitre, L., Gnidehou, S., Kaniewski, J., Ohayon, R., Virion, A., Dupuy, C. J. Biol. Chem. (2004) [Pubmed]
  11. Dual oxidase2 is expressed all along the digestive tract. El Hassani, R.A., Benfares, N., Caillou, B., Talbot, M., Sabourin, J.C., Belotte, V., Morand, S., Gnidehou, S., Agnandji, D., Ohayon, R., Kaniewski, J., Noël-Hudson, M.S., Bidart, J.M., Schlumberger, M., Virion, A., Dupuy, C. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  12. Expression of reduced nicotinamide adenine dinucleotide phosphate oxidase (ThoX, LNOX, Duox) genes and proteins in human thyroid tissues. Caillou, B., Dupuy, C., Lacroix, L., Nocera, M., Talbot, M., Ohayon, R., Dème, D., Bidart, J.M., Schlumberger, M., Virion, A. J. Clin. Endocrinol. Metab. (2001) [Pubmed]
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