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Gene Review

DUOX1  -  dual oxidase 1

Homo sapiens

Synonyms: DUOX, Dual oxidase 1, LNOX1, Large NOX 1, Long NOX 1, ...
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Disease relevance of DUOX1


Psychiatry related information on DUOX1

  • 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 DUOX1


Chemical compound and disease context of DUOX1


Biological context of DUOX1


Anatomical context of DUOX1

  • So far, because of the impairment of maturation and of the targeting process, transfecting DUOX into nonthyroid cell lines has not led to the expression of a functional H2O2-generating system at the plasma membrane [13].
  • Since it was found in the intestine, duodenum, and colon, in addition to thyroid, we suggest that it be called LNOX, the new family of long homologs of NOX flavoproteins rather than THOX and/or DUOX [14].
  • It has been proposed that DUOX retention in the endoplasmatic reticulum (ER) of heterologous systems is due to the lack of an unidentified component required for functional maturation of the enzyme [2].
  • Furthermore, we detected Duox1-dependent H2O2 release by cultured human bronchial epithelial cells [6].
  • We examined Duox1 and Duox2 expression in secretory glands and on mucosal surfaces and give evidence for their presence and activity in salivary glands, rectum, trachea, and bronchium [6].

Associations of DUOX1 with chemical compounds

  • Duox2 (and probably Duox1) is a glycoflavoprotein involved in thyroid hormone biosynthesis, as the thyroid H2O2 generator functionally associated with Tpo (thyroperoxidase) [13].
  • The particulate fractions of these cells stably or transiently transfected with human or porcine DUOX cDNA demonstrate a functional NADPH/Ca2+-dependent H2O2-generating activity [13].
  • The level of THOX2 mRNA was increased by cAMP in these cells and it was decreased in the thyroids of rats treated with the antithyroid drug methimazole, unlike the TPO and NIS mRNAs [14].
  • ThOX proteins (thyroid oxidase) also called Duox are believed to be responsible for H(2)O(2) generation [15].
  • Expression of reduced nicotinamide adenine dinucleotide phosphate oxidase (ThoX, LNOX, Duox) genes and proteins in human thyroid tissues [4].
  • Although the activation domain of Noxa1 was not required for Duox function, mutation of a proline-rich domain in the Duox C terminus, a potential interaction motif for the Noxa1 Src homology domain 3, caused up-regulation of basal and stimulated H2O2 production [16].

Other interactions of DUOX1

  • In the 10 paired samples, variations of DUOX and TPO gene expressions were not correlated [1].
  • EFP1 and Duox mRNA share similar distribution in nine different tissues [15].
  • However, no functional DUOX-based NADPH oxidase has ever been reconstituted at the plasma membrane of transfected cells [2].
  • 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 [2].
  • Homologues of gp91phox, called Nox and Duox, are present in a large variety of non-phagocytic cells [17].

Analytical, diagnostic and therapeutic context of DUOX1

  • To investigate the source of H(2)O(2) produced by airway epithelia, PCR was used to screen nicotinamide adenine dinucleotide phosphate (NADPH) oxidase expression in human airway epithelia redifferentiated at the air-liquid interface (ALI) and demonstrated the presence of Duox1 and 2 [11].
  • Western blots of culture extracts indicated strong expression of Duox, and immunohistochemistry of human tracheal sections localized the protein to the apical portion of epithelial cells [11].


  1. 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]
  2. Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. Grasberger, H., Refetoff, S. J. Biol. Chem. (2006) [Pubmed]
  3. Correlation between the loss of thyroglobulin iodination and the expression of thyroid-specific proteins involved in iodine metabolism in thyroid carcinomas. Gérard, A.C., Daumerie, C., Mestdagh, C., Gohy, S., De Burbure, C., Costagliola, S., Miot, F., Nollevaux, M.C., Denef, J.F., Rahier, J., Franc, B., De Vijlder, J.J., Colin, I.M., Many, M.C. J. Clin. Endocrinol. Metab. (2003) [Pubmed]
  4. 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]
  5. Dual oxidase 1 and 2 expression in airway epithelium of smokers and patients with mild/moderate chronic obstructive pulmonary disease. Nagai, K., Betsuyaku, T., Suzuki, M., Nasuhara, Y., Kaga, K., Kondo, S., Nishimura, M. Antioxid. Redox Signal. (2008) [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. Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. Edens, W.A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J.M., Lee, T., Edens, H.A., Tang, X., Sullards, C., Flaherty, D.B., Benian, G.M., Lambeth, J.D. J. Cell Biol. (2001) [Pubmed]
  8. Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells. Shao, M.X., Nadel, J.A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  9. Airway Epithelial Cell Migration and Wound Repair by ATP-mediated Activation of Dual Oxidase 1. Wesley, U.V., Bove, P.F., Hristova, M., McCarthy, S., van der Vliet, A. J. Biol. Chem. (2007) [Pubmed]
  10. 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]
  11. Regulated hydrogen peroxide production by Duox in human airway epithelial cells. Forteza, R., Salathe, M., Miot, F., Forteza, R., Conner, G.E. Am. J. Respir. Cell Mol. Biol. (2005) [Pubmed]
  12. RNA interference of dual oxidase in the plant nematode Meloidogyne incognita. Bakhetia, M., Charlton, W., Atkinson, H.J., McPherson, M.J. Mol. Plant Microbe Interact. (2005) [Pubmed]
  13. 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]
  14. Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5. Dupuy, C., Pomerance, M., Ohayon, R., Noël-Hudson, M.S., Dème, D., Chaaraoui, M., Francon, J., Virion, A. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  15. Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. Wang, D., De Deken, X., Milenkovic, M., Song, Y., Pirson, I., Dumont, J.E., Miot, F. J. Biol. Chem. (2005) [Pubmed]
  16. Inhibitory action of NoxA1 on dual oxidase activity in airway cells. Pacquelet, S., Lehmann, M., Luxen, S., Regazzoni, K., Frausto, M., Noack, D., Knaus, U.G. J. Biol. Chem. (2008) [Pubmed]
  17. The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Vignais, P.V. Cell. Mol. Life Sci. (2002) [Pubmed]
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