DUOX2

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Dual oxidase 2
Identifiers
Symbols DUOX2 ; LNOX2; NOXEF2; P138-TOX; THOX2
External IDs Template:OMIM5 Template:MGI HomoloGene9689
RNA expression pattern
PBB GE DUOX2 219727 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Dual oxidase 2, also known as DUOX2, is a human gene.[1]

The protein encoded by this gene is a glycoprotein and a member of the NADPH oxidase family. The synthesis of thyroid hormone is catalyzed by a protein complex located at the apical membrane of thyroid follicular cells. This complex contains an iodide transporter, thyroperoxidase, and a peroxide generating system that includes this encoded protein and DUOX1. This protein is known as dual oxidase because it has both a peroxidase homology domain and a gp91phox domain.[1]

References

  1. 1.0 1.1 "Entrez Gene: DUOX2 dual oxidase 2".

Further reading

  • Lambeth JD (2002). "Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases". Curr. Opin. Hematol. 9 (1): 11–7. PMID 11753072.
  • Moreno JC, Visser TJ (2007). "New phenotypes in thyroid dyshormonogenesis: hypothyroidism due to DUOX2 mutations". Endocrine development. 10: 99–117. doi:10.1159/0000106822. PMID 17684392.
  • Dupuy C, Ohayon R, Valent A; et al. (2000). "Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cdnas". J. Biol. Chem. 274 (52): 37265–9. PMID 10601291.
  • Dias Neto E, Correa RG, Verjovski-Almeida S; et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. PMID 10737800.
  • De Deken X, Wang D, Many MC; et al. (2000). "Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family". J. Biol. Chem. 275 (30): 23227–33. doi:10.1074/jbc.M000916200. PMID 10806195.
  • Dupuy C, Pomerance M, Ohayon R; et al. (2000). "Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5". Biochem. Biophys. Res. Commun. 277 (2): 287–92. doi:10.1006/bbrc.2000.3671. PMID 11032719.
  • Caillou B, Dupuy C, Lacroix L; et al. (2001). "Expression of reduced nicotinamide adenine dinucleotide phosphate oxidase (ThoX, LNOX, Duox) genes and proteins in human thyroid tissues". J. Clin. Endocrinol. Metab. 86 (7): 3351–8. PMID 11443211.
  • Edens WA, Sharling L, Cheng G; et al. (2001). "Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox". J. Cell Biol. 154 (4): 879–91. doi:10.1083/jcb.200103132. PMID 11514595.
  • Lacroix L, Nocera M, Mian C; et al. (2002). "Expression of nicotinamide adenine dinucleotide phosphate oxidase flavoprotein DUOX genes and proteins in human papillary and follicular thyroid carcinomas". Thyroid. 11 (11): 1017–23. doi:10.1089/105072501753271699. PMID 11762710.
  • De Deken X, Wang D, Dumont JE, Miot F (2002). "Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system". Exp. Cell Res. 273 (2): 187–96. doi:10.1006/excr.2001.5444. PMID 11822874.
  • Moreno JC, Bikker H, Kempers MJ; et al. (2002). "Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism". N. Engl. J. Med. 347 (2): 95–102. doi:10.1056/NEJMoa012752. PMID 12110737.
  • Geiszt M, Witta J, Baffi J; et al. (2003). "Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense". FASEB J. 17 (11): 1502–4. doi:10.1096/fj.02-1104fje. PMID 12824283.
  • Pachucki J, Wang D, Christophe D, Miot F (2004). "Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions". Mol. Cell. Endocrinol. 214 (1–2): 53–62. doi:10.1016/j.mce.2003.11.026. PMID 15062544.
  • Morand S, Agnandji D, Noel-Hudson MS; et al. (2004). "Targeting of the dual oxidase 2 N-terminal region to the plasma membrane". J. Biol. Chem. 279 (29): 30244–51. doi:10.1074/jbc.M405406200. PMID 15150274.
  • Schwarzer C, Machen TE, Illek B, Fischer H (2004). "NADPH oxidase-dependent acid production in airway epithelial cells". J. Biol. Chem. 279 (35): 36454–61. doi:10.1074/jbc.M404983200. PMID 15210697.
  • Wang D, De Deken X, Milenkovic M; et al. (2005). "Identification of a novel partner of duox: EFP1, a thioredoxin-related protein". J. Biol. Chem. 280 (4): 3096–103. doi:10.1074/jbc.M407709200. PMID 15561711.
  • El Hassani RA, Benfares N, Caillou B; et al. (2005). "Dual oxidase2 is expressed all along the digestive tract". Am. J. Physiol. Gastrointest. Liver Physiol. 288 (5): G933–42. doi:10.1152/ajpgi.00198.2004. PMID 15591162.
  • Forteza R, Salathe M, Miot F; et al. (2005). "Regulated hydrogen peroxide production by Duox in human airway epithelial cells". Am. J. Respir. Cell Mol. Biol. 32 (5): 462–9. doi:10.1165/rcmb.2004-0302OC. PMID 15677770.
  • Ameziane-El-Hassani R, Morand S, Boucher JL; et al. (2005). "Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity". J. Biol. Chem. 280 (34): 30046–54. doi:10.1074/jbc.M500516200. PMID 15972824.

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