DUOX1

Jump to navigation Jump to search


Dual oxidase 1
Identifiers
Symbols DUOX1 ; LNOX1; MGC138840; MGC138841; NOXEF1; THOX1
External IDs Template:OMIM5 Template:MGI HomoloGene68136
RNA expression pattern
PBB GE DUOX1 219597 s 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 1, also known as DUOX1, 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 DUOX2. This protein is known as dual oxidase because it has both a peroxidase homology domain and a gp91phox domain. Two alternatively spliced transcript variants encoding the same protein have been described for this gene.[1]

References

  1. 1.0 1.1 "Entrez Gene: DUOX1 dual oxidase 1".

Further reading

  • Lambeth JD (2002). "Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases". Curr. Opin. Hematol. 9 (1): 11–7. PMID 11753072.
  • 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.
  • 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.
  • 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.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Kalinina N, Agrotis A, Tararak E; et al. (2002). "Cytochrome b558-dependent NAD(P)H oxidase-phox units in smooth muscle and macrophages of atherosclerotic lesions". Arterioscler. Thromb. Vasc. Biol. 22 (12): 2037–43. PMID 12482831.
  • 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.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • 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.
  • 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.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • 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.
  • Shao MX, Nadel JA (2005). "Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells". Proc. Natl. Acad. Sci. U.S.A. 102 (3): 767–72. doi:10.1073/pnas.0408932102. PMID 15640347.
  • 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.
  • Harper RW, Xu C, Eiserich JP; et al. (2005). "Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium". FEBS Lett. 579 (21): 4911–7. doi:10.1016/j.febslet.2005.08.002. PMID 16111680.

Template:WikiDoc Sources