DUOX1

From Wikipedia, the free encyclopedia

Dual oxidase 1

Identifiers

DUOX1; LNOX1; MGC138840; MGC138841; NOXEF1; THOX1

External IDs

OMIM: 606758 MGI: 2139422 HomoloGene: 68136

Gene ontology
Molecular Function:	• peroxidase activity • iron ion binding • calcium ion binding • NAD(P)H oxidase activity • oxidoreductase activity • FAD binding • NADP binding
Cellular Component:	• membrane • integral to membrane • apical plasma membrane
Biological Process:	• electron transport • cytokine and chemokine mediated signaling pathway • cuticle development • hormone biosynthetic process • superoxide release • hydrogen peroxide catabolic process • hydrogen peroxide biosynthetic process • response to cAMP

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_017434 (mRNA)
NP_059130 (protein)

XM_130483 (mRNA)
XP_130483 (protein)

Location

Chr 15: 43.21 - 43.25 Mb

n/a

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: DUOX1 dual oxidase 1.

[edit] 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.