DUOX2

From Wikipedia, the free encyclopedia

Dual oxidase 2

Identifiers

DUOX2; LNOX2; NOXEF2; P138-TOX; THOX2

External IDs

OMIM: 606759 MGI: 3036280 HomoloGene: 9689

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 • response to virus • 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

Refseq

NM_014080 (mRNA)
NP_054799 (protein)

XM_619809 (mRNA)
XP_619809 (protein)

Location

Chr 15: 43.17 - 43.19 Mb

Chr 2: 121.97 - 121.99 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: DUOX2 dual oxidase 2.

[edit] 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.