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Gene Review

CYBRD1  -  cytochrome b reductase 1

Homo sapiens

Synonyms: CYB561A2, Cytochrome b reductase 1, DCYTB, Duodenal cytochrome b, FLJ23462, ...
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Disease relevance of CYBRD1


High impact information on CYBRD1


Biological context of CYBRD1


Anatomical context of CYBRD1

  • Dcytb expression was found in other tissues apart from the duodenum and its regulation and functions at these other sites are of interest in iron metabolism [10].
  • Using Northern and Western blots, RT-PCR and confocal microscopy, we studied the expression and localisation of Dcytb in cell lines and tissues of CD1 mice [10].
  • Novel genes associated with iron uptake include Dcytb, a putative iron-regulated reductase and DMT1, a Fe(II) carrier in the brush border membrane [11].
  • RESULTS: Dcytb (duodenal ferric reductase) was expressed at very low levels in the large intestine, compared to the duodenum, while Ireg1 and DMT1 were expressed at significant levels in the large intestine and were increased in iron-deficient caecum, proximal and distal colon, with the most significant increases seen in the distal colon [12].
  • Dcytb expression was found in respiratory epithelium in vitro and in vivo and was responsive to iron concentration [9].

Associations of CYBRD1 with chemical compounds

  • Dcytb, the iron regulated ferric reductase may also utilize cytoplasmic ascorbate as electron donor for transmembrane reduction of iron [10].
  • Dcytb has been identified as the mammalian transplasma ferric reductase that catalyzes the reduction of ferric to ferrous iron in the process of iron absorption [10].
  • In this model, His48, an invariant residue in the cytochrome b reductase family, forms an interaction with the propionic acid group of the D-ring of the heme cofactor [6].
  • Iron transport was measured in human bronchial epithelial (HBE) cells using inductively coupled plasma atomic emission spectroscopy and was demonstrated to be partially inhibited in the presence of Dcytb-blocking antibody, suggesting that Dcytb reduces Fe(3+) for cellular iron transport [9].

Other interactions of CYBRD1


  1. Analysis of genes implicated in iron regulation in individuals presenting with primary iron overload. Zaahl, M.G., Merryweather-Clarke, A.T., Kotze, M.J., van der Merwe, S., Warnich, L., Robson, K.J. Hum. Genet. (2004) [Pubmed]
  2. Modulation of iron transport proteins in human colorectal carcinogenesis. Brookes, M.J., Hughes, S., Turner, F.E., Reynolds, G., Sharma, N., Ismail, T., Berx, G., McKie, A.T., Hotchin, N., Anderson, G.J., Iqbal, T., Tselepis, C. Gut (2006) [Pubmed]
  3. An iron-regulated ferric reductase associated with the absorption of dietary iron. McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F., Simpson, R.J. Science (2001) [Pubmed]
  4. Spectroscopic and kinetic characterization of the recombinant wild-type and C242S mutant of the cytochrome b reductase fragment of nitrate reductase. Ratnam, K., Shiraishi, N., Campbell, W.H., Hille, R. J. Biol. Chem. (1995) [Pubmed]
  5. Duodenal expression of iron transport molecules in untreated haemochromatosis subjects. Stuart, K.A., Anderson, G.J., Frazer, D.M., Powell, L.W., McCullen, M., Fletcher, L.M., Crawford, D.H. Gut (2003) [Pubmed]
  6. Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 A, its ADP complex and an active-site mutant and modeling of the cytochrome b domain. Lu, G., Lindqvist, Y., Schneider, G., Dwivedi, U., Campbell, W. J. Mol. Biol. (1995) [Pubmed]
  7. Duodenal Dcytb and hephaestin mRNA expression are not significantly modulated by variations in body iron homeostasis. Gleeson, F., Ryan, E., Barrett, S., Russell, J., Kelleher, B., Crowe, J. Blood Cells Mol. Dis. (2005) [Pubmed]
  8. Iron Imports. II. Iron uptake at the apical membrane in the intestine. Mackenzie, B., Garrick, M.D. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  9. Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells. Turi, J.L., Wang, X., McKie, A.T., Nozik-Grayck, E., Mamo, L.B., Crissman, K., Piantadosi, C.A., Ghio, A.J. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
  10. Molecular and functional roles of duodenal cytochrome B (Dcytb) in iron metabolism. Latunde-Dada, G.O., Van der Westhuizen, J., Vulpe, C.D., Anderson, G.J., Simpson, R.J., McKie, A.T. Blood Cells Mol. Dis. (2002) [Pubmed]
  11. Iron absorption: biochemical and molecular insights into the importance of iron species for intestinal uptake. Cremonesi, P., Acebron, A., Raja, K.B., Simpson, R.J. Pharmacol. Toxicol. (2002) [Pubmed]
  12. Expression of iron absorption genes in mouse large intestine. Takeuchi, K., Bjarnason, I., Laftah, A.H., Latunde-Dada, G.O., Simpson, R.J., McKie, A.T. Scand. J. Gastroenterol. (2005) [Pubmed]
  13. Molecular evidence for the role of a ferric reductase in iron transport. McKie, A.T., Latunde-Dada, G.O., Miret, S., McGregor, J.A., Anderson, G.J., Vulpe, C.D., Wrigglesworth, J.M., Simpson, R.J. Biochem. Soc. Trans. (2002) [Pubmed]
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