DOI: 10.1042/bst0361239. The role of Dcytb in iron metabolism: an update

The role of Dcytb in iron metabolism: an update

10.1042/bst0361239

Crossref journal-article

Portland Press Ltd.

Biochemical Society Transactions (288)

Abstract

Dcytb (duodenal cytochrome b) is an iron-regulated ferric reductase highly expressed in duodenal enterocytes. Its location and strong regulation by iron has indicated it plays an important role in iron absorption. Expression of Dcytb in cells (Caco-2 and MDCK) was found to increase both ferric reductase activity and stimulate uptake of 59Fe. An additional increase in cupric reductase activity was found in MDCK (Madin–Darby canine kidney) cells expressing Dcytb. Expression and purification of Dcytb in insect cells reveals that Dcytb is a di-haem protein and that the haems are reducible by ascorbate, indicating that ascorbate is the likely intracelluar electron donor. Studies underway in Dcytb-knockout mice reveal that Dcytb is the only iron-regulated ferric reductase in the duodenal mucosa and that loss of Dcytb affects iron absorption.

Bibliography

McKie, A. T. (2008). The role of Dcytb in iron metabolism: an update. Biochemical Society Transactions, 36(6), 1239â1241.

Authors 1

Andrew T. McKie (first)

References 21 Referenced 77

{'key': '2021111720401750600_B1', 'first-page': '2294', 'article-title': 'Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae', 'volume': '10', 'author': 'Dancis', 'year': '1990', 'journal-title': 'Mol. Cell. Biol.'} / Mol. Cell. Biol. / Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae by Dancis (1990)
10.1073/pnas.89.9.3869 / Proc. Natl. Acad. Sci. U.S.A. / Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron by Dancis (1992)
10.1038/17800 / Nature / A ferric-chelate reductase for iron uptake from soils by Robinson (1999)
10.1074/jbc.272.21.13786 / J. Biol. Chem. / The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator by Georgatsou (1997)
10.1074/jbc.270.1.128 / J. Biol. Chem. / Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae by Hassett (1995)
10.1126/science.1057206 / Science / An iron-regulated ferric reductase associated with the absorption of dietary iron by McKie (2001)
10.1074/jbc.M606543200 / J. Biol. Chem. / Human erythrocyte membranes contain a cytochrome b561 that may be involved in extracellular ascorbate recycling by Su (2006)
10.1016/S1570-9639(03)00242-5 / Biochim. Biophys. Acta / Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases by Vargas (2003)
10.1016/j.bbagen.2006.07.019 / Biochim. Biophys. Acta / An ascorbate-reducible cytochrome b561 is localized in macrophage lysosomes by Zhang (2006)
10.1038/ng1658 / Nat. Genet. / Identification of a ferrireductase required for efficient transferrindependent iron uptake in erythroid cells by Ohgami (2005)
10.1016/S1097-2765(00)80425-6 / Mol. Cell / A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation by McKie (2000)
10.1182/blood-2005-02-0716 / Blood / Cybrd1 (duodenal cytochrome b) is not necessary for dietary iron absorption in mice by Gunshin (2005)
10.1016/j.cmet.2006.08.009 / Cell Metab. / Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function by Nose (2006)
10.1093/jn/138.6.991 / J. Nutr. / Duodenal cytochrome b expression stimulates iron uptake by human intestinal epithelial cells by Latunde-Dada (2008)
10.1016/j.febslet.2008.05.010 / FEBS Lett. / Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro by Wyman (2008)
10.1111/j.1742-4658.2006.05381.x / FEBS J. / Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases by Su (2006)
10.1016/j.bbabio.2007.12.001 / Biochim. Biophys. Acta / Functional characterization of human duodenal cytochrome b (Cybrd1): redox properties in relation to iron and ascorbate metabolism by Oakhill (2008)
10.1074/jbc.272.37.23206 / J. Biol. Chem. / Existence of two heme B centers in cytochrome b561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy by Tsubaki (1997)
10.1016/j.abb.2005.09.006 / Arch. Biochem. Biophys. / Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561 by Berczi (2005)
Choi J.H. Latunde-Dada Y. Laftah A. McKie A.T. Simpson R.J. The role of DcytB in intestinal iron absorption 2008 http://www.biochemistry.org/meetings/abstracts/SA078/SA078P007.pdf(abstract)
10.1016/0005-2736(87)90255-0 / Biochim. Biophys. Acta / Comparison of 59Fe3+ uptake in vitro and in vivo by mouse duodenum by Raja (1987)

Dates

Type	When
Created	16 years, 9 months ago (Dec. 2, 2008, 12:27 p.m.)
Deposited	3 years, 9 months ago (Nov. 17, 2021, 7:58 p.m.)
Indexed	1 month ago (Aug. 3, 2025, 6:49 p.m.)
Issued	16 years, 9 months ago (Nov. 19, 2008)
Published	16 years, 9 months ago (Nov. 19, 2008)
Published Online	16 years, 9 months ago (Nov. 19, 2008)
Published Print	16 years, 9 months ago (Dec. 1, 2008)

Funders 0

None

BibTeX

@article{McKie_2008, title={The role of Dcytb in iron metabolism: an update}, volume={36}, ISSN={1470-8752}, url={http://dx.doi.org/10.1042/bst0361239}, DOI={10.1042/bst0361239}, number={6}, journal={Biochemical Society Transactions}, publisher={Portland Press Ltd.}, author={McKie, Andrew T.}, year={2008}, month=nov, pages={1239–1241} }

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