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Cytochrome b reductase 1

Dcytb, CYBRD1
This gene is a member of the cytochrome b(561) family that encodes an iron-regulated protein. It highly expressed in the duodenal brush border membrane. It has ferric reductase activity and is believed to play a physiological role in dietary iron absorption. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: DMT1, Transferrin, Hepcidin, hephaestin, HFE
Papers on Dcytb
Prolyl hydroxylase inhibition corrects functional iron deficiency and inflammation-induced anaemia in rats.
Rabinowitz et al., San Diego, United States. In Br J Pharmacol, Aug 2015
KEY RESULTS: Oral administration of JNJ-42905343 to healthy rats increased the gene expression of cytochrome b (DcytB) and divalent metal-ion transporter 1 (DMT1) in the duodenum, and increased plasma EPO.
Duodenal cytochrome b (DCYTB) in iron metabolism: an update on function and regulation.
Richardson et al., Sydney, Australia. In Nutrients, Apr 2015
One member of this family; duodenal cytochrome b (DCYTB); may play an important role in ascorbate-dependent reduction of non-heme iron in the gut prior to uptake by ferrous-iron transporters.
Age-dependent expression of duodenal cytochrome b, divalent metal transporter 1, ferroportin 1, and hephaestin in the duodenum of rats.
Chang et al., Shijiazhuang, China. In J Gastroenterol Hepatol, Mar 2015
The expression of duodenal cytochrome b (DcytB), divalent metal transporter 1 (DMT1), ferroportin 1 (FPN1), hephaestin, and hepcidin were measured by real-time polymerase chain reaction or Western blot.
Iron and oxygen sensing: a tale of 2 interacting elements?
McKie et al., London, United Kingdom. In Metallomics, Feb 2015
In terms of responses to iron HIF2α is of major importance in key tissues such as the intestine where several iron transporters (Ferroportin, Dcytb) contain HREs within their promoters which bind HIF2α.
Studies on different iron source absorption by in situ ligated intestinal loops of broilers.
Liu et al., Harbin, China. In Biol Trace Elem Res, Feb 2015
Compared with inorganic iron groups, in which higher FeSO4 absorption than Fe2(SO4)3 was observed, supplementation with organic Fe glycine chelate significantly increased the Fe concentration in the duodenum and jejunum (P < 0.05), however, decreased DMT1 and DcytB messenger RNA (mRNA) levels (P < 0.05).
A nanoparticulate ferritin-core mimetic is well taken up by HuTu 80 duodenal cells and its absorption in mice is regulated by body iron.
Powell et al., London, United Kingdom. In J Nutr, 2014
Finally, we further probed the mechanism of cellular acquisition of nano Fe(III) by assessing ferritin formation, as a measure of Fe uptake and utilization, in HuTu 80 duodenal cancer cells with targeted inhibition of divalent metal transporter 1 (DMT1) and duodenal cytochrome b (DCYTB) before exposure to the supplemented iron sources.
Rice and Bean Targets for Biofortification Combined with High Carotenoid Content Crops Regulate Transcriptional Mechanisms Increasing Iron Bioavailability.
Martino et al., Viçosa, Brazil. In Nutrients, 2014
The evaluations included: hemoglobin gain, hemoglobin regeneration efficiency (HRE), gene expression of divalente metal transporter 1 (DMT-1), duodenal citocromo B (DcytB), ferroportin, hephaestin, transferrin and ferritin and total plasma antioxidant capacity (TAC).
Higher iron pearl millet (Pennisetum glaucum L.) provides more absorbable iron that is limited by increased polyphenolic content.
Glahn et al., Ithaca, United States. In Nutr J, 2014
DMT-1, DcytB, and ferroportin mRNA-expression was higher (P<0.05) and liver-ferritin was lower (P>0.05) in the Low-Fe group versus High-Fe group.
Duodenal cytochrome b (Cybrd 1) and HIF-2α expression during acute hypoxic exposure in mice.
McKie et al., London, United Kingdom. In Eur J Nutr, 2011
Increased iron absorption reported in early hypoxia could be accounted for in part by the enhancement of Dcytb expression by Hif-2alpha in the duodenum.
Intestinal ferritin H is required for an accurate control of iron absorption.
Kühn et al., Lausanne, Switzerland. In Cell Metab, 2010
As expected for iron-loaded animals, the ferritin H-deleted mice showed induced liver hepcidin mRNA levels and reduced duodenal expression of DMT1 and DcytB mRNA.
Intestinal hypoxia-inducible transcription factors are essential for iron absorption following iron deficiency.
Gonzalez et al., Bethesda, United States. In Cell Metab, 2009
Duodenal cytochrome b (DcytB) and divalent metal transporter 1 (DMT1) are regulators of iron absorption.
The role of Dcytb in iron metabolism: an update.
McKie, London, United Kingdom. In Biochem Soc Trans, 2008
Dcytb (duodenal cytochrome b) is an iron-regulated ferric reductase highly expressed in duodenal enterocytes.
Ascorbic acid--important for iron metabolism.
Tzatchev et al., Sofia, Bulgaria. In Folia Med (plovdiv), 2008
The increase of plasma ascorbate in human iron deficiency, especially in females in active age, could explain gender-related biological variation of plasma levels of vitamin C. The possible participation of ferric reductase activity Dcytb in transferrin cycle in liver and in neutrophil host defense implies new aspects of the role of vitamin C in the regulation of iron homeostasis.
Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro.
Sharp et al., London, United Kingdom. In Febs Lett, 2008
Dcytb plays a physiological role in both iron and copper uptake, through divalent metal transporter 1 (DMT1) and copper transporter 1, respectively.
Duodenal cytochrome B expression stimulates iron uptake by human intestinal epithelial cells.
McKie et al., London, United Kingdom. In J Nutr, 2008
The results of this study confirm that Dcytb can act as a ferric reductase that stimulates iron uptake in Caco-2 cells.
Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.
McKie et al., London, United Kingdom. In Biochim Biophys Acta, 2008
Functional characterization of Cybrd1 heme groups and iron/ascorbate metabolism.
Recombinant expression and initial characterization of the putative human enteric ferric reductase Dcytb.
Mauk et al., Vancouver, Canada. In Biochemistry, 2008
The current study concerns the recombinant expression, purification, and initial spectroscopic characterization of a recombinant form of the human ferric reductase.
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression.
Deng et al., Bethesda, United States. In Cell Metab, 2005
Transcript levels of genes involved in intestinal iron absorption, including Dcytb, DMT1, and ferroportin, are significantly elevated in the absence of hepcidin.
Structure/function overview of proteins involved in iron storage and transport.
Evans et al., London, United Kingdom. In Curr Med Chem, 2004
We review our current understanding of the intestinal absorption of iron in the light of recently identified membrane proteins, namely the ferrric reductase, Dcytb, the two iron(II) transport proteins, DMT1 and ferroportin/Ireg1, and hephaestin, the membrane-bound homologue of the ferroxidase ceruloplasmin.
An iron-regulated ferric reductase associated with the absorption of dietary iron.
Simpson et al., London, United Kingdom. In Science, 2001
We have isolated a complementary DNA, Dcytb (for duodenal cytochrome b), which encoded a putative plasma membrane di-heme protein in mouse duodenal mucosa.
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