Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells

American Journal of Physiology. Lung Cellular and Molecular Physiology
Jennifer TuriAndrew J Ghio

Abstract

Catalytically active iron in the lung causes oxidative stress and promotes microbial growth that can be limited by intracellular sequestration of iron within ferritin. Because cellular iron uptake requires membrane ferrireductase activity that in the gut can be provided by duodenal cytochrome b (Dcytb), we sought Dcytb in the lung to test the hypothesis that it contributes to epithelial iron regulation by reducing Fe(3+) for cellular iron transport. Dcytb expression was found in respiratory epithelium in vitro and in vivo and was responsive to iron concentration. 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. A definite source of reducing equivalents for Dcytb was sought but not identified. We found no evidence that ascorbate was involved but did demonstrate that O(2)(-). production decreased when Dcytb function was blocked. The presence of Dcytb in airway epithelial cells and its regulation by iron therefore may contribute to pulmonary cytoprotection.

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Citations

Jul 3, 2007·Biochemistry·Yury KamenskyGraham Palmer
Apr 22, 2009·Molecular BioSystems·Valerie HowerSuzy V Torti
Sep 4, 2010·Antioxidants & Redox Signaling·Domenico Del PrincipeMaria Valeria Catani
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Oct 29, 2013·Journal of Agricultural and Food Chemistry·Ravindranadh PalikaPullakhandam Raghu
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Sep 25, 2017·Metallomics : Integrated Biometal Science·F SchlottmannG O Latunde-Dada
Dec 5, 2018·Frontiers in Molecular Biosciences·Harry G ShermanFrankie J Rawson

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