Where is iron regulated




















Currently, it is known to involve the loss of alveolar surface area emphysema and airway inflammation bronchitis , primarily due to exposure to cigarette smoke CS. CS causes epithelial cell death, resulting in pulmonary emphysema. Moreover, CS induces iron accumulation in the mitochondria and cytosol, resulting in programmed cell death. Find articles by Nimesh Bhaskaran.

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The publisher's final edited version of this article is available at Science. See other articles in PMC that cite the published article. Abstract Eukaryotic cells require iron for survival and have developed regulatory mechanisms for maintaining appropriate intracellular iron concentrations.

Open in a separate window. Footnotes Supporting Online Material www. S1 to S8 Table S1 References. References and Notes 1. Rouault TA. EMBO J. Ishikawa H, et al. Yamanaka K, et al. Cell Biol. Wang J, et al. Cardozo T, Pagano M. Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells. Pinto J. Volke M. Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors.

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Ohgami R. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Richardson D. Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol. Levy J. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Trenor C. The molecular defect in hypotransferrinemic mice. Gunshin H. Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver.

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Duce J. Smith C. Iron transport and the kidney. Kozyraki R. Megalin-dependent cubilin-mediated endocytosis is a major pathway for the apical uptake of transferrin in polarized epithelia. Goetz D. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition.

Yang J. An iron delivery pathway mediated by a lipocalin. Mori K. Endocytic delivery of lipocalin—siderophore—iron complex rescues the kidney from ischemia-reperfusion injury.

Devireddy L. A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake. FEBS Lett. A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production.

Flo T. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Breuer W. The importance of non-transferrin bound iron in disorders of iron metabolism. Hider R. Nature of nontransferrin-bound iron. Huang H.

Is the iron donor lipocalin 2 implicated in the pathophysiology of hereditary hemochromatosis? Liuzzi J. Zip14 Slc39a14 mediates non-transferrin-bound iron uptake into cells. Zhao N. Chen T. TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis. Scara5 is a ferritin receptor mediating non-transferrin iron delivery. Binding and uptake of H-ferritin are mediated by human transferrin receptor Muhlenhoff U. Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron—sulfur cluster.

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Discovery of genes essential for heme biosynthesis through large-scale gene expression analysis. Johnson D. Structure, function, and formation of biological iron—sulfur clusters. Lill R. Function and biogenesis of iron—sulphur proteins. Human iron—sulfur cluster assembly, cellular iron homeostasis, and disease.

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Redox Signaling. Takagi H. Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? Mikhael M. Ferritin does not donate its iron for haem synthesis in macrophages. Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J. Specific iron chelators determine the route of ferritin degradation.

Ferreira C. Early embryonic lethality of H ferritin gene deletion in mice. Darshan D. Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage. Levi S. Neuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation. Best Pract. Mitochondrial ferritin. Cazzola M. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Cohen L. Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway.

Intracellular labile iron. Petrat F. The chelatable iron pool in living cells: a methodically defined quantity.

Rauen U. Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities. Epsztejn S. H-Ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties. Kaur D. Genetic or pharmacological iron chelation prevents MPTP-induced neurotoxicity in vivo : a novel therapy for Parkinson's disease.

Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease. Brain Res. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Recalcati S. Iron regulatory proteins: from molecular mechanisms to drug development. Wallander M. Molecular control of vertebrate iron homeostasis by iron regulatory proteins.

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Wingert R. Deficiency of glutaredoxin 5 reveals Fe—S clusters are required for vertebrate haem synthesis. Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts. Hubert N. Previously uncharacterized isoforms of divalent metal transporter DMT - 1: implications for regulation and cellular function.

Cloning and characterization of a mammalian protein-coupled metal-ion transporter. Zhang D. A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression.

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Tong W. Shi Y.



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