Journal
NUTRIENTS
Volume 5, Issue 10, Pages 4022-4050Publisher
MDPI
DOI: 10.3390/nu5104022
Keywords
iron stores; ferritin; iron mobilization; lysosomes; proteasome; autophagy; DMT1; ferroportin; erythrocyte iron recycling; hepcidin; erythropoietin
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From the nutritional standpoint, several aspects of the biochemistry and physiology of iron are unique. In stark contrast to most other elements, most of the iron in mammals is in the blood attached to red blood cell hemoglobin and transporting oxygen to cells for oxidative phosphorylation and other purposes. Controlled and uncontrolled blood loss thus has a major impact on iron availability. Also, in contrast to most other nutrients, iron is poorly absorbed and poorly excreted. Moreover, amounts absorbed (similar to 1 mg/day in adults) are much less than the total iron (similar to 20 mg/day) cycling into and out of hemoglobin, involving bone marrow erythropoiesis and reticuloendothelial cell degradation of aged red cells. In the face of uncertainties in iron bioavailability, the mammalian organism has evolved a complex system to retain and store iron not immediately in use, and to make that iron available when and where it is needed. Iron is stored innocuously in the large hollow protein, ferritin, particularly in cells of the liver, spleen and bone marrow. Our current understanding of the molecular, cellular and physiological mechanisms by which this stored iron in ferritin is mobilized and distributedwithin the cell or to other organsis the subject of this review.
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