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Erythroferrone is a protein hormone encoded in humans by the ERFE gene. Erythroferrone is produced by erythroblasts, inhibits the production of hepcidin in the liver, and so increases the amount of iron metabolism available for hemoglobin synthesis. Skeletal muscle secreted ERFE has been shown to maintain systemic metabolic homeostasis.
Seldin and his colleagues have written: "Myonectin is expressed and secreted predominantly by skeletal muscle.... (Our) results suggest that myonectin is a nutrient-responsive metabolic regulator secreted by skeletal muscle in response to changes in cellular energy state resulting from glucose or fatty acid fluxes. Many metabolically relevant secreted proteins (e.g. adiponectin, leptin, resistin, and RBP) and the signaling pathways they regulate in tissues are known to be dysregulated in the condition of obesity. The reduction in expression and circulating levels of myonectin in the obese state may represent yet another component of the complex metabolic circuitry dysregulated by excess caloric intake. Although exercise has long been known to have profound positive impacts on systemic insulin sensitivity and energy balance, the underlying mechanisms remain incompletely understood. That voluntary exercise dramatically increases the expression and circulating levels of myonectin to promote fatty acid uptake into cells may underlie one of the beneficial effects of physical exercise."Marcus M. Seldin, Jonathan M. Peterson, Mardi S. Byerly, Zhikui Wei, and G. William Wong. "Myonectin (CTRP15), a Novel Myokine That Links Skeletal Muscle to Systemic Lipid Homeostasis." THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 287, NO. 15, pp. 11968–11980, April 6, 2012, doi: 10.1074/jbc.M111.336834 originally published online February 17, 2012.
Myonectin was shown in 2015 to be identical to erythroferrone, a hormone produced in erythroblasts that is involved in iron metabolism.>
Its mechanism of action is to inhibit the expression of the liver hormone, hepcidin. This process is governed by the renal hormone, erythropoietin. By suppressing hepcidin, ERFE increases the function of the cellular iron export channel, ferroportin. This then results in increased iron absorption from the intestine and mobilization of iron from stores, which can then be used in the synthesis of hemoglobin in new red blood cells. Erythroferrone inhibits hepcidin synthesis by binding bone morphogenetic proteins and thereby inhibiting the bone morphogenetic protein pathway that controls hepcidin expression.
Mice deficient in the gene encoding erythroferrone have transient maturational hemoglobin deficits and impaired hepcidin suppression in response to phlebotomy with a delayed recovery from anemia.
In its role as myonectin, it also promotes lipid uptake into adipocytes and hepatocytes.
Erythroferrone levels in blood have been shown by immunoassay to be higher after blood loss or erythropoetin administration. Patients with beta-thalassemia have very high levels, and these decrease after blood transfusion.
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