How Does Anemia Affect Blood Glucose Levels – Multi-Omic Analysis of Small RNAs, Transcriptomes and Degradation in T. turgidum—Regulatory Networks of Grain Development and Abiotic Stress Response
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How Does Anemia Affect Blood Glucose Levels
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Diabetes, Anemia, And Iron Supplements: What To Know
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Anemia Symptoms You Shouldn’t Ignore
Lady Davis Institute of Medical Research, Jewish General Hospital and Department of Medicine, McGill University, Montreal, QC H3Y 1P3, Canada
Submission received: September 17, 2020 / Reviewed: October 7, 2020 / Accepted: October 16, 2020 / Published: October 21, 2020
(This article belongs to the Special Issue Transport, Cellular Uptake and Iron Metabolism: Molecular Aspects and Regulation in Health and Disease)
Iron is essential for energy metabolism, and conditions of iron deficiency or excess are harmful to organisms and cells. Therefore, the metabolism of iron and carbohydrates is strictly regulated. Serum iron and glucose levels are subject to hormonal regulation by hepcidin and insulin, respectively. Hepcidin is a peptide hormone derived from the liver that inactivates the iron exporter ferroportin in target cells, thereby limiting the release of iron into the bloodstream. Insulin is a protein hormone secreted from pancreatic β-cells that stimulates glucose uptake and metabolism through insulin receptor signaling. There is increasing evidence that systemic, but also cellular iron and glucose metabolic pathways are interconnected. This review article presents relevant data obtained mainly from mouse models and biochemical studies. Additionally, it discusses iron and glucose metabolism in the context of human disease.
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Iron is a transition metal with critical biological functions [1]. In mammals, most of the body’s iron is found in the hemoglobin of red blood cells and mediates oxygen transport. A large amount of iron is also found in the myoglobin of skeletal muscle cells. Other cell types require smaller quantities of iron for use by some metalloproteins. These include metabolic enzymes and oxidoreductases, which catalyze electron transfer reactions. The activity of mitochondrial aconitase, the enzyme that catalyzes the conversion of citrate to isocitrate in the tricarboxylic acid (TCA) cycle, depends on the 4Fe-4S cluster in its active site. Additionally, four of the five complexes in the mitochondrial electron transport chain contain hemoproteins (such as cytochromes) or iron-sulfur cluster proteins. Therefore, iron is essential for cellular energy metabolism.
Cell culture experiments show that iron deficiency inhibits not only mitochondrial aconitase, but also other enzymes of the TCA cycle such as citrate synthase, isocitrate dehydrogenase and succinate dehydrogenase [2]. This reduces the formation of NADH and ATP, and also reduces oxygen consumption in the electron transport chain. To compensate for the inhibition in respiration, iron-deficient cells increase glycolysis for ATP synthesis. Conversely, excess iron negatively affects mitochondrial function. Thus, excess iron in the diet of rats reduces oxidative phosphorylation in liver mitochondria and also promotes mitochondrial dysfunction due to oxidative stress [3]. This is consistent with the notion that although iron is an essential nutrient, it can also be a potent biohazard by promoting oxidative stress [4]. The iron face of Janus shows that a balanced iron metabolism is essential for health [5]. Mechanisms underlying the regulation of systemic and cellular iron metabolism are summarized below.
Developing erythroid cells in the bone marrow and most cells in other tissues obtain iron from transferrin, the plasma iron carrier [6]. Transferrin is mostly replenished by iron recycled from tissue macrophages, which phagocytose iron-rich red blood cells and degrade heme via HO-1 (heme oxygenase 1). The freed iron is then released into the bloodstream via the iron exporter ferroportin for reuse. Intestinal enterocytes absorb iron from dietary sources via DMT1 (divalent metal transporter 1), which is expressed at the apical site, and release it into the plasma at the basolateral site via ferroportin. Luminal iron is previously reduced from Fe
By ferrireductases, such as DCYTB (duodenal cytochrome B). Ferroportin, DMT1 and DCYTB are transcriptionally induced in iron-deficient enterocytes by HIF2α (hypoxia-inducible factor 2α) to stimulate iron absorption [7]. Under physiological conditions, the contribution of dietary iron to the pool of transferrin-bound plasma iron is small and mostly serves to compensate for nonspecific iron loss.
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The release of iron from cells is important for body iron homeostasis and is negatively regulated by hepcidin, a peptide hormone that inactivates ferroportin in macrophages, enterocytes and other target cells [8] (Figure 1). Circulating hepcidin is synthesized by hepatocytes in the liver; however, hepcidin is also produced locally in other tissues and appears to have critical cell-autonomous functions [ 9 , 10 , 11 ]. The HAMP gene encoding hepcidin is mainly induced in response to iron signals or inflammation [8]. Hepcidin deficiency causes an uncontrolled release of iron into the plasma, a gradual saturation of transferrin and the formation of redox-active transferrin unbound iron (NTBI). This is taken up by hepatocytes and other tissue parenchymal cells leading to systemic iron overload (hemochromatosis) [12]. On the other hand, the continuous inflammatory induction of hepcidin contributes to inflammatory anemia, the most frequent anemia among chronic patients [13].
Iron intake triggers hepcidin induction in response to increased iron saturation plasma transfer and BMP6 (bone morphogenetic protein 6) secretion from liver sinusoidal endothelial cells [14] (Figure 1). Endothelial cells also secrete BMP2, which is thought to regulate basal hepcidin expression. Binding of BMP6 or BMP2 to cell surface BMP receptors promotes regulatory SMAD1/5/8 phosphorylation, SMAD4 recruitment, and translocation of the complex to the nucleus for transcriptional activation of the HAMP promoter. HJV (hemojuvelin) is a BMP co-receptor and enhancer of iron signaling to hepcidin, and its disruption leads to severe hemochromatosis in humans and mice. HFE and TfR2 (transferrin receptor 2) may be additional factors, as their inactivation is associated with milder hemochromatosis. HFE physically interacts with TfR1 (transferrin receptor 1) [15], and this may affect its iron signaling function. Iron signaling to hepcidin is negatively regulated by matriptase-2, a serine protease encoded by the TMPRSS6 gene that operates by cleaving and inactivating HJV.
Induction of inflammation by hepcidin is mainly mediated by IL-6 [16]. Upon binding to its receptor, IL-6 triggers phosphorylation of STAT3 by JAK1/2 kinase. Phosphorylated STAT3 translocates to the nucleus for transcriptional HAMP induction. Experimental evidence suggests cooperation between BMP/SMAD and IL-6/STAT3 signaling. Therefore, pharmacological inhibition of the SMAD pathway [17, 18], or genetic inactivation of some of its components [19, 20] attenuates the inflammatory hepcidin response.
Cellular iron uptake involves binding of transferrin to TfR1 on the plasma membrane, which is followed by internalization of the complex via endocytosis, release of iron from acidic endosomes and exit to the cytosol via DMT1. Internal iron is used in mitochondria for the synthesis of heme and iron-sulfur clusters. Excess iron is either stored in the cytosol in ferritin, an iron storage protein, or exported from the cell via ferroportin. The expression of TfR1, ferritin and ferroportin is coordinately regulated by post-transcriptional mechanisms. In iron-deficient cells, iron regulatory proteins (IRP1 and IRP2) interact with iron response elements (IREs) in the untranslated region of tfR1, ferritin and ferroportin [21]. The RNA/protein complex promotes stabilization of TfR1 and translational repression of ferritin and ferroportin mRNA, leading to enhanced iron acquisition for metabolic purposes. Increased intracellular iron triggers inactivation of IRP1 and IRP2 for IRE binding, allowing degradation of TfR1 mRNA and synthesis of ferritin and ferroportin. This response prevents excessive accumulation of unprotected iron in cells. The IRE/IRP system also contributes to the regulation of further proteins linked directly or indirectly to iron metabolism such as DMT1, the heme biosynthetic enzyme ALAS2 (aminolevulinic acid synthase 2), mitochondrial aconitase, or the transcription factor HIF2α.
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Although IRP1 and IRP2 share extensive similarities, they are regulated differently. Thus, iron converts IRP1 to cytosolic aconitase at the expense of its RNA binding activity via
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