Anemia of Chronic Disease (Basic and Clinical Oncology) by Gunter Weiss, Victor R. Gordeuk, Chaim Hershko

By Gunter Weiss, Victor R. Gordeuk, Chaim Hershko

This publication summarizes the most up-tp-date learn at the anemia of power sickness and identifies potent diagnostic suggestions for this universal scientific condition-covering key themes on the topic of the layout and choice of healing recommendations together with the therapy of the underlying disorder, the biology of erythropoietin and the rules of erythropoiesis, the disturbance of iron homeostasis, and the advanced nature of the systemic inflammatory reaction.

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IRON REGULATORY PROTEINS, IRP1 AND IRP2 IRP1 and IRP2 are cytoplasmic polypeptides of 889 and 964 amino acids, respectively (181,182). They are both members of the iron–sulfur cluster isomerase family and display high Regulation of Iron Metabolism 29 homology to m-aconitase (183). Human IRP1 shares 57% sequence identity and 75% similarity with human IRP2. In addition, human IRP1 is 31% identical and 56% similar to porcine m-aconitase. By analogy to the known structure of m-aconitase (184), IRP1 and IRP2 are projected to contain three compact domains, linked to a fourth domain by a flexible hinge region (Fig.

Ferrous iron is then transported across the intestinal mucosa by the divalent metal transporter 1 Figure 3 A model for dietary iron absorption in the duodenum. Ferric iron is reduced in the intestinal lumen by Dcytb. Ferrous iron is then transported across the apical membrane of mature enterocytes by DMT1. The mechanism for iron traffic within the enterocyte is completely unknown. The export of iron across the basolateral membrane of enterocytes to circulation is mediated by ferroportin. This step is coupled with reoxidation of ferrous to ferric iron by membrane-bound hephaestin.

10a). Three iron atoms co-ordinate to C437, C503, and C506 in the polypeptide backbone, while the fourth, Fea binds to the solvent (H2O) and is directly involved in catalysis (isomerization of citrate to isocitrate). Both c- and m-aconitases display similar catalytic efficiencies (195,196), but the physiological function of c-aconitase is unclear. Iron starvation promotes a slow disassembly of the 4Fe–4S cluster and the resulting apoIRP1 acquires IRE-binding activity. This may trigger a structural rearrangement leading to a more ‘‘open’’ cleft that 30 Pantopoulos Figure 10 Models for the regulation of IRP1 (a) and IRP2 (b), which, based on homology with mitochondrial aconitase, are depicted as proteins containing three compact domains (1–3) linked to a fourth (4) via a flexible hinge region.

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