By Gunter Weiss, Victor R. Gordeuk, Chaim Hershko
This e-book summarizes the most up-tp-date study at the anemia of persistent disorder and identifies powerful diagnostic suggestions for this universal medical condition-covering key issues relating to the layout and choice of healing ideas together with the remedy of the underlying ailment, the biology of erythropoietin and the rules of erythropoiesis, the disturbance of iron homeostasis, and the complicated nature of the systemic inflammatory reaction.
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Additional resources for Anemia of Chronic Disease (Basic and Clinical Oncology)
Taken together, in these animal models, defects in DMT1 activity lead to iron deficiency and severe hypochromic microcytic anemia. Defective expression of hephaestin in hemizygous male sex-linked anemia (sla) mice is also associated with microcytic anemia due to inefficient iron delivery to the circulation (56). 12 Pantopoulos The important function of ceruloplasmin in body iron metabolism is evident by the severe iron overload associated with human aceruloplasminemia (61,62). This disorder is characterized by normal Tf saturation, poor response to venesection therapy due to ensuing anemia, iron loading of macrophages and, notably, iron deposition in the brain (42), which does not occur in other forms of hemochromatosis.
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. 10). A notable difference between IRP1 and IRP2 is that the latter contains a cysteine- and proline-rich insertion of 73 amino acids, embedded within domain 1, which is encoded by a unique exon.
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.
Anemia of Chronic Disease (Basic and Clinical Oncology) by Gunter Weiss, Victor R. Gordeuk, Chaim Hershko