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

By Gunter Weiss, Victor R. Gordeuk, Chaim Hershko

This e-book summarizes the most up-tp-date learn at the anemia of continual sickness and identifies powerful diagnostic recommendations for this universal scientific condition-covering key subject matters concerning the layout and choice of healing techniques together with the remedy of the underlying affliction, the biology of erythropoietin and the law of erythropoiesis, the disturbance of iron homeostasis, and the complicated nature of the systemic inflammatory reaction.

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Of particular interest is the response of IRP2 to hypoxia. A decrease in oxygen tension or treatment of cells with cobalt (that mimics hypoxic conditions) lead to IRP2 stabilization (220) without activating IRP1 (221). Targeted Disruption of IRP1 or IRP2 The function of IRP1 and IRP2 in the body has been examined by gene targeting experiments. IRP1À=À mice lack any discernible phenotype (187). By contrast, IRP2À=À mice display aberrant iron homeostasis and accumulate iron in the intestinal mucosa and the central nervous system and, moreover, develop a progressive neurodegenerative disorder (222).

Interestingly, mice lacking expression of either b2-microglobulin (34–36) or classical MHC class I molecules (37) also develop iron overload. Additional disorders of hereditary iron overload include juvenile hemochromatosis (HH of type 2) (38), HH of types 3, 4, and 5 (26,39), neonatal hemochromatosis (40), African iron overload (41), aceruloplasminemia (42), hypotransferrinemia= atransferrinemia (39), and heme oxygenase 1 deficiency (39). The above disorders are rare or extremely rare, but studies on the underlying molecular mechanisms and the development of animal models (43) have provided and continue to provide valuable insights on the regulation of iron metabolism in the body.

A) The post-translational regulation of bifunctional IRP1 in response to iron, NO, and H2O2 is mediated by an iron–sulfur cluster switch. In iron-replete cells, IRP1 assembles a cubane 4Fe–4S cluster between domains 1–3 and 4. Iron starvation, NO, and H2O2 trigger the switch of 4Fe–4S– to apoIRP1, resulting in the conversion of cytosolic aconitase to IRE-binding protein. (b) Regulation of IRP2 at the level of protein stability. IRP2, which contains a 73 amino acid insertion within domain 1, is stable in iron-starved, hypoxic, or NOtreated cells.

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