By Gunter Weiss, Victor R. Gordeuk, Chaim Hershko
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Extra resources for Anemia of Chronic Disease (Basic and Clinical Oncology)
These assemble to a symmetric shell-like ˚ , with a potential to store structure forming a cavity of $80 A up to 4500 Fe(III) ions in form of ferric oxy-hydroxide phosphate. Iron incorporation into ferritin requires a ferroxidase activity associated with H-subunits and a nucleation center associated with L-subunits. The composition of ferritin Hand L-subunits differs in various tissues. For example, H-ferritin is enriched in the heart, while L-ferritin predominates in the liver. Iron stored in ferritin can be mobilized during iron deficiency for metabolic needs, but the mechanism is incompletely characterized.
The hydroxylation of P402 and P564 is carried out by specific prolyl-4-hydroxylases, which are members of the family of 2-oxoglutarate-dependent oxygenases (6). The reaction has an absolute requirement for iron and depends on oxygen availability. ’’ IRON’S TOXICITY When present in excess, iron may turn into a potent biohazard. Iron’s toxicity is based on its ability to catalyze the 4 Pantopoulos generation of hydroxyl radicals (OH) in the presence of superoxide (O2À) and hydrogen peroxide (H2O2) (7), according to Fenton and Haber=Weiss chemistry (Fig.
The apoTf-TfR1 complex recycles on the cell surface, while Fe(III) is reduced to Fe(II) and transported across the endosomal membrane into the cytosol, where it is utilized for Figure 7 Schematic representation of the Tf–TfR cycle. Plasma diferric transferrin (Tf) binds to cell surface TfR (TfR1 or TfR2) and the Tf–TfR complex is internalized by endocytosis. Acidification of the endosome results in the release of ferric iron from Tf and reduction and subsequent transport of ferrous iron across the endosomal membrane by DMT1.