IRON METABOLISM: THE REGULATION OF INTESTINAL ABSORPTION AND LIVER STORAGE.
Annual summary rept.,
NEW ENGLAND MEDICAL CENTER HOSPITALS BOSTON MASS
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Following the ingestion of hemoglobin the heme ring is taken up intact by the small intestinal epithelial cell. Within the cell the alpha-methene bridge is oxidized and the iron released from the heme ring. The heme-splitting reaction is the result of peroxides generated by the action of xanthene oxidase on its substrates. Transferrin is capable of enhancing the removal of Fe59 from an in vitro suspension of intestinal epithelial cell. This varies directly with the unsaturated iron binding capacity. Other chemical chelators of iron have no effect. Using Iodine-125 labelled transferrin, it has been shown that the molecule will specifically bind to the membrane of the epithelial cell. This suggests that transferrin plays an important role in regulating the transfer of iron from the cell to the plasma. Iron deficiency is a systemic disorder in which decreased hemoglobin production appears to be the major clinical finding. However, iron deficient red cells have also been shown to have an increase in autohemolysis and a decreased plasticity as measured by filtration through millipore filters. These findings help explain the shortened red blood cell survival noted in iron deficiency which is partially corrected by splenectomy. Author
- Anatomy and Physiology