TAILIEUCHUNG - Chapter 098. Iron Deficiency and Other Hypoproliferative Anemias (Part 2)

Internal iron exchange. Normally about 80% of iron passing through the plasma transferrin pool is recycled from broken-down red cells. Absorption of about 1 mg/d is required from the diet in men, mg/d in women to maintain homeostasis. As long as transferrin saturation is maintained between 20–60% and erythropoiesis is not increased, iron stores are not required. However, in the event of blood loss, dietary iron deficiency, or inadequate iron absorption, up to 40 mg/d of iron can be mobilized from stores. RE, reticuloendothelial. The iron-transferrin complex circulates in the plasma until it interacts with specific transferrin receptors on the surface. | Chapter 098. Iron Deficiency and Other Hypoproliferative Anemias Part 2 Figure 98-1 ftwqp tf j-. - .n-te-fc-. Wt íc. R . L7th Edition httpi www. cce Copyright The McGrew-Hill Compenitl. inc. All rughtf t4í8 J cI. Exlravaseuiar excharwe Internal iron exchange. Normally about 80 of iron passing through the plasma transferrin pool is recycled from broken-down red cells. Absorption of about 1 mg d is required from the diet in men mg d in women to maintain homeostasis. As long as transferrin saturation is maintained between 20-60 and erythropoiesis is not increased iron stores are not required. However in the event of blood loss dietary iron deficiency or inadequate iron absorption up to 40 mg d of iron can be mobilized from stores. RE reticuloendothelial. The iron-transferrin complex circulates in the plasma until it interacts with specific transferrin receptors on the surface of marrow erythroid cells. Diferric transferrin has the highest affinity for transferrin receptors apotransferrin transferrin not carrying iron has very little affinity. While transferrin receptors are found on cells in many tissues within the body and all cells at some time during development will display transferrin receptors the cell having the greatest number of receptors 300 000 to 400 000 cell is the developing erythroblast. Once the iron-bearing transferrin interacts with its receptor the complex is internalized via clathrin-coated pits and transported to an acidic endosome where the iron is released at the low pH. The iron is then made available for heme synthesis while the transferrin-receptor complex is recycled to the surface of the cell where the bulk of the transferrin is released back into circulation and the transferrin receptor reanchors into the cell membrane. At this point a certain amount of the transferrin receptor protein may be released into circulation and can be measured as soluble transferrin receptor protein. Within the erythroid cell iron in excess .

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