The following HTML text is provided to enhance online
readability. Many aspects of typography translate only awkwardly to HTML.
Please use the page image
as the authoritative form to ensure accuracy.
Dietary Reference Intakes for Vitamin A, Vitamin K, Arsenic, Boron, Chromium, Copper, Iodine, Iron, Manganese, Molybdenum, Nickel, Silicon, Vanadium, and Zinc
The median serum transferrin saturation was 26 to 30 percent for men and 21 to 24 percent for women (Appendix Table G-2). The median serum transferrin saturation was 21 percent for pregnant women and 22 percent for adolescent girls. These values exceed the cut-off value of 16 percent (Table 9-2).
Erythrocyte Protoporphyrin Concentration. Heme is formed in developing erythrocytes by the incorporation of iron into protoporphyrin IX by ferrochetalase. If there is insufficient iron for optimal hemoglobin synthesis, erythrocytes accumulate an excess of protoporphyrin, which remains in the cells for the duration of their lifespans (Cook, 1999). An increased erythrocyte protoporphyrin concentration in the blood therefore indicates that the erythrocytes matured at a time when the iron supply was suboptimal. The cut off concentration for erythrocyte protoporphyrin concentration is greater than 70 μg/dL of erythrocytes. Erythrocyte protoporphyrin concentration is again not specific for iron deficiency and is also associated with inadequate iron delivery to developing erythrocytes (e.g., anemia of chronic disease) or impaired heme synthesis (e.g., lead poisoning). In iron deficiency, zinc can be incorporated into protoporphyrin IX, resulting in the formation of zinc protoporphyrin (Braun, 1999). The zinc protoporphyrin:heme ratio is used as an indicator of impaired heme synthesis and is sensitive to an insufficient iron delivery to the erythrocyte (Braun, 1999).
Soluble Serum Transferrin Receptor Concentration. The surfaces of all cells express transferrin receptors in proportion to their requirement for iron. A truncated form of the extracellular component of the transferrin receptor is produced by proteolytic cleavage and released into the plasma in direct proportion to the number of receptors expressed on the surfaces of body tissues. As functional iron depletion occurs, more transferrin receptors appear on cell surfaces. The concentration of proteolytically cleaved extracellular domains, or soluble serum transferrin receptors (sTfR), rises in parallel. The magnitude of the increase is proportional to the functional iron deficit. The sTfR concentration appears to be a specific and sensitive indicator of early iron deficiency (Akesson et al., 1998; Cook et al., 1990). Furthermore, sTfR concentration is not affected by infectious, inflammatory, and neoplastic disorders (Ferguson et al., 1992). Because commercial assays for sTfR have become available only recently, there is a lack of data relating iron intake to sTfR concentration, as well as relating sTfR concentration to functional outcomes. This indicator may prove to be very useful in identifying