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In human cells, the best-characterized iron-sensing mechanism is the result of post-transcriptional regulation of mRNA (the chemical instructions derived from DNA genes to make proteins). Sequences of mRNA called iron-responsive elements (IREs) are contained within the mRNA sequences that code for transferrin receptors and for ferritin.
The amino acids which bind the iron ion to the transferrin are identical for both lobes; two tyrosines, one histidine, and one aspartic acid. For the iron ion to bind, an anion is required, preferably carbonate (CO 2− 3). [18] [13] Transferrin also has a transferrin iron-bound receptor; it is a disulfide-linked homodimer. [16]
For people who require dialysis or have chronic kidney disease, iron should be given with erythropoietin, depending on some laboratory parameters such as ferritin and transferrin saturation. [ 11 ] Erythropoietin is also used to treat anemia in people, and cats and dogs, with chronic kidney disease who are not on dialysis (those in Stage 3 or 4 ...
Iron deficiency, or sideropenia, is the state in which a body lacks enough iron to supply its needs. Iron is present in all cells in the human body and has several vital functions, such as carrying oxygen to the tissues from the lungs as a key component of the hemoglobin protein, acting as a transport medium for electrons within the cells in the form of cytochromes, and facilitating oxygen ...
Human iron metabolism is the set of chemical reactions that maintain human homeostasis of iron at the systemic and cellular level. Iron is both necessary to the body and potentially toxic. Controlling iron levels in the body is a critically important part of many aspects of human health and disease.
The human body has protective mechanisms in place to prevent excess free ferric iron from circulating the body. When being transported throughout the body, iron is bound to an iron transporting protein called transferrin to prevent iron from being absorbed into different cells. [6] Any excess iron is stored as ferritin in the liver. [6]
It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with transferrin. [6] The HFE gene contains 7 exons spanning 12 kb. [7] The full-length transcript represents 6 exons. [8] HFE protein is composed of 343 amino acids. There are several components, in sequence ...
The existence of a receptor for transferrin iron uptake has been recognized since the late 1950s. [2] Earlier two transferrin receptors in humans, transferrin receptor 1 and transferrin receptor 2 had been characterized and until recently cellular iron uptake was believed to occur chiefly via these two well documented transferrin receptors ...
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