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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.
TfR1 = transferrin receptor 1 in Human iron metabolism. TfR1 is a transmembrane glycoprotein composed of two disulfide-linked monomers joined by two disulfide bonds. Each monomer binds one holo-transferrin molecule creating an iron-Tf-TfR complex which enters the cell by endocytosis. [9]
Transferrin receptor 2 (TfR2) is a protein that in humans is encoded by the TFR2 gene. [ 5 ] [ 6 ] This protein is involved in the uptake of transferrin -bound iron into cells by endocytosis , although its role is minor compared to transferrin receptor 1 .
Iron import can occur via endocytosis of transferrin receptor 1 or via ferrous iron importers DMT1 and ZIP14, which require the activity of iron reductases such as STEAP2, SDR-2 and Dcytb. Intracellular iron can be stored in ferritin and used for protein biosynthesis, or to generate reactive oxygen species (ROS) and regulate transcription via ...
[1] Blood testing of the soluble transferrin receptor (sTfR) is used as a measure of functional iron status and the investigation of iron deficiency anemia. Ferritin, a routine investigation for anemia, is an acute-phase reactant, and may be elevated in states of inflammation, thereby falsely indicating that iron stores are adequate. [2]
And more transferrin receptors make it easier for the cell to bring in more iron from transferrin-iron complexes circulating outside the cell. But, as iron binds to more and more IRE-BPs, they change shape and unbind the transferrin receptor mRNA. The transferrin receptor mRNA is rapidly degraded without the IRE-BP attached to it. The cell ...
The protein encoded by this gene is an integral membrane protein that is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is thought that this protein functions to regulate circulating iron uptake by regulating the interaction of the transferrin receptor with transferrin. [6]
The CD nomenclature was proposed and established in the 1st International Workshop and Conference on Human Leukocyte Differentiation Antigens (HLDA), held in Paris in 1982. [4] [5] This system was intended for the classification of the many monoclonal antibodies (mAbs) generated by different laboratories around the world against epitopes on the surface molecules of leukocytes (white blood cells).