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Transferrin and transferrin receptors update

Free Radical Biology and Medicine, 2019
In vertebrates, transferrin (Tf) safely delivers iron through circulation to cells. Tf-bound iron is incorporated through Tf receptor (TfR) 1-mediated endocytosis. TfR1 can mediate cellular uptake of both Tf and H-ferritin, an iron storage protein. New World arenaviruses, which cause hemorrhagic fever, and Plasmodium vivax use TfR1 for entry into host ...
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Transferrin receptor 1

The International Journal of Biochemistry & Cell Biology, 2004
With the discovery that transferrin serves as the iron source for hemoglobin-synthesizing immature red blood cells came the demonstration that a cell surface receptor, now known as transferrin receptor 1, is required for iron delivery from transferrin to cells.
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Reticulocyte membrane transferrin receptors

Canadian Journal of Biochemistry, 1980
A membrane protein with specific transferrin binding activity has been isolated from rabbit reticulocytes. The isolation procedure involved the immunoprecipitation by antibody to transferrin of transferring–receptor complexes from reticulocyte membrane proteins which had been solubilized with nonionic detergent.
B, Ecarot-Charrier   +3 more
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Serum transferrin receptor

American Journal of Hematology, 2008
AbstractTransferrin receptors (TfRs) are the conventional pathway by which cells acquire iron for physiological requirements. Under iron‐deficient conditions there is an increased concentration of surface TfR, especially on bone marrow erythroid precursors, as a mechanism to sequester needed iron.
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Erythropoiesis and transferrin receptors

Current Opinion in Hematology, 2015
The type 1 transferrin receptor (TfR1) is well known as a key player in erythroid differentiation through its role in iron uptake. Recently, it has been demonstrated that TfR1 could also have signaling functions in erythroid cells. Moreover, the second transferrin receptor, TfR2, whose signaling functions in hepatic cells are well established, was ...
Ivan C, Moura   +3 more
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Diferric transferrin regulates transferrin receptor 2 protein stability

Blood, 2004
AbstractTransferrin receptor 2 (TfR2) is a type 2 transmembrane protein expressed in hepatocytes that binds iron-bound transferrin (Tf). Mutations in TfR2 cause one form of hereditary hemochromatosis, a disease in which excessive absorption of dietary iron can lead to liver cirrhosis, diabetes, arthritis, and heart failure. The function of TfR2 in iron
Martha B, Johnson, Caroline A, Enns
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Relationship between Soluble Transferrin Receptors in Serum and Membrane-Bound Transferrin Receptors

Acta Haematologica, 1998
The expression of transferrin receptors on the cell membrane of erythroblasts was analysed with flow cytometry in patients with different forms of anaemia. At the same time the concentration of soluble transferrin receptors (sTfRs) was analysed in serum. It was shown that only in iron deficiency a high concentration of sTfRs in serum could be explained
Kuiper -Kramer, PA   +5 more
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The transferrin receptor

Trends in Biochemical Sciences, 1982
Abstract The isolation and analysis of the transferrin receptor has been greatly aided by the use of monoclonal antibodies. The receptor is a disulphide-linked homo-dimer which spans the membrane and binds two molecules of transferrin. Controlling genes for this receptor in humans have been mapped to chromosome 3 using cell hybrids.
Roland Newman   +4 more
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Diffusion of transferrin receptor clusters

Biophysical Chemistry, 1998
Two dimensional motion of membrane receptors provides a mechanism for interaction among receptors in the plane of the membrane. In some cases the lateral diffusion leads to formation of clusters which may also be mobile. We have used image cross-correlation (ICCS) spectroscopy technique to measure the translational motion of transferrin receptors in ...
M, Srivastava, N O, Petersen
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Bacterial transferrin and lactoferrin receptors

Trends in Microbiology, 1996
Pathogenic members of the Neisseriaceae and Pasteurellaceae express outer-membrane receptor proteins involved in the direct assimilation of iron from the host glycoproteins transferrin and lactoferrin. The critical requirement of iron for growth suggests that this function is an important component of colonization and infection. A model describing this
S D, Gray-Owen, A B, Schryvers
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