Transferrin receptor 2: a new molecule in iron metabolism

Transferrin receptor 1 (TfR1) which mediates uptake of transferrin-bound iron, is essential for life in mammals. Recently, a close homologue of human transferrin receptor 1 was cloned and called transferrin receptor 2 (TfR2). A similar molecule has been identified in the mouse. Human transferrin rec...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 2003-03, Vol.35 (3), p.292-296
Main Authors: Trinder, Debbie, Baker, Erica
Format: Article
Language:English
Subjects:
Animals
cell cycle
CHO Cells
Cloning, Molecular
Cricetinae
erythroblasts
genes
hepatocytes
homeostasis
Humans
Hydrogen-Ion Concentration
Iron
Iron - metabolism
iron absorption
iron overload
Liver
Liver - metabolism
messenger RNA
Mice
Mutation
receptors
Receptors, Transferrin - metabolism
Receptors, Transferrin - physiology
RNA, Messenger - metabolism
transferrin
Transferrin receptor 1
Transferrin receptor 2
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Summary:Transferrin receptor 1 (TfR1) which mediates uptake of transferrin-bound iron, is essential for life in mammals. Recently, a close homologue of human transferrin receptor 1 was cloned and called transferrin receptor 2 (TfR2). A similar molecule has been identified in the mouse. Human transferrin receptor 2 is 45% identical with transferrin receptor 1 in the extracellular domain, but contains no iron responsive element in its mRNA and is apparently not regulated by intracellular iron concentration nor by interaction with HFE. Transferrin receptor 2, like transferrin receptor 1, binds transferrin in a pH-dependent manner (but with 25 times lower affinity) and delivers iron to cells. However, transferrin receptor 2 distribution differs from transferrin receptor 1, increasing in differentiating hepatocytes and decreasing in differentiating erythroblasts. Expression of both receptors is cell cycle dependent. Mutations in the human transferrin receptor 2 gene cause iron overload disease, suggesting it has a role in iron homeostasis.
ISSN:1357-2725
1878-5875
DOI:10.1016/S1357-2725(02)00258-3