Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 292-296 |
| Journal | International Journal of Biochemistry & Cell Biology |
| Volume | 35 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2003 |
Fingerprint
Cite this
}
Transferrin receptor 2: a new molecule in iron metabolism. / Trinder, Debbie; Baker, Erica.
In: International Journal of Biochemistry & Cell Biology, Vol. 35, No. 3, 2003, p. 292-296.Research output: Contribution to journal › Article
TY - JOUR
T1 - Transferrin receptor 2: a new molecule in iron metabolism
AU - Trinder, Debbie
AU - Baker, Erica
PY - 2003
Y1 - 2003
N2 - 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. (C) 2002 Elsevier Science Ltd. All rights reserved.
AB - 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. (C) 2002 Elsevier Science Ltd. All rights reserved.
U2 - 10.1016/S1357-2725(02)00258-3
DO - 10.1016/S1357-2725(02)00258-3
M3 - Article
VL - 35
SP - 292
EP - 296
JO - The International Journal of Biochemistry & Cell Biology
JF - The International Journal of Biochemistry & Cell Biology
SN - 1357-2725
IS - 3
ER -