TFRC

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TFRC

A gene on chromosome 3q29 that encodes transferrin receptor, a protein required for development of erythrocytes and the nervous system.
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E2-treated SKOV-3 showed slightly reduced intracellular labile iron content, reduced expression of hepcidin and significantly increased expression of TFR1 but not TFR2; FPN expression was overall similar to that of controls.
On the other hand, ferric-transferrin complex (holo-transferrin) in excess displaces the human hemochomatosis gene product (HFE) from TFR1 allowing it to bind to TFR2 to upregulate hepcidin synthesis [1,5].
Based on these findings, it was expected that E2-treated cells will tend to upregulate the expression of TFR1 and/or TFR2 as means of compensating for lost intracellular iron.
As shown in Figure 5A, the expression of TFR1 mRNA in cells treated with 10 and 20 nM E2 and cultured for 24 h was slightly lower than that in untreated cells.
iii) E2 treatment alters TFR1 and TFR2 expression (Figures 4 and 5), which enables treated cells to differentially respond to labile iron depletion.
Genetic and functional identification of some iron-related proteins OMIM# Gene Locus Function Hephaestin 300167 HEPH Xql l-ql2 Oxidizes Fe+2 to Fe+3 Hepcidin 606464 HAMP 19ql3 Induces internalization, ubiquitination and degradation of ferroportin via Janus kinase 2 Transferrin 190000 IT 3q21 Transports iron from enterocyte to cells Transferrin 190010 TFR1 3q29 Transports Tf receptor 1 through the cell (CD71) membrane Transferrin 604720 TFR2 7q22 Transports Tf receptor 2 through the cell membrane especially in hepatocytes STEAP3 609671 STEAP3 2ql4.
At the more neutral pH of the plasma, apotransferrin dissociates from TFR1 and is ready to take next shipment of iron.
On the other hand, if the IREs are in the 3' UTR of mRNA, as in the case of TFR-1, the binding of IRPs to multiple IREs in the 3' UTR of TFR1 leads to stabilization of TFR-1 mRNA by inhibiting its degradation by nuclease digestion (49).
As discussed above, under iron deficiency conditions, IRPs actively bind IREs and stabilize TFR1 mRNA and simultaneously decrease translation of ferritin mRNA, consequently increasing the uptake and availability of iron in the cell.
Similarly this protein is also known to complex with TFR1 (55).
The type 3 HH is caused by mutations in TFR2, a homologue of TFR1, with limited tissue distribution.
Amgard TFR1 is a durable, fiber-reactive phosphorus flame retardant for use with cellulosic fabrics.